Os03g0281900 - Revision history

192.168.72.52: /* Structured Information */

2015-06-12T05:45:36Z

‎Structured Information

Shijc at 13:45, 27 December 2014

2014-12-27T13:45:25Z

Shijc at 13:43, 27 December 2014

2014-12-27T13:43:30Z

Shijc at 13:40, 27 December 2014

2014-12-27T13:40:04Z

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Shijc at 13:33, 27 December 2014

2014-12-27T13:33:10Z

Shijc at 13:26, 27 December 2014

2014-12-27T13:26:04Z

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124.16.129.48 at 19:33, 22 July 2012

2012-07-22T19:33:12Z

127.0.0.1: Created page with "{{JaponicaGene| GeneName = Os03g0281900| Description = ABC transporter related domain containing protein| Version = NM_001056281.1 GI:115452290 GeneID:4332449| Length = 26..."

2012-06-24T12:32:51Z

Created page with "{{JaponicaGene| GeneName = Os03g0281900| Description = ABC transporter related domain containing protein| Version = NM_001056281.1 GI:115452290 GeneID:4332449| Length = 26..."

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{{JaponicaGene|
GeneName = 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 = [[:category:Japonica Chromosome 3|Chromosome 3]]|
AP = Chromosome 3:9704996..9707687|
CDS = 9705038..9707401|
GCID = <gbrowseImage1>
name=NC_008396:9704996..9707687
source=RiceChromosome03
preset=GeneLocation
</gbrowseImage1>|
GSID = <gbrowseImage2>
name=NC_008396:9704996..9707687
source=RiceChromosome03
preset=GeneLocation
</gbrowseImage2>|
CDNA = <cdnaseq>atgtcgcggtttgtcgacaagctgccgctgttcgaccggaggccgtcgccgatggaggaggccgagggcctcccgcgcagtggctatcttgggcagctgcaccaccaccagtactaccagccgcacagcaacatgctgccgctggagcagtcgccgccgacgagcacgaagcacacgtcggtcacgctcgcgcagctcctgaagcgcgtgaacgacgcgcgcagcgggtcgtcgacgcccatctcgtcgccgcgctacaccatcgagctgggcgggtccaagccggagtccgtcagcagcgagagcgacgaccaccactccgacgacggcggcagcgaggggcagccgagggcgctcgtgctcaagttcaccgacctgacgtacagcgtgaagcagcggaggaaggggtcgtgcctgccgttccgtcgtgcggcggcggacgagcccgagctgcccgcgatgaggacgctgctcgacggcatctccggcgaggcccgggacggcgagatcatggcggtgctcggcgcgagcgggtccggcaagagcacgctcatcgacgcgctcgccaaccgcatcgccaaggagagcctccacggctccgtcacgatcaacggcgagtccatcgacagcaacctgctcaaggtcatctcagcgtacgtccggcaggaggaccttctgtacccgatgctcaccgtcgaggagacgctcatgttcgccgccgagttccgcctgccgcgctccctccccaccagggagaagaagaagcgggtgaaggagctaatcgaccagctcggcctgaagagagcggcgaacacgatcatcggcgacgagggccaccgcggcgtgtcgggaggcgagcgccggcgcgtctccatcggtgtcgacatcatccacaacccgatcatgctgttcctcgacgagcccacctccgggctggactccaccagcgcgttcatggtggtgacggtcctcaaggccatcgcgcagagcggcagcgtcgtcgtcatgtccatccaccagccgagctaccgcatcctcggcctcctcgaccgcctcctgttcctctcccgcgggaagacggtgtactacggcccgccgagcgagctgccgccgttcttcctcgacttcggcaagcccatcccggacaacgagaacccgacggagttcgcgctggacctcatcaaggagatggagaccgagacggaggggaccaagcgtctcgccgagcacaacgcggcgtggcagctgaagcaccacggggaaggccgcgggtacggcggcaagccggggatgtccctcaaggaggccatcagcgccagcatctcgcgcgggaagctcgtgtccggcgcgaccgacggcaccgtgtcggtcgccgcctccgaccattctgcgccgccgccgtcgtcgtcgtccgtgtccaagttcgtcaacccgttctggatcgagatgggggtgctgacgcgtcgcgcgttcatcaacacgaagcgcacgccggaggtgttcatcatccgcctcgcggcggtgctggtcaccgggttcatcctcgccaccatcttctggcgcctggacgagtcgcccaagggcgtgcaggagcggctgggcttcttcgccatcgccatgtccaccatgtactacacctgctccgacgcgctcccggtgttcctcagcgagcgctacatcttcctcagggagacggcgtacaacgcgtaccgccgctcatcctacgtgctctcccacaccatcgtcggcttcccgtcgctcgtggttctctccttcgcgttcgcgctcaccaccttcttctccgtggggctcgccggtggcgtgaacgggttcttctacttcgtggcaatcgtgctggcctccttctgggcggggagcggcttcgccacgttcctctccggcgtggtgacgcacgtgatgctggggttccccgtggtgctctccacgctcgcctacttcctcctcttcagcggcttcttcatcaaccgcgacaggatcccgcgctactggctgtggttccactacatctcgctcgtcaagtacccgtacgaggcggtgatgcagaacgagttcggcgacccgacgaggtgcttcgtccgcggcgtgcagatgttcgacaacacgccgctggcggcgctgccggcggcggtcaaggtgcgggtgctgcagtccatgtcggcgtcgctcggcgtgaacatcggcacggggacgtgcatcaccacgggaccggacttcctgaagcagcaggcgatcaccgacttcggcaagtgggagtgcctctggatcaccgtcgcgtggggattcctcttccgcatcctcttctacatctcgctgctgctcggcagcaggaacaagcggaggtag</cdnaseq>|
AA = <aaseq>MSRFVDKLPLFDRRPSPMEEAEGLPRSGYLGQLHHHQYYQPHSN MLPLEQSPPTSTKHTSVTLAQLLKRVNDARSGSSTPISSPRYTIELGGSKPESVSSES DDHHSDDGGSEGQPRALVLKFTDLTYSVKQRRKGSCLPFRRAAADEPELPAMRTLLDG ISGEARDGEIMAVLGASGSGKSTLIDALANRIAKESLHGSVTINGESIDSNLLKVISA YVRQEDLLYPMLTVEETLMFAAEFRLPRSLPTREKKKRVKELIDQLGLKRAANTIIGD EGHRGVSGGERRRVSIGVDIIHNPIMLFLDEPTSGLDSTSAFMVVTVLKAIAQSGSVV VMSIHQPSYRILGLLDRLLFLSRGKTVYYGPPSELPPFFLDFGKPIPDNENPTEFALD LIKEMETETEGTKRLAEHNAAWQLKHHGEGRGYGGKPGMSLKEAISASISRGKLVSGA TDGTVSVAASDHSAPPPSSSSVSKFVNPFWIEMGVLTRRAFINTKRTPEVFIIRLAAV LVTGFILATIFWRLDESPKGVQERLGFFAIAMSTMYYTCSDALPVFLSERYIFLRETA YNAYRRSSYVLSHTIVGFPSLVVLSFAFALTTFFSVGLAGGVNGFFYFVAIVLASFWA GSGFATFLSGVVTHVMLGFPVVLSTLAYFLLFSGFFINRDRIPRYWLWFHYISLVKYP YEAVMQNEFGDPTRCFVRGVQMFDNTPLAALPAAVKVRVLQSMSASLGVNIGTGTCIT TGPDFLKQQAITDFGKWECLWITVAWGFLFRILFYISLLLGSRNKRR</aaseq>|
DNA = <dnaseqindica>43..2406#tacttgtattggtaagagactaagagagtgagcttgccggagatgtcgcggtttgtcgacaagctgccgctgttcgaccggaggccgtcgccgatggaggaggccgagggcctcccgcgcagtggctatcttgggcagctgcaccaccaccagtactaccagccgcacagcaacatgctgccgctggagcagtcgccgccgacgagcacgaagcacacgtcggtcacgctcgcgcagctcctgaagcgcgtgaacgacgcgcgcagcgggtcgtcgacgcccatctcgtcgccgcgctacaccatcgagctgggcgggtccaagccggagtccgtcagcagcgagagcgacgaccaccactccgacgacggcggcagcgaggggcagccgagggcgctcgtgctcaagttcaccgacctgacgtacagcgtgaagcagcggaggaaggggtcgtgcctgccgttccgtcgtgcggcggcggacgagcccgagctgcccgcgatgaggacgctgctcgacggcatctccggcgaggcccgggacggcgagatcatggcggtgctcggcgcgagcgggtccggcaagagcacgctcatcgacgcgctcgccaaccgcatcgccaaggagagcctccacggctccgtcacgatcaacggcgagtccatcgacagcaacctgctcaaggtcatctcagcgtacgtccggcaggaggaccttctgtacccgatgctcaccgtcgaggagacgctcatgttcgccgccgagttccgcctgccgcgctccctccccaccagggagaagaagaagcgggtgaaggagctaatcgaccagctcggcctgaagagagcggcgaacacgatcatcggcgacgagggccaccgcggcgtgtcgggaggcgagcgccggcgcgtctccatcggtgtcgacatcatccacaacccgatcatgctgttcctcgacgagcccacctccgggctggactccaccagcgcgttcatggtggtgacggtcctcaaggccatcgcgcagagcggcagcgtcgtcgtcatgtccatccaccagccgagctaccgcatcctcggcctcctcgaccgcctcctgttcctctcccgcgggaagacggtgtactacggcccgccgagcgagctgccgccgttcttcctcgacttcggcaagcccatcccggacaacgagaacccgacggagttcgcgctggacctcatcaaggagatggagaccgagacggaggggaccaagcgtctcgccgagcacaacgcggcgtggcagctgaagcaccacggggaaggccgcgggtacggcggcaagccggggatgtccctcaaggaggccatcagcgccagcatctcgcgcgggaagctcgtgtccggcgcgaccgacggcaccgtgtcggtcgccgcctccgaccattctgcgccgccgccgtcgtcgtcgtccgtgtccaagttcgtcaacccgttctggatcgagatgggggtgctgacgcgtcgcgcgttcatcaacacgaagcgcacgccggaggtgttcatcatccgcctcgcggcggtgctggtcaccgggttcatcctcgccaccatcttctggcgcctggacgagtcgcccaagggcgtgcaggagcggctgggcttcttcgccatcgccatgtccaccatgtactacacctgctccgacgcgctcccggtgttcctcagcgagcgctacatcttcctcagggagacggcgtacaacgcgtaccgccgctcatcctacgtgctctcccacaccatcgtcggcttcccgtcgctcgtggttctctccttcgcgttcgcgctcaccaccttcttctccgtggggctcgccggtggcgtgaacgggttcttctacttcgtggcaatcgtgctggcctccttctgggcggggagcggcttcgccacgttcctctccggcgtggtgacgcacgtgatgctggggttccccgtggtgctctccacgctcgcctacttcctcctcttcagcggcttcttcatcaaccgcgacaggatcccgcgctactggctgtggttccactacatctcgctcgtcaagtacccgtacgaggcggtgatgcagaacgagttcggcgacccgacgaggtgcttcgtccgcggcgtgcagatgttcgacaacacgccgctggcggcgctgccggcggcggtcaaggtgcgggtgctgcagtccatgtcggcgtcgctcggcgtgaacatcggcacggggacgtgcatcaccacgggaccggacttcctgaagcagcaggcgatcaccgacttcggcaagtgggagtgcctctggatcaccgtcgcgtggggattcctcttccgcatcctcttctacatctcgctgctgctcggcagcaggaacaagcggaggtagacgacgacgacgaccaccttgctgatcgatcagtagctcgtacgtgatagcgatcgtcacctcgtctcaccgcagcggcggcgtggaccggccggcttcgttggagcaagcgacgcgtgggacaccattggttgcatggtttcccttgttttttttttcacttgttaaacatttcgatgttttttgattaaccgcctgtgattaacatgggacgggagttgtttgtaaaatttgtgtgcaagttgcaagtcgaaattgtatctggatgatatgacatttttttttc</dnaseqindica>|
Link = [http://www.ncbi.nlm.nih.gov/nuccore/NM_001056281.1 RefSeq:Os03g0281900]|
}}
[[Category:Genes]]
[[Category:Japonica mRNA]]
[[Category:Oryza Sativa Japonica Group]]
[[Category:Japonica Genes]]
[[Category:Japonica Chromosome 3]]
[[Category:Chromosome 3]]

@@ 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" />).'']]
 '''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 <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.
+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. 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. 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.
@@ Line 11: / Line 11: @@
 [[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'''
-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.
+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.
 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.

@@ 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" />).'']]
 '''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 <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.
+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. 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.
+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. 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.
+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" />).'']]

@@ Line 4: / Line 4: @@
 ===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" />).'']]
-‘’’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.
 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).
@@ Line 10: / Line 10: @@
 [[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.
 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.

← Older revision		Revision as of 19:33, 22 July 2012
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		+	==Annotated Information==
		+	===Function===
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		+	===Expression===
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		+	===Evolution===
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		+	==Structured Information==
	{{JaponicaGene\|		{{JaponicaGene\|
	GeneName = Os03g0281900\|		GeneName = Os03g0281900\|

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 ==Structured Information==
 [[Category:Genes]]
 [[Category:Japonica mRNA]]