Os03g0281900

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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 Cite error: The opening <ref> tag is malformed or has a bad name [7]. 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 [8][9], while the chain length in maize roots ranged only from C16 to C26 in rhizodermal and hypodermal cell walls [8]. 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 [8][9]. The total contents of aliphatic suberin fraction and its monomers were significantly increased in rice (cv. Azucena) roots by stagnant deoxygenated treatments [9], 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 [10] and maize [8], 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 [3]. Further studies are needed to understand the correlation between waterlogging tolerance and accumulation of the chain lengths of C28 and C30 of aliphatic suberin.

rcn1-2 (cv. Shiokari background) mutant shows reduced aliphatic suberin monomer contents. (from reference [1]).

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 [5][11][12]. 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 [11]. 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 [13][14][15][16]. In barley, HvABCG31 (a full-size ABCG transporter) is also involved in cutin formation [17]. Additionally, its rice ortholog OsABCG31 may affect cutin formation, although the cutin contents of osabcg31 have not been reported [17] Cite error: Closing </ref> missing for <ref> tag [2] [3] [4] [5] [6] [18] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [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 1.2 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 5.2 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. ↑ 7.0 7.1 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.
  8. ↑ 8.0 8.1 8.2 8.3 8.4 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.
  9. ↑ 9.0 9.1 9.2 9.3 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.
  10. ↑ 10.0 10.1 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.
  11. ↑ 11.0 11.1 11.2 Franke, R. and Schreiber, L. (2007) Suberin – a biopolyester forming apoplastic plant interfaces. Curr. Opin. Plant Biol. 10, 252–259.
  12. ↑ 12.0 12.1 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.
  13. ↑ 13.0 13.1 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.
  14. ↑ 14.0 14.1 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.
  15. ↑ 15.0 15.1 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.
  16. ↑ 16.0 16.1 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.
  17. ↑ 17.0 17.1 17.2 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.
  18. ↑ 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.
  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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