Difference between revisions of "Os03g0281900"

From RiceWiki
Jump to: navigation, search
Line 5: Line 5:
 
[[File: Shijc-Os03g0281900-Fig1.png|right|thumb|200px|'' rcn1-2 mutant (cv. Shiokari background) shows defect in the suberization in the hypodermis but not in the endodermis. (from reference <ref name="ref1" />).'']]
 
[[File: Shijc-Os03g0281900-Fig1.png|right|thumb|200px|'' rcn1-2 mutant (cv. Shiokari background) shows defect in the suberization in the hypodermis but not in the endodermis. (from reference <ref name="ref1" />).'']]
 
'''Role of hypodermal suberin under waterlogged conditions'''
 
'''Role of hypodermal suberin under waterlogged conditions'''
−
Rice is well adapted to waterlogged conditions. However, the rice mutant, rcn1 developed a short and shallow root system when growing in a rice paddy field or in deoxygenated stagnant nutrient solution (Figures 1 and S2). Waterlogging negatively affects the growth and survival of most plants, because oxygen is limited and phytotoxic compounds can accumulate in waterlogged soils <ref name="ref2" />. The apoplastic barrier in the hypodermis reduces soil and microbial toxins taken up into the roots from waterlogged soils <ref name="ref2" /> <ref name="ref3" />. Furthermore, the suberized barrier in the hypodermis may limit radial oxygen loss (ROL) from the aerenchyma in the roots to anaerobic (i.e. deep) soil <ref name="ref4" /> <ref name="ref5" /> <ref name="ref6" />. The rcn1 mutants had a well lignified sclerenchyma under stagnant deoxygenated conditions, but rcn1 lacked hypodermal suberization under aerated and stagnant deoxygenated conditions (Figures 3a, S3a and S4a). In a wetland plant, Phragmites australis, the penetration of periodic acid is stopped at the suberized hypodermis, but the apoplastic tracer easily penetrated the thickened and lignified cell walls at the sclerenchyma <ref name="ref3" />. In the wild types of rice grown in stagnant deoxygenated conditions, the apoplastic tracers (periodic acid and berberine) were unable to penetrate at the outside of the suberized hypodermis (Figures 5 and S6). But, rcn1 could not stop their penetration in the OPR even in the presence of a well lignified sclerenchyma (Figures 5 and S6). A sufficient suberized apoplastic transport barrier was not formed in the hypodermis of rcn1. This is one of the reasons why rcn1 could not develop roots longer than about 100 mm length in waterlogged soil or deoxygenated stagnant nutrient solution (Figures 1 and S2). Our results suggest that rice needs hypodermal suberization to act as an apoplastic barrier under wetland conditions.
+
Rice is well adapted to waterlogged conditions. However, the rice mutant, rcn1 developed a short and shallow root system when growing in a rice paddy field or in deoxygenated stagnant nutrient solution. Waterlogging negatively affects the growth and survival of most plants, because oxygen is limited and phytotoxic compounds can accumulate in waterlogged soils <ref name="ref2" />. The apoplastic barrier in the hypodermis reduces soil and microbial toxins taken up into the roots from waterlogged soils <ref name="ref2" /> <ref name="ref3" />. Furthermore, the suberized barrier in the hypodermis may limit radial oxygen loss (ROL) from the aerenchyma in the roots to anaerobic (i.e. deep) soil <ref name="ref4" /> <ref name="ref5" /> <ref name="ref6" />. The rcn1 mutants had a well lignified sclerenchyma under stagnant deoxygenated conditions, but rcn1 lacked hypodermal suberization under aerated and stagnant deoxygenated conditions. In a wetland plant, Phragmites australis, the penetration of periodic acid is stopped at the suberized hypodermis, but the apoplastic tracer easily penetrated the thickened and lignified cell walls at the sclerenchyma <ref name="ref3" />. In the wild types of rice grown in stagnant deoxygenated conditions, the apoplastic tracers (periodic acid and berberine) were unable to penetrate at the outside of the suberized hypodermis. But, rcn1 could not stop their penetration in the OPR even in the presence of a well lignified sclerenchyma. A sufficient suberized apoplastic transport barrier was not formed in the hypodermis of rcn1. This is one of the reasons why rcn1 could not develop roots longer than about 100 mm length in waterlogged soil or deoxygenated stagnant nutrient solution. Our results suggest that rice needs hypodermal suberization to act as an apoplastic barrier under wetland conditions.
−
Suberin of the rcn1 mutants and the wild types is composed of five aliphatic substance classes and two aromatic monomers (Figures 4 and S5). Suberin forms a barrier against water flow, and the aliphatic domain is thought to be more important than the aromatic domain for establishing the barrier <ref name="ref7"> <ref name="ref8">. Our results are consistent with this idea because the rcn1 mutants, which have a high level of aromatic monomers, could not block the penetration of apoplastic tracers (Figures 5 and S6).
+
Suberin of the rcn1 mutants and the wild types is composed of five aliphatic substance classes and two aromatic monomers. Suberin forms a barrier against water flow, and the aliphatic domain is thought to be more important than the aromatic domain for establishing the barrier <ref name="ref7"> <ref name="ref8">. Our results are consistent with this idea because the rcn1 mutants, which have a high level of aromatic monomers, could not block the penetration of apoplastic tracers.
−
On the other hand, some of the aliphatic suberin fractions were dramatically reduced in the rcn1 mutants compared with the wild type, especially under stagnant deoxygenated conditions (Figure 4 and S5). In rice, the chain lengths of aliphatic suberin monomers ranged from C16 to C30 <ref name="ref9"><ref name="ref10">, while the chain length in maize roots ranged only from C16 to C26 in rhizodermal and hypodermal cell walls <ref name="ref9">. In our results, chain lengths of aliphatic suberin ranged from C16 to C30 and chain lengths of C20 and C22 were less common than other lengths (Figure S7), as was previously reported for rice root suberin <ref name="ref9"><ref name="ref10">. The total contents of aliphatic suberin fraction and its monomers were significantly increased in rice (cv. Azucena) roots by stagnant deoxygenated treatments <ref name="ref10">, which is in agreement with the data for wild types in our results. There was a remarkable increase in the chain length of C28 and C30 monomers of aliphatic suberin (fatty acids and ω-OH fatty acids) in the wild types under stagnant deoxygenated conditions (Figures 4 and S5). In the rcn1 mutants, however, monomers with chain lengths of C28 and C30 in the OPR did not greatly increase under stagnant deoxygenated conditions (Figure S7). Chain lengths of C28 and C30 of aliphatic suberin are absent in Arabidopsis <ref name="ref11"> and maize <ref name="ref9">, which are non-wetland species. On the other hand, P. australis and Glyceria maxima, which are wetland species, develop a well suberized hypodermis in the roots and were able to form a barrier to ROL. Their roots accumulated significant amounts of monomers with chain lengths between C28 and C30 <ref name="ref3" />. Further studies are needed to understand the correlation between waterlogging tolerance and accumulation of the chain lengths of C28 and C30 of aliphatic suberin.
+
On the other hand, some of the aliphatic suberin fractions were dramatically reduced in the rcn1 mutants compared with the wild type, especially under stagnant deoxygenated conditions. In rice, the chain lengths of aliphatic suberin monomers ranged from C16 to C30 <ref name="ref9"><ref name="ref10">, while the chain length in maize roots ranged only from C16 to C26 in rhizodermal and hypodermal cell walls <ref name="ref9">. In our results, chain lengths of aliphatic suberin ranged from C16 to C30 and chain lengths of C20 and C22 were less common than other lengths, as was previously reported for rice root suberin <ref name="ref9"><ref name="ref10">. The total contents of aliphatic suberin fraction and its monomers were significantly increased in rice (cv. Azucena) roots by stagnant deoxygenated treatments <ref name="ref10">, which is in agreement with the data for wild types in our results. There was a remarkable increase in the chain length of C28 and C30 monomers of aliphatic suberin (fatty acids and ω-OH fatty acids) in the wild types under stagnant deoxygenated conditions. In the rcn1 mutants, however, monomers with chain lengths of C28 and C30 in the OPR did not greatly increase under stagnant deoxygenated conditions. Chain lengths of C28 and C30 of aliphatic suberin are absent in Arabidopsis <ref name="ref11"> and maize <ref name="ref9">, which are non-wetland species. On the other hand, P. australis and Glyceria maxima, which are wetland species, develop a well suberized hypodermis in the roots and were able to form a barrier to ROL. Their roots accumulated significant amounts of monomers with chain lengths between C28 and C30 <ref name="ref3" />. Further studies are needed to understand the correlation between waterlogging tolerance and accumulation of the chain lengths of C28 and C30 of aliphatic suberin.
  
 
[[File: Shijc-Os03g0281900-Fig2.png|right|thumb|200px|'' rcn1-2 (cv. Shiokari background) mutant shows reduced aliphatic suberin monomer contents. (from reference <ref name="ref1" />).'']]
 
[[File: Shijc-Os03g0281900-Fig2.png|right|thumb|200px|'' rcn1-2 (cv. Shiokari background) mutant shows reduced aliphatic suberin monomer contents. (from reference <ref name="ref1" />).'']]
 
'''RCN1/OsABCG5 is involved in hypodermal suberization'''
 
'''RCN1/OsABCG5 is involved in hypodermal suberization'''
−
Suberin monomers are thought to be transported to their extracellular destination in the apoplast by a vesicular pathway and/or export by ABC transporters localized in the plasma membrane <ref name="ref5" /><ref name="ref12" /><ref name="ref13" />. The structure of suberin is close to the structure of cutin, which form a cuticular layer that covers all plant aerial surfaces. Thus, the biosynthesis of suberin may be similar to the biosynthesis of cutin and associated waxes <ref name="ref12" />. So far, two Arabidopsis WBC/WHITE-subgroup ABC transporters, AtABCG11 and AtABCG12, which are localized in the plasma membrane, have been implicated in the formation of cuticular waxes <ref name="ref14" /><ref name="ref15" /><ref name="ref16" /><ref name="ref17" />. In barley, HvABCG31 (a full-size ABCG transporter) is also involved in cutin formation <ref name="ref18" />. Additionally, its rice ortholog OsABCG31 may affect cutin formation, although the cutin contents of osabcg31 have not been reported <ref name="ref18" /> <ref name="ref11"> reported that an AtABCG11-silenced line (dso-4) has reduced suberin contents in the root as well as reduced cutin and wax (i.e. an ABC transporter affects suberin accumulation in roots). They suggested that the reduced suberin in dso-4 results from the perturbation of cutin and/or wax transport because suberin and cutin share common precursors. dso-4 clearly suppressed the expressions of suberin-related genes, e.g. 3-KETOACYL-COA SYNTHASE2 (KCS2/DAISY) and CYP86A1 <ref name="ref11">. However, the authors suggested that AtABCG11 does not regulate suberin biosynthesis directly because AtABCG11 was expressed in lateral root primordia, developing lateral roots and root tips, but not in the endodermis in the root <ref name="ref17" />. By contrast, RCN1/OsABCG5 expression was associated with suberized cells in roots (i.e. the endodermis and hypodermis) (Figure 2). Furthermore, hypodermal suberization declined in both of the rcn1 mutants (Figures 3, S3 and S4). These results support our hypothesis that RCN1/OsABCG5 is directly involved in suberin formation in the hypodermis.
+
Suberin monomers are thought to be transported to their extracellular destination in the apoplast by a vesicular pathway and/or export by ABC transporters localized in the plasma membrane <ref name="ref5" /><ref name="ref12" /><ref name="ref13" />. The structure of suberin is close to the structure of cutin, which form a cuticular layer that covers all plant aerial surfaces. Thus, the biosynthesis of suberin may be similar to the biosynthesis of cutin and associated waxes <ref name="ref12" />. So far, two Arabidopsis WBC/WHITE-subgroup ABC transporters, AtABCG11 and AtABCG12, which are localized in the plasma membrane, have been implicated in the formation of cuticular waxes <ref name="ref14" /><ref name="ref15" /><ref name="ref16" /><ref name="ref17" />. In barley, HvABCG31 (a full-size ABCG transporter) is also involved in cutin formation <ref name="ref18" />. Additionally, its rice ortholog OsABCG31 may affect cutin formation, although the cutin contents of osabcg31 have not been reported <ref name="ref18" /> <ref name="ref11"> reported that an AtABCG11-silenced line (dso-4) has reduced suberin contents in the root as well as reduced cutin and wax (i.e. an ABC transporter affects suberin accumulation in roots). They suggested that the reduced suberin in dso-4 results from the perturbation of cutin and/or wax transport because suberin and cutin share common precursors. dso-4 clearly suppressed the expressions of suberin-related genes, e.g. 3-KETOACYL-COA SYNTHASE2 (KCS2/DAISY) and CYP86A1 <ref name="ref11">. However, the authors suggested that AtABCG11 does not regulate suberin biosynthesis directly because AtABCG11 was expressed in lateral root primordia, developing lateral roots and root tips, but not in the endodermis in the root <ref name="ref17" />. By contrast, RCN1/OsABCG5 expression was associated with suberized cells in roots (i.e. the endodermis and hypodermis). Furthermore, hypodermal suberization declined in both of the rcn1 mutants. These results support our hypothesis that RCN1/OsABCG5 is directly involved in suberin formation in the hypodermis.
 
Some suberin components were less abundant in the rcn1 mutants than in the wild types. When a transporter exports a substance to the apoplast, the loss-of-function mutant of its transporter reduced the substance in the apoplast compared with the wild type. In the present study, the OPR in both of rcn1 mutants had significantly reduced amounts of very-long-chain fatty acids (≥C28) of suberin main monomers (i.e. fatty acids and ω-OH fatty acids) and diacids of C16 than the wild types. This suggests that RCN1/OsABCG5 exports very-long-chain fatty acids of suberin monomers and/or diacids to the apoplast in the hypodermis. On the other hand, some suberin components were more abundant in the rcn1 mutants than in the wild types. These accumulations may be secondary effects of the reduction of the contents of very long chains of aliphatic suberin monomers in the hypodermis.
 
Some suberin components were less abundant in the rcn1 mutants than in the wild types. When a transporter exports a substance to the apoplast, the loss-of-function mutant of its transporter reduced the substance in the apoplast compared with the wild type. In the present study, the OPR in both of rcn1 mutants had significantly reduced amounts of very-long-chain fatty acids (≥C28) of suberin main monomers (i.e. fatty acids and ω-OH fatty acids) and diacids of C16 than the wild types. This suggests that RCN1/OsABCG5 exports very-long-chain fatty acids of suberin monomers and/or diacids to the apoplast in the hypodermis. On the other hand, some suberin components were more abundant in the rcn1 mutants than in the wild types. These accumulations may be secondary effects of the reduction of the contents of very long chains of aliphatic suberin monomers in the hypodermis.
−
In rice, the endodermis is also well suberized. The RCN1/OsABCG5 gene was expressed not only in the hypodermis but also in the endodermis under stagnant deoxygenated conditions (Figure 2e,f). However, in rcn1, very-long-chain fatty acids (≥C28) of suberin main monomers were reduced in the hypodermis but not in the endodermis (Figures 4b and S5b). Under waterlogged soil and stagnant deoxygenated conditions, the rcn1 mutants clearly lacked suberization at the hypodermis (Figures 3, S3 and S4) and had noticeably abnormal root systems (Figures 1 and S2). The rcn1 mutants were originally isolated by their smaller number of culms <ref name="ref19" />. However, stagnant deoxygenated treatments did not change the culm (i.e. tiller) number of rcn1 mutants (Figure S8). The reduced number of culms (tillers) in rcn1 mutants may be caused by a mechanism that differs from the mechanism of suberization in the hypodermis. Because RCN1/OsABCG5 belongs to the half-size WBC/WHITE subgroup of ABCG proteins <ref name="ref19" />, it is thought to form a homo-dimer or hetero-dimer to function as a transporter to mediate the movement of substrates across the membrane. Some human ABCG proteins function as homo-dimers, although their substrate and their localization can be altered when they form hetero-dimers with other subfamily members <ref name="ref20" /> <ref name="ref21" /> <ref name="ref22" />. RCN1/OsABCG5 might function with a different partner in the hypodermis and endodermis under waterlogged conditions, and also in developing tillers. Further studies are needed to test this hypothesis.  
+
In rice, the endodermis is also well suberized. The RCN1/OsABCG5 gene was expressed not only in the hypodermis but also in the endodermis under stagnant deoxygenated conditions. However, in rcn1, very-long-chain fatty acids (≥C28) of suberin main monomers were reduced in the hypodermis but not in the endodermis. Under waterlogged soil and stagnant deoxygenated conditions, the rcn1 mutants clearly lacked suberization at the hypodermis and had noticeably abnormal root systems. The rcn1 mutants were originally isolated by their smaller number of culms <ref name="ref19" />. However, stagnant deoxygenated treatments did not change the culm (i.e. tiller) number of rcn1 mutants. The reduced number of culms (tillers) in rcn1 mutants may be caused by a mechanism that differs from the mechanism of suberization in the hypodermis. Because RCN1/OsABCG5 belongs to the half-size WBC/WHITE subgroup of ABCG proteins <ref name="ref19" />, it is thought to form a homo-dimer or hetero-dimer to function as a transporter to mediate the movement of substrates across the membrane. Some human ABCG proteins function as homo-dimers, although their substrate and their localization can be altered when they form hetero-dimers with other subfamily members <ref name="ref20" /> <ref name="ref21" /> <ref name="ref22" />. RCN1/OsABCG5 might function with a different partner in the hypodermis and endodermis under waterlogged conditions, and also in developing tillers. Further studies are needed to test this hypothesis.  
  
 
===Mutation===
 
===Mutation===
 
[[File: Shijc-Os03g0281900-Fig3.png|right|thumb|200px|'' A rice mutant, reduced culm number1 (rcn1), cannot develop long roots under waterlogged soil conditions or stagnant deoxygenated conditions. (from reference <ref name="ref1" />).'']]
 
[[File: Shijc-Os03g0281900-Fig3.png|right|thumb|200px|'' A rice mutant, reduced culm number1 (rcn1), cannot develop long roots under waterlogged soil conditions or stagnant deoxygenated conditions. (from reference <ref name="ref1" />).'']]
−
two allelic lines of the rice rcn1 mutants, reduced culm number1-1 (rcn1-1, whose background cultivar is ‘Akamuro’) and rcn1-2 (whose background cultivar is ‘Shiokari’), showed a reduced tillering phenotype <ref name="ref19" />. rcn1-1 and rcn1-2 had single point mutations in the RCN1/OsABCG5 gene (LOC_Os03g17350), causing amino acid substitutions R488C and A684P, respectively (Figure S1) <ref name="ref19" />. In waterlogged soil conditions, the roots of rcn1-1 and rcn1-2 were shorter (maximum root length was about 100 mm), and less flexible than those of the wild type (the roots did not droop when the plant was held in the air) (Figures 1a and S2b). This phenotype was more severe in rcn1-2 (Figure S2). rcn1-1 and rcn1-2 also developed short and inflexible roots when grown in stagnant deoxygenated nutrient solution, which mimics waterlogged soil conditions (Figures 1b and S2d). In stagnant deoxygenated conditions, the roots of rcn1 mutants were brownish compared with those of the wild type (white roots) (Figures 1b and S2d). The abnormal root phenotypes were not observed when the mutants were grown under well drained soil conditions (Figure S2a) or in well-aerated nutrient solution (Figure S2c), suggesting that the mutations in the RCN1/OsABCG5 gene affected root morphology under hypoxic conditions, but not under aerobic conditions. The rcn1-1 roots were completely recovered by introduction of a wild-type RCN1/OsABCG5 gene, but not by introduction of empty vector plasmid (without RCN1/OsABCG5 gene) (Figure 1b). Together, these results suggest that RCN1/OsABCG5 plays an important role in root growth in a hypoxia-specific manner.
+
two allelic lines of the rice rcn1 mutants, reduced culm number1-1 (rcn1-1, whose background cultivar is ‘Akamuro’) and rcn1-2 (whose background cultivar is ‘Shiokari’), showed a reduced tillering phenotype <ref name="ref19" />. rcn1-1 and rcn1-2 had single point mutations in the RCN1/OsABCG5 gene (LOC_Os03g17350), causing amino acid substitutions R488C and A684P, respectively <ref name="ref19" />. In waterlogged soil conditions, the roots of rcn1-1 and rcn1-2 were shorter (maximum root length was about 100 mm), and less flexible than those of the wild type (the roots did not droop when the plant was held in the air). This phenotype was more severe in rcn1-2. rcn1-1 and rcn1-2 also developed short and inflexible roots when grown in stagnant deoxygenated nutrient solution, which mimics waterlogged soil conditions. In stagnant deoxygenated conditions, the roots of rcn1 mutants were brownish compared with those of the wild type (white roots). The abnormal root phenotypes were not observed when the mutants were grown under well drained soil conditions or in well-aerated nutrient solution, suggesting that the mutations in the RCN1/OsABCG5 gene affected root morphology under hypoxic conditions, but not under aerobic conditions. The rcn1-1 roots were completely recovered by introduction of a wild-type RCN1/OsABCG5 gene, but not by introduction of empty vector plasmid (without RCN1/OsABCG5 gene). Together, these results suggest that RCN1/OsABCG5 plays an important role in root growth in a hypoxia-specific manner.
  
 
===Expression===
 
===Expression===
 
[[File: Shijc-Os03g0281900-Fig4.png|right|thumb|200px|'' RCN1/OsABCG5 is expressed in the hypodermis as well as the endodermis in roots. (from reference <ref name="ref1" />).'']]
 
[[File: Shijc-Os03g0281900-Fig4.png|right|thumb|200px|'' RCN1/OsABCG5 is expressed in the hypodermis as well as the endodermis in roots. (from reference <ref name="ref1" />).'']]
−
RCN1/OsABCG5 gene expression was analyzed in the wild type (cv. Shiokari) by quantitative RT-PCR in three different zones (zone I: 0–15 mm behind the root apex, zone II: 15–25 mm behind the root apex, and zone III: 50–70 mm behind the root apex) (Figure 2a) of roots grown in aerated or stagnant deoxygenated nutrient solution. In all of the zones (I, II and III) of wild-type roots, RCN1/OsABCG5 expression was 4- to 187-times greater under stagnant deoxygenated conditions than under aerated conditions (Figure 2b). In particular, RCN1/OsABCG5 was highly expressed in zone II under stagnant deoxygenated conditions (Figure 2b).
+
RCN1/OsABCG5 gene expression was analyzed in the wild type (cv. Shiokari) by quantitative RT-PCR in three different zones (zone I: 0–15 mm behind the root apex, zone II: 15–25 mm behind the root apex, and zone III: 50–70 mm behind the root apex of roots grown in aerated or stagnant deoxygenated nutrient solution. In all of the zones (I, II and III) of wild-type roots, RCN1/OsABCG5 expression was 4- to 187-times greater under stagnant deoxygenated conditions than under aerated conditions. In particular, RCN1/OsABCG5 was highly expressed in zone II under stagnant deoxygenated conditions.
−
To determine whether RCN1/OsABCG5 expression in roots is specific to a cell type or to a tissue. RCN1/OsABCG5 expression was enhanced by stagnant deoxygenated treatment in all CC, CP and OPR tissues (Figure 2c). The transcript levels were especially high in OPR and CC under stagnant deoxygenated conditions (Figure 2c).
+
To determine whether RCN1/OsABCG5 expression in roots is specific to a cell type or to a tissue. RCN1/OsABCG5 expression was enhanced by stagnant deoxygenated treatment in all CC, CP and OPR tissues. The transcript levels were especially high in OPR and CC under stagnant deoxygenated conditions.
−
To confirm these results, GUS activity in RCN1/OsABCG5Pro::GFP:GUS plants was observed. GUS activity was high in zone II of roots grown under stagnant deoxygenated conditions (Figure 2d). Moreover, GUS activity was observed in the hypodermis (Figure 2e) and the endodermis (Figure 2f) of zone II in RCN1/OsABCG5Pro::GFP:GUS plants grown under stagnant conditions. These results suggest that RCN1/OsABCG5 was expressed specifically in the hypodermis as well as in the endodermis in rice roots under stagnant deoxygenated conditions (waterlogged conditions). Additionally, GFP-tagged RCN1/OsABCG5 was localized in the plasma membrane of hypodermal cells (Figure 2g,h), suggesting that RCN1/OsABCG5 works as an ABC transporter at the plasma membrane.
+
To confirm these results, GUS activity in RCN1/OsABCG5Pro::GFP:GUS plants was observed. GUS activity was high in zone II of roots grown under stagnant deoxygenated conditions. Moreover, GUS activity was observed in the hypodermis and the endodermis of zone II in RCN1/OsABCG5Pro::GFP:GUS plants grown under stagnant conditions. These results suggest that RCN1/OsABCG5 was expressed specifically in the hypodermis as well as in the endodermis in rice roots under stagnant deoxygenated conditions (waterlogged conditions). Additionally, GFP-tagged RCN1/OsABCG5 was localized in the plasma membrane of hypodermal cells, suggesting that RCN1/OsABCG5 works as an ABC transporter at the plasma membrane.
  
 
==Labs working on this gene==
 
==Labs working on this gene==

Revision as of 13:40, 27 December 2014

RCN1/OsABCG5, an ATP-binding cassette (ABC) transporter, is required for hypodermal suberization of roots in rice. [1]

Annotated Information

Function

rcn1-2 mutant (cv. Shiokari background) shows defect in the suberization in the hypodermis but not in the endodermis. (from reference [1]).

Role of hypodermal suberin under waterlogged conditions Rice is well adapted to waterlogged conditions. However, the rice mutant, rcn1 developed a short and shallow root system when growing in a rice paddy field or in deoxygenated stagnant nutrient solution. Waterlogging negatively affects the growth and survival of most plants, because oxygen is limited and phytotoxic compounds can accumulate in waterlogged soils [2]. The apoplastic barrier in the hypodermis reduces soil and microbial toxins taken up into the roots from waterlogged soils [2] [3]. Furthermore, the suberized barrier in the hypodermis may limit radial oxygen loss (ROL) from the aerenchyma in the roots to anaerobic (i.e. deep) soil [4] [5] [6]. The rcn1 mutants had a well lignified sclerenchyma under stagnant deoxygenated conditions, but rcn1 lacked hypodermal suberization under aerated and stagnant deoxygenated conditions. In a wetland plant, Phragmites australis, the penetration of periodic acid is stopped at the suberized hypodermis, but the apoplastic tracer easily penetrated the thickened and lignified cell walls at the sclerenchyma [3]. In the wild types of rice grown in stagnant deoxygenated conditions, the apoplastic tracers (periodic acid and berberine) were unable to penetrate at the outside of the suberized hypodermis. But, rcn1 could not stop their penetration in the OPR even in the presence of a well lignified sclerenchyma. A sufficient suberized apoplastic transport barrier was not formed in the hypodermis of rcn1. This is one of the reasons why rcn1 could not develop roots longer than about 100 mm length in waterlogged soil or deoxygenated stagnant nutrient solution. Our results suggest that rice needs hypodermal suberization to act as an apoplastic barrier under wetland conditions. Suberin of the rcn1 mutants and the wild types is composed of five aliphatic substance classes and two aromatic monomers. Suberin forms a barrier against water flow, and the aliphatic domain is thought to be more important than the aromatic domain for establishing the barrier Cite error: Closing </ref> missing for <ref> tag [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] </references>

Structured Information

Gene Name

Os03g0281900

Description

ABC transporter related domain containing protein

Version

NM_001056281.1 GI:115452290 GeneID:4332449

Length

2692 bp

Definition

Oryza sativa Japonica Group Os03g0281900, complete gene.

Source

Oryza sativa Japonica Group 

 ORGANISM  Oryza sativa Japonica Group
           Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
           Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
           clade; Ehrhartoideae; Oryzeae; Oryza.
Chromosome

Chromosome 3

Location

Chromosome 3:9704996..9707687

Sequence Coding Region

9705038..9707401

Expression

GEO Profiles:Os03g0281900

Genome Context

<gbrowseImage1> name=NC_008396:9704996..9707687 source=RiceChromosome03 preset=GeneLocation </gbrowseImage1>

Gene Structure

<gbrowseImage2> name=NC_008396:9704996..9707687 source=RiceChromosome03 preset=GeneLocation </gbrowseImage2>

Coding Sequence

<cdnaseq>atgtcgcggtttgtcgacaagctgccgctgttcgaccggaggccgtcgccgatggaggaggccgagggcctcccgcgcagtggctatcttgggcagctgcaccaccaccagtactaccagccgcacagcaacatgctgccgctggagcagtcgccgccgacgagcacgaagcacacgtcggtcacgctcgcgcagctcctgaagcgcgtgaacgacgcgcgcagcgggtcgtcgacgcccatctcgtcgccgcgctacaccatcgagctgggcgggtccaagccggagtccgtcagcagcgagagcgacgaccaccactccgacgacggcggcagcgaggggcagccgagggcgctcgtgctcaagttcaccgacctgacgtacagcgtgaagcagcggaggaaggggtcgtgcctgccgttccgtcgtgcggcggcggacgagcccgagctgcccgcgatgaggacgctgctcgacggcatctccggcgaggcccgggacggcgagatcatggcggtgctcggcgcgagcgggtccggcaagagcacgctcatcgacgcgctcgccaaccgcatcgccaaggagagcctccacggctccgtcacgatcaacggcgagtccatcgacagcaacctgctcaaggtcatctcagcgtacgtccggcaggaggaccttctgtacccgatgctcaccgtcgaggagacgctcatgttcgccgccgagttccgcctgccgcgctccctccccaccagggagaagaagaagcgggtgaaggagctaatcgaccagctcggcctgaagagagcggcgaacacgatcatcggcgacgagggccaccgcggcgtgtcgggaggcgagcgccggcgcgtctccatcggtgtcgacatcatccacaacccgatcatgctgttcctcgacgagcccacctccgggctggactccaccagcgcgttcatggtggtgacggtcctcaaggccatcgcgcagagcggcagcgtcgtcgtcatgtccatccaccagccgagctaccgcatcctcggcctcctcgaccgcctcctgttcctctcccgcgggaagacggtgtactacggcccgccgagcgagctgccgccgttcttcctcgacttcggcaagcccatcccggacaacgagaacccgacggagttcgcgctggacctcatcaaggagatggagaccgagacggaggggaccaagcgtctcgccgagcacaacgcggcgtggcagctgaagcaccacggggaaggccgcgggtacggcggcaagccggggatgtccctcaaggaggccatcagcgccagcatctcgcgcgggaagctcgtgtccggcgcgaccgacggcaccgtgtcggtcgccgcctccgaccattctgcgccgccgccgtcgtcgtcgtccgtgtccaagttcgtcaacccgttctggatcgagatgggggtgctgacgcgtcgcgcgttcatcaacacgaagcgcacgccggaggtgttcatcatccgcctcgcggcggtgctggtcaccgggttcatcctcgccaccatcttctggcgcctggacgagtcgcccaagggcgtgcaggagcggctgggcttcttcgccatcgccatgtccaccatgtactacacctgctccgacgcgctcccggtgttcctcagcgagcgctacatcttcctcagggagacggcgtacaacgcgtaccgccgctcatcctacgtgctctcccacaccatcgtcggcttcccgtcgctcgtggttctctccttcgcgttcgcgctcaccaccttcttctccgtggggctcgccggtggcgtgaacgggttcttctacttcgtggcaatcgtgctggcctccttctgggcggggagcggcttcgccacgttcctctccggcgtggtgacgcacgtgatgctggggttccccgtggtgctctccacgctcgcctacttcctcctcttcagcggcttcttcatcaaccgcgacaggatcccgcgctactggctgtggttccactacatctcgctcgtcaagtacccgtacgaggcggtgatgcagaacgagttcggcgacccgacgaggtgcttcgtccgcggcgtgcagatgttcgacaacacgccgctggcggcgctgccggcggcggtcaaggtgcgggtgctgcagtccatgtcggcgtcgctcggcgtgaacatcggcacggggacgtgcatcaccacgggaccggacttcctgaagcagcaggcgatcaccgacttcggcaagtgggagtgcctctggatcaccgtcgcgtggggattcctcttccgcatcctcttctacatctcgctgctgctcggcagcaggaacaagcggaggtag</cdnaseq>

Protein Sequence

<aaseq>MSRFVDKLPLFDRRPSPMEEAEGLPRSGYLGQLHHHQYYQPHSN MLPLEQSPPTSTKHTSVTLAQLLKRVNDARSGSSTPISSPRYTIELGGSKPESVSSES DDHHSDDGGSEGQPRALVLKFTDLTYSVKQRRKGSCLPFRRAAADEPELPAMRTLLDG ISGEARDGEIMAVLGASGSGKSTLIDALANRIAKESLHGSVTINGESIDSNLLKVISA YVRQEDLLYPMLTVEETLMFAAEFRLPRSLPTREKKKRVKELIDQLGLKRAANTIIGD EGHRGVSGGERRRVSIGVDIIHNPIMLFLDEPTSGLDSTSAFMVVTVLKAIAQSGSVV VMSIHQPSYRILGLLDRLLFLSRGKTVYYGPPSELPPFFLDFGKPIPDNENPTEFALD LIKEMETETEGTKRLAEHNAAWQLKHHGEGRGYGGKPGMSLKEAISASISRGKLVSGA TDGTVSVAASDHSAPPPSSSSVSKFVNPFWIEMGVLTRRAFINTKRTPEVFIIRLAAV LVTGFILATIFWRLDESPKGVQERLGFFAIAMSTMYYTCSDALPVFLSERYIFLRETA YNAYRRSSYVLSHTIVGFPSLVVLSFAFALTTFFSVGLAGGVNGFFYFVAIVLASFWA GSGFATFLSGVVTHVMLGFPVVLSTLAYFLLFSGFFINRDRIPRYWLWFHYISLVKYP YEAVMQNEFGDPTRCFVRGVQMFDNTPLAALPAAVKVRVLQSMSASLGVNIGTGTCIT TGPDFLKQQAITDFGKWECLWITVAWGFLFRILFYISLLLGSRNKRR</aaseq>

Gene Sequence

<dnaseqindica>43..2406#tacttgtattggtaagagactaagagagtgagcttgccggagatgtcgcggtttgtcgacaagctgccgctgttcgaccggaggccgtcgccgatggaggaggccgagggcctcccgcgcagtggctatcttgggcagctgcaccaccaccagtactaccagccgcacagcaacatgctgccgctggagcagtcgccgccgacgagcacgaagcacacgtcggtcacgctcgcgcagctcctgaagcgcgtgaacgacgcgcgcagcgggtcgtcgacgcccatctcgtcgccgcgctacaccatcgagctgggcgggtccaagccggagtccgtcagcagcgagagcgacgaccaccactccgacgacggcggcagcgaggggcagccgagggcgctcgtgctcaagttcaccgacctgacgtacagcgtgaagcagcggaggaaggggtcgtgcctgccgttccgtcgtgcggcggcggacgagcccgagctgcccgcgatgaggacgctgctcgacggcatctccggcgaggcccgggacggcgagatcatggcggtgctcggcgcgagcgggtccggcaagagcacgctcatcgacgcgctcgccaaccgcatcgccaaggagagcctccacggctccgtcacgatcaacggcgagtccatcgacagcaacctgctcaaggtcatctcagcgtacgtccggcaggaggaccttctgtacccgatgctcaccgtcgaggagacgctcatgttcgccgccgagttccgcctgccgcgctccctccccaccagggagaagaagaagcgggtgaaggagctaatcgaccagctcggcctgaagagagcggcgaacacgatcatcggcgacgagggccaccgcggcgtgtcgggaggcgagcgccggcgcgtctccatcggtgtcgacatcatccacaacccgatcatgctgttcctcgacgagcccacctccgggctggactccaccagcgcgttcatggtggtgacggtcctcaaggccatcgcgcagagcggcagcgtcgtcgtcatgtccatccaccagccgagctaccgcatcctcggcctcctcgaccgcctcctgttcctctcccgcgggaagacggtgtactacggcccgccgagcgagctgccgccgttcttcctcgacttcggcaagcccatcccggacaacgagaacccgacggagttcgcgctggacctcatcaaggagatggagaccgagacggaggggaccaagcgtctcgccgagcacaacgcggcgtggcagctgaagcaccacggggaaggccgcgggtacggcggcaagccggggatgtccctcaaggaggccatcagcgccagcatctcgcgcgggaagctcgtgtccggcgcgaccgacggcaccgtgtcggtcgccgcctccgaccattctgcgccgccgccgtcgtcgtcgtccgtgtccaagttcgtcaacccgttctggatcgagatgggggtgctgacgcgtcgcgcgttcatcaacacgaagcgcacgccggaggtgttcatcatccgcctcgcggcggtgctggtcaccgggttcatcctcgccaccatcttctggcgcctggacgagtcgcccaagggcgtgcaggagcggctgggcttcttcgccatcgccatgtccaccatgtactacacctgctccgacgcgctcccggtgttcctcagcgagcgctacatcttcctcagggagacggcgtacaacgcgtaccgccgctcatcctacgtgctctcccacaccatcgtcggcttcccgtcgctcgtggttctctccttcgcgttcgcgctcaccaccttcttctccgtggggctcgccggtggcgtgaacgggttcttctacttcgtggcaatcgtgctggcctccttctgggcggggagcggcttcgccacgttcctctccggcgtggtgacgcacgtgatgctggggttccccgtggtgctctccacgctcgcctacttcctcctcttcagcggcttcttcatcaaccgcgacaggatcccgcgctactggctgtggttccactacatctcgctcgtcaagtacccgtacgaggcggtgatgcagaacgagttcggcgacccgacgaggtgcttcgtccgcggcgtgcagatgttcgacaacacgccgctggcggcgctgccggcggcggtcaaggtgcgggtgctgcagtccatgtcggcgtcgctcggcgtgaacatcggcacggggacgtgcatcaccacgggaccggacttcctgaagcagcaggcgatcaccgacttcggcaagtgggagtgcctctggatcaccgtcgcgtggggattcctcttccgcatcctcttctacatctcgctgctgctcggcagcaggaacaagcggaggtagacgacgacgacgaccaccttgctgatcgatcagtagctcgtacgtgatagcgatcgtcacctcgtctcaccgcagcggcggcgtggaccggccggcttcgttggagcaagcgacgcgtgggacaccattggttgcatggtttcccttgttttttttttcacttgttaaacatttcgatgttttttgattaaccgcctgtgattaacatgggacgggagttgtttgtaaaatttgtgtgcaagttgcaagtcgaaattgtatctggatgatatgacatttttttttc</dnaseqindica>

External Link(s)

NCBI Gene:Os03g0281900, RefSeq:Os03g0281900

  1. ↑ 1.0 1.1 Cite error: Invalid <ref> tag; no text was provided for refs named ref1
  2. ↑ 2.0 2.1 2.2 Armstrong, W. (1979) Aeration in higher plants. Adv. Bot. Res. 7, 225–332.
  3. ↑ 3.0 3.1 3.2 Soukup, A., Armstrong, W., Schreiber, L., Franke, R. and Votrubová, O. (2007) Apoplastic barriers to radial oxygen loss and solute penetration: a chemical and functional comparison of the exodermis of two wetland species, Phragmites australis and Glyceria maxima. New Phytol. 173, 264–278.
  4. ↑ 4.0 4.1 Kotula, L., Ranathunge, K., Schreiber, L. and Steudle, E. (2009) Functional and chemical comparison of apoplastic barriers to radial oxygen loss in roots of rice (Oryza sativa L.) grown in aerated or deoxygenated solution. J. Exp. Bot. 60, 2155–2167.
  5. ↑ 5.0 5.1 Ranathunge, K., Schreiber, L. and Franke, R. (2011b) Suberin research in the genomics era - new interest for an old polymer. Plant Sci. 180, 399–413.
  6. ↑ 6.0 6.1 Watanabe, K., Nishiuchi, S., Kulichikhin, K. and Nakazono, M. (2013) Does suberin accumulation in plant roots contribute to waterlogging tolerance? Front. Plant Sci. 4, 1–7.
  7. ↑ Schönherr, J. (1982) Resistance of plant surfaces to water loss: transport properties of cutin, suberin and associated lipids. In Physiological Plant Ecology II, Water Relations and Carbon Assimilation, Encyclopedia of Plant Physiology New Series Volume 12B (Lange, O.L., Nobel, P.S., Osmond, C.B. and Ziegler, H., eds). Berlin, Heidelberg, New York: Springer, pp. 154–179.
  8. ↑ Vogt, E., Schönherr, J. and Schmidt, H.W. (1983) Water permeability of periderm membranes isolated enzymatically from potato tubers (Solanum tuberosum L.). Planta, 158, 294–301.
  9. ↑ Schreiber, L., Franke, R., Hartmann, K.D., Ranathunge, K. and Steudle, E. (2005) The chemical composition of suberin in apoplastic barriers affects radial hydraulic conductivity differently in the roots of rice (Oryza sativa L. cv. IR64) and corn (Zea mays L. cv. Helix). J. Exp. Bot. 56, 1427–1436.
  10. ↑ Ranathunge, K., Lin, J., Steudle, E. and Schreiber, L. (2011a) Stagnant deoxygenated growth enhances root suberization and lignifications, but differentially affects water and NaCl permeabilities in rice (Oryza sativa L.) roots. Plant, Cell Environ. 34, 1223–1240.
  11. ↑ Panikashvili, D., Shi, J.X., Bocobza, S., Franke, R.B., Schreiber, L. and Aharoni, A. (2010) The Arabidopsis DSO/ABCG11 transporter affects cutin metabolism in reproductive organs and suberin in roots. Mol. Plant 3, 563–575.
  12. ↑ Franke, R. and Schreiber, L. (2007) Suberin – a biopolyester forming apoplastic plant interfaces. Curr. Opin. Plant Biol. 10, 252–259.
  13. ↑ Beisson, F., Li-Beisson, Y. and Pollard, M. (2012) Solving the puzzles of cutin and suberin polymer biosynthesis. Curr. Opin. Plant Biol. 15, 329–337.
  14. ↑ Pighin, J.A., Zheng, H., Balakshin, L.J., Goodman, I.P., Western, T.L., Jetter, R., Kunst, L. and Samuels, A.L. (2004) Plant cuticular lipid export requires an ABC transporter. Science, 306, 702–704.
  15. ↑ Bird, D., Beisson, F., Brigham, A., Shin, J., Greer, S., Jetter, R., Kunst, L., Wu, X., Yephremov, A. and Samuels, L. (2007) Characterization of Arabidopsis ABCG11/WBC11, an ATP binding cassette (ABC) transporter that is required for cuticular lipid secretion. Plant J. 52, 485–498.
  16. ↑ Luo, B., Xue, X., Hu, W., Wang, L. and Chen, X. (2007) An ABC transporter gene of Arabidopsis thaliana, AtWBC11, is involved in cuticle development and prevention of organ fusion. Plant Cell Physiol. 48, 1790–1802.
  17. ↑ Panikashvili, D., Savaldi-Goldstein, S., Mandel, T., Yifhar, T., Franke, R.B., Höfer, R., Schreiber, L., Chory, J. and Aharoni, A. (2007) The Arabidopsis DESPERADO/AtWBC11 transporter is required for cutin and wax secretion. Plant Physiol. 145, 1345–1360.
  18. ↑ Chen, G., Komatsuda, T., Ma, J.F. et al. (2011) An ATP-binding cassette subfamily G full transporter is essential for the retention of leaf water in both wild barley and rice. Proc. Natl Acad. Sci. USA, 108, 12354–12359.
  19. ↑ Yasuno, N., Takamure, I., Kidou, S., Tokuji, Y., Ureshi, A., Funabiki, A., Ashikaga, K., Yamanouchi, U., Yano, M. and Kato, K. (2009) Rice shoot branching requires an ATP-binding cassette subfamily G protein. New Phytol. 182, 91–101.
  20. ↑ Graf, G.A., Li, W., Gerard, R.D., Gelissen, I., White, A., Cohen, J.C. and Hobbs, H.H. (2002) Coexpression of ATP-binding cassette proteins ABCG5 and ABCG8 permits their transport to the apical surface. J. Clin. Invest. 110, 659–669.
  21. ↑ Graf, G.A., Yu, L., Li, W., Gerard, R., Tuma, P.L., Cohen, J.C. and Hobbs, H.H. (2003) ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and biliary cholesterol excretion. J. Biol. Chem. 278, 48275–48282.
  22. ↑ Hirata, T., Okabe, M., Kobayashi, A., Ueda, K. and Matsuo, M. (2009) Molecular mechanisms of subcellular localization of ABCG5 and ABCG8. Biosci. Biotechnol. Biochem. 73, 619–626.
Retrieved from "https://ngdc.cncb.ac.cn/ricewiki/index.php?title=Os03g0281900&oldid=184521"