Difference between revisions of "Os03g0281900"

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===Function===
 
===Function===
 
[[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 (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.
 
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 (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).
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[[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) (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.
 
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.

Revision as of 13:33, 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 (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 [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 (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 [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 (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. 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 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.
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