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Identification and functional analysis of proteins in response to light intensity, temperature and water potential in Brassica rapa hypocotyl

Hypocotyl elongation is an early event in plant growth and development and is sensitive to fluctuations in light, temperature, water potential and nutrients. Most research on hypocotyl elongation has focused on the regulatory mechanism of a single environment factor. However, information about combi...

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Autores principales: Wang, Hongfei, Shang, Qingmao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6850590/
https://www.ncbi.nlm.nih.gov/pubmed/30456857
http://dx.doi.org/10.1111/ppl.12865
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author Wang, Hongfei
Shang, Qingmao
author_facet Wang, Hongfei
Shang, Qingmao
author_sort Wang, Hongfei
collection PubMed
description Hypocotyl elongation is an early event in plant growth and development and is sensitive to fluctuations in light, temperature, water potential and nutrients. Most research on hypocotyl elongation has focused on the regulatory mechanism of a single environment factor. However, information about combined effects of multi‐environment factors remains unavailable, and overlapping sites of the environmental factors signaling pathways in the regulation of hypocotyl elongation remain unclear. To identify how cross‐talks among light intensity, temperature and water potential regulate hypocotyl elongation in Brassica rapa L. ssp. chinesis, a comprehensive isobaric tag for relative and absolute quantitation‐based proteomic approach was adopted. In total, 7259 proteins were quantified, and 378 differentially expressed proteins (DEPs) were responsive to all three environmental factors. The DEPs were involved in a variety of biochemical processes, including signal transduction, cytoskeletal organization, carbohydrate metabolism, cell wall organization, protein modification and transport. The DEPs did not function in isolation, but acted in a large and complex interaction network to affect hypocotyl elongation. Among the DEPs, phyB was outstanding for its significant fold change in quantity and complex interaction networks with other proteins. In addition, changes of sensitivity to environmental factors in phyB‐9 suggested a key role in the regulation of hypocotyl elongation. Overall, the data presented in this study show a profile of proteins interaction network in response to light intensity, temperature and water potential and provides molecular basis of hypocotyl elongation in B. rapa.
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spelling pubmed-68505902019-11-18 Identification and functional analysis of proteins in response to light intensity, temperature and water potential in Brassica rapa hypocotyl Wang, Hongfei Shang, Qingmao Physiol Plant Original Articles Hypocotyl elongation is an early event in plant growth and development and is sensitive to fluctuations in light, temperature, water potential and nutrients. Most research on hypocotyl elongation has focused on the regulatory mechanism of a single environment factor. However, information about combined effects of multi‐environment factors remains unavailable, and overlapping sites of the environmental factors signaling pathways in the regulation of hypocotyl elongation remain unclear. To identify how cross‐talks among light intensity, temperature and water potential regulate hypocotyl elongation in Brassica rapa L. ssp. chinesis, a comprehensive isobaric tag for relative and absolute quantitation‐based proteomic approach was adopted. In total, 7259 proteins were quantified, and 378 differentially expressed proteins (DEPs) were responsive to all three environmental factors. The DEPs were involved in a variety of biochemical processes, including signal transduction, cytoskeletal organization, carbohydrate metabolism, cell wall organization, protein modification and transport. The DEPs did not function in isolation, but acted in a large and complex interaction network to affect hypocotyl elongation. Among the DEPs, phyB was outstanding for its significant fold change in quantity and complex interaction networks with other proteins. In addition, changes of sensitivity to environmental factors in phyB‐9 suggested a key role in the regulation of hypocotyl elongation. Overall, the data presented in this study show a profile of proteins interaction network in response to light intensity, temperature and water potential and provides molecular basis of hypocotyl elongation in B. rapa. Blackwell Publishing Ltd 2019-01-10 2019-09 /pmc/articles/PMC6850590/ /pubmed/30456857 http://dx.doi.org/10.1111/ppl.12865 Text en © 2018 The Authors. Physiologia Plantarum published by John Wiley & Sons Ltd on behalf of Scandinavian Plant Physiology Society. 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 Articles
Wang, Hongfei
Shang, Qingmao
Identification and functional analysis of proteins in response to light intensity, temperature and water potential in Brassica rapa hypocotyl
title Identification and functional analysis of proteins in response to light intensity, temperature and water potential in Brassica rapa hypocotyl
title_full Identification and functional analysis of proteins in response to light intensity, temperature and water potential in Brassica rapa hypocotyl
title_fullStr Identification and functional analysis of proteins in response to light intensity, temperature and water potential in Brassica rapa hypocotyl
title_full_unstemmed Identification and functional analysis of proteins in response to light intensity, temperature and water potential in Brassica rapa hypocotyl
title_short Identification and functional analysis of proteins in response to light intensity, temperature and water potential in Brassica rapa hypocotyl
title_sort identification and functional analysis of proteins in response to light intensity, temperature and water potential in brassica rapa hypocotyl
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6850590/
https://www.ncbi.nlm.nih.gov/pubmed/30456857
http://dx.doi.org/10.1111/ppl.12865
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