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Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.)

Auxin response factors (ARFs) are key regulators of plant growth and development. Through interaction with auxin/indole acetic acid (Aux/IAA) proteins, they influence the expression of auxin response genes. An ARF gene family has been predicted in rice, but the functions of the individual structural...

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Autores principales: Shen, ChenJia, Wang, SuiKang, Bai, YouHuang, Wu, YunRong, Zhang, SaiNa, Chen, Ming, Guilfoyle, Tom J., Wu, Ping, Qi, YanHua
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2935870/
https://www.ncbi.nlm.nih.gov/pubmed/20693412
http://dx.doi.org/10.1093/jxb/erq208
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author Shen, ChenJia
Wang, SuiKang
Bai, YouHuang
Wu, YunRong
Zhang, SaiNa
Chen, Ming
Guilfoyle, Tom J.
Wu, Ping
Qi, YanHua
author_facet Shen, ChenJia
Wang, SuiKang
Bai, YouHuang
Wu, YunRong
Zhang, SaiNa
Chen, Ming
Guilfoyle, Tom J.
Wu, Ping
Qi, YanHua
author_sort Shen, ChenJia
collection PubMed
description Auxin response factors (ARFs) are key regulators of plant growth and development. Through interaction with auxin/indole acetic acid (Aux/IAA) proteins, they influence the expression of auxin response genes. An ARF gene family has been predicted in rice, but the functions of the individual structural domains of the OsARFs remain obscure. Bioinformatics was used to analyse the position of the DNA-binding domain (DBD), middle region (MR), and C-terminal dimerization domain (CTD) of OsARFs, and experimentally confirmed the presence of a classical monopartite nuclear localization signal (NLS) in the DBD. The DBD was shown to contribute to nuclear localization of OsARF proteins in addition to its known DNA-binding function. Interactions between 14 integrated OsARFs and 15 OsIAA proteins were tested using yeast two-hybrid assays. It was found that eight OsARF activators interacted with the 15 OsIAA proteins, while six OsARF repressors did not. The interactions between the MR+CTD or CTD of 10 OsARFs and 15 OsIAA proteins were also tested and the results were consistent with those of each intact OsARF, although some slight differences in interaction intensity were observed by α-galactosidase quantitative assays. The truncated CTD of OsARF11 did not interact with any OsIAA, implying that the CTD is required for ARF–IAA dimerization, and that the MR influences the interaction intensity in yeast. A subset of the interactions in yeast were also observed in tobacco plants using firefly luciferase complementation imaging assays, indicating that these interactions are specific in plants, and might have a special role in the auxin signalling response. This study provides new insight into the structure of OsARF proteins and ARF–Aux/IAA interactions.
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spelling pubmed-29358702010-09-13 Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.) Shen, ChenJia Wang, SuiKang Bai, YouHuang Wu, YunRong Zhang, SaiNa Chen, Ming Guilfoyle, Tom J. Wu, Ping Qi, YanHua J Exp Bot Research Papers Auxin response factors (ARFs) are key regulators of plant growth and development. Through interaction with auxin/indole acetic acid (Aux/IAA) proteins, they influence the expression of auxin response genes. An ARF gene family has been predicted in rice, but the functions of the individual structural domains of the OsARFs remain obscure. Bioinformatics was used to analyse the position of the DNA-binding domain (DBD), middle region (MR), and C-terminal dimerization domain (CTD) of OsARFs, and experimentally confirmed the presence of a classical monopartite nuclear localization signal (NLS) in the DBD. The DBD was shown to contribute to nuclear localization of OsARF proteins in addition to its known DNA-binding function. Interactions between 14 integrated OsARFs and 15 OsIAA proteins were tested using yeast two-hybrid assays. It was found that eight OsARF activators interacted with the 15 OsIAA proteins, while six OsARF repressors did not. The interactions between the MR+CTD or CTD of 10 OsARFs and 15 OsIAA proteins were also tested and the results were consistent with those of each intact OsARF, although some slight differences in interaction intensity were observed by α-galactosidase quantitative assays. The truncated CTD of OsARF11 did not interact with any OsIAA, implying that the CTD is required for ARF–IAA dimerization, and that the MR influences the interaction intensity in yeast. A subset of the interactions in yeast were also observed in tobacco plants using firefly luciferase complementation imaging assays, indicating that these interactions are specific in plants, and might have a special role in the auxin signalling response. This study provides new insight into the structure of OsARF proteins and ARF–Aux/IAA interactions. Oxford University Press 2010-09 2010-08-06 /pmc/articles/PMC2935870/ /pubmed/20693412 http://dx.doi.org/10.1093/jxb/erq208 Text en © 2010 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)
spellingShingle Research Papers
Shen, ChenJia
Wang, SuiKang
Bai, YouHuang
Wu, YunRong
Zhang, SaiNa
Chen, Ming
Guilfoyle, Tom J.
Wu, Ping
Qi, YanHua
Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.)
title Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.)
title_full Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.)
title_fullStr Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.)
title_full_unstemmed Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.)
title_short Functional analysis of the structural domain of ARF proteins in rice (Oryza sativa L.)
title_sort functional analysis of the structural domain of arf proteins in rice (oryza sativa l.)
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2935870/
https://www.ncbi.nlm.nih.gov/pubmed/20693412
http://dx.doi.org/10.1093/jxb/erq208
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