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A GDSL‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley

The hydrophobic cuticle covers the surface of the most aerial organs of land plants. The barley mutant eceriferum‐zv (cer‐zv), which is hypersensitive to drought, is unable to accumulate a sufficient quantity of cutin in its leaf cuticle. The mutated locus has been mapped to a 0.02 cM segment in the...

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Autores principales: Li, Chao, Chen, Guoxiong, Mishina, Kohei, Yamaji, Naoki, Ma, Jian Feng, Yukuhiro, Fumiko, Tagiri, Akemi, Liu, Cheng, Pourkheirandish, Mohammad, Anwar, Nadia, Ohta, Masaru, Zhao, Pengshan, Lundqvist, Udda, Li, Xinrong, Komatsuda, Takao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6508521/
https://www.ncbi.nlm.nih.gov/pubmed/31245672
http://dx.doi.org/10.1002/pld3.25
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author Li, Chao
Chen, Guoxiong
Mishina, Kohei
Yamaji, Naoki
Ma, Jian Feng
Yukuhiro, Fumiko
Tagiri, Akemi
Liu, Cheng
Pourkheirandish, Mohammad
Anwar, Nadia
Ohta, Masaru
Zhao, Pengshan
Lundqvist, Udda
Li, Xinrong
Komatsuda, Takao
author_facet Li, Chao
Chen, Guoxiong
Mishina, Kohei
Yamaji, Naoki
Ma, Jian Feng
Yukuhiro, Fumiko
Tagiri, Akemi
Liu, Cheng
Pourkheirandish, Mohammad
Anwar, Nadia
Ohta, Masaru
Zhao, Pengshan
Lundqvist, Udda
Li, Xinrong
Komatsuda, Takao
author_sort Li, Chao
collection PubMed
description The hydrophobic cuticle covers the surface of the most aerial organs of land plants. The barley mutant eceriferum‐zv (cer‐zv), which is hypersensitive to drought, is unable to accumulate a sufficient quantity of cutin in its leaf cuticle. The mutated locus has been mapped to a 0.02 cM segment in the pericentromeric region of chromosome 4H. As a map‐based cloning approach to isolate the gene was therefore considered unlikely to be feasible, a comparison was instead made between the transcriptomes of the mutant and the wild type. In conjunction with extant genomic information, on the basis of predicted functionality, only two genes were considered likely to encode a product associated with cutin formation. When eight independent cer‐zv mutant alleles were resequenced with respect to the two candidate genes, it was confirmed that the gene underlying the mutation in each allele encodes a Gly‐Asp‐Ser‐Leu (GDSL)‐motif esterase/acyltransferase/lipase. The gene was transcribed in the epidermis, and its product was exclusively deposited in cell wall at the boundary of the cuticle in the leaf elongation zone, coinciding with the major site of cutin deposition. CER‐ZV is speculated to function in the deposition of cutin polymer. Its homologs were found in green algae, moss, and euphyllophytes, indicating that it is highly conserved in plant kingdom.
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spelling pubmed-65085212019-06-26 A GDSL‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley Li, Chao Chen, Guoxiong Mishina, Kohei Yamaji, Naoki Ma, Jian Feng Yukuhiro, Fumiko Tagiri, Akemi Liu, Cheng Pourkheirandish, Mohammad Anwar, Nadia Ohta, Masaru Zhao, Pengshan Lundqvist, Udda Li, Xinrong Komatsuda, Takao Plant Direct Original Research The hydrophobic cuticle covers the surface of the most aerial organs of land plants. The barley mutant eceriferum‐zv (cer‐zv), which is hypersensitive to drought, is unable to accumulate a sufficient quantity of cutin in its leaf cuticle. The mutated locus has been mapped to a 0.02 cM segment in the pericentromeric region of chromosome 4H. As a map‐based cloning approach to isolate the gene was therefore considered unlikely to be feasible, a comparison was instead made between the transcriptomes of the mutant and the wild type. In conjunction with extant genomic information, on the basis of predicted functionality, only two genes were considered likely to encode a product associated with cutin formation. When eight independent cer‐zv mutant alleles were resequenced with respect to the two candidate genes, it was confirmed that the gene underlying the mutation in each allele encodes a Gly‐Asp‐Ser‐Leu (GDSL)‐motif esterase/acyltransferase/lipase. The gene was transcribed in the epidermis, and its product was exclusively deposited in cell wall at the boundary of the cuticle in the leaf elongation zone, coinciding with the major site of cutin deposition. CER‐ZV is speculated to function in the deposition of cutin polymer. Its homologs were found in green algae, moss, and euphyllophytes, indicating that it is highly conserved in plant kingdom. John Wiley and Sons Inc. 2017-11-03 /pmc/articles/PMC6508521/ /pubmed/31245672 http://dx.doi.org/10.1002/pld3.25 Text en © 2017 The Authors. Plant Direct published by American Society of Plant Biologists, Society for Experimental Biology and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Research
Li, Chao
Chen, Guoxiong
Mishina, Kohei
Yamaji, Naoki
Ma, Jian Feng
Yukuhiro, Fumiko
Tagiri, Akemi
Liu, Cheng
Pourkheirandish, Mohammad
Anwar, Nadia
Ohta, Masaru
Zhao, Pengshan
Lundqvist, Udda
Li, Xinrong
Komatsuda, Takao
A GDSL‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley
title A GDSL‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley
title_full A GDSL‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley
title_fullStr A GDSL‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley
title_full_unstemmed A GDSL‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley
title_short A GDSL‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley
title_sort gdsl‐motif esterase/acyltransferase/lipase is responsible for leaf water retention in barley
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6508521/
https://www.ncbi.nlm.nih.gov/pubmed/31245672
http://dx.doi.org/10.1002/pld3.25
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