Cargando…

Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice

Ribulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) is a nuclear gene that encodes a chloroplast protein that plays an important role in photosynthesis. Some reports have indicated that it may play a role in acclimation to different abiotic stresses. In this paper, we analyzed the stress-...

Descripción completa

Detalles Bibliográficos
Autores principales: Chen, Yue, Wang, Xiao-Man, Zhou, Li, He, Yi, Wang, Dun, Qi, Yan-Hua, Jiang, De-An
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4610672/
https://www.ncbi.nlm.nih.gov/pubmed/26479064
http://dx.doi.org/10.1371/journal.pone.0140934
_version_ 1782395985295572992
author Chen, Yue
Wang, Xiao-Man
Zhou, Li
He, Yi
Wang, Dun
Qi, Yan-Hua
Jiang, De-An
author_facet Chen, Yue
Wang, Xiao-Man
Zhou, Li
He, Yi
Wang, Dun
Qi, Yan-Hua
Jiang, De-An
author_sort Chen, Yue
collection PubMed
description Ribulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) is a nuclear gene that encodes a chloroplast protein that plays an important role in photosynthesis. Some reports have indicated that it may play a role in acclimation to different abiotic stresses. In this paper, we analyzed the stress-responsive elements in the 2.0 kb 5’-upstream regions of the RCA gene promoter and the primary, secondary and tertiary structure of the protein. We identified some cis-elements of multiple stress-related components in the RCA promoter. Amino acid and evolution analyses showed that the RCA protein had conserved regions between different species; however, the size and type varied. The secondary structures, binding sites and tertiary structures of the RCA proteins were also different. This might reflect the differences in the transcription and translation levels of the two RCA isoforms during adaptation to different abiotic stresses. Although both the transcription and translation levels of RCA isoforms in the rice leaves increased under various stresses, the large isoform was increased more significantly in the chloroplast stroma and thylakoid. It can be concluded that RCA, especially RCA(L), is also a multiple responder to abiotic stresses in rice, which provides new insights into RCA functions.
format Online
Article
Text
id pubmed-4610672
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-46106722015-10-29 Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice Chen, Yue Wang, Xiao-Man Zhou, Li He, Yi Wang, Dun Qi, Yan-Hua Jiang, De-An PLoS One Research Article Ribulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) is a nuclear gene that encodes a chloroplast protein that plays an important role in photosynthesis. Some reports have indicated that it may play a role in acclimation to different abiotic stresses. In this paper, we analyzed the stress-responsive elements in the 2.0 kb 5’-upstream regions of the RCA gene promoter and the primary, secondary and tertiary structure of the protein. We identified some cis-elements of multiple stress-related components in the RCA promoter. Amino acid and evolution analyses showed that the RCA protein had conserved regions between different species; however, the size and type varied. The secondary structures, binding sites and tertiary structures of the RCA proteins were also different. This might reflect the differences in the transcription and translation levels of the two RCA isoforms during adaptation to different abiotic stresses. Although both the transcription and translation levels of RCA isoforms in the rice leaves increased under various stresses, the large isoform was increased more significantly in the chloroplast stroma and thylakoid. It can be concluded that RCA, especially RCA(L), is also a multiple responder to abiotic stresses in rice, which provides new insights into RCA functions. Public Library of Science 2015-10-19 /pmc/articles/PMC4610672/ /pubmed/26479064 http://dx.doi.org/10.1371/journal.pone.0140934 Text en © 2015 Chen et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Chen, Yue
Wang, Xiao-Man
Zhou, Li
He, Yi
Wang, Dun
Qi, Yan-Hua
Jiang, De-An
Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice
title Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice
title_full Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice
title_fullStr Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice
title_full_unstemmed Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice
title_short Rubisco Activase Is Also a Multiple Responder to Abiotic Stresses in Rice
title_sort rubisco activase is also a multiple responder to abiotic stresses in rice
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4610672/
https://www.ncbi.nlm.nih.gov/pubmed/26479064
http://dx.doi.org/10.1371/journal.pone.0140934
work_keys_str_mv AT chenyue rubiscoactivaseisalsoamultiplerespondertoabioticstressesinrice
AT wangxiaoman rubiscoactivaseisalsoamultiplerespondertoabioticstressesinrice
AT zhouli rubiscoactivaseisalsoamultiplerespondertoabioticstressesinrice
AT heyi rubiscoactivaseisalsoamultiplerespondertoabioticstressesinrice
AT wangdun rubiscoactivaseisalsoamultiplerespondertoabioticstressesinrice
AT qiyanhua rubiscoactivaseisalsoamultiplerespondertoabioticstressesinrice
AT jiangdean rubiscoactivaseisalsoamultiplerespondertoabioticstressesinrice