Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization

The three-member family of Arabidopsis extra-large G proteins (XLG1-3) defines the prototype of an atypical Gα subunit in the heterotrimeric G protein complex. Recent evidence indicate that XLG subunits operate along with its Gβγ dimer in root morphology, stress responsiveness, and cytokinin induced...

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Main Authors: Ying Liang, Yajun Gao, Alan M. Jones
Format: Article
Language:English
Published: Frontiers Media S.A. 2017-06-01
Series:Frontiers in Plant Science
Subjects:
SZF
Online Access:http://journal.frontiersin.org/article/10.3389/fpls.2017.01015/full
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spelling doaj-a179296ea5b04ac98e285b357bfc43962020-11-24T22:43:55ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2017-06-01810.3389/fpls.2017.01015260095Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular LocalizationYing Liang0Ying Liang1Yajun Gao2Alan M. Jones3Alan M. Jones4College of Natural Resources and Environment, Northwest A&F UniversityXianyang, ChinaDepartment of Biology University of North Carolina at Chapel HillChapel Hill, NC, United StatesCollege of Natural Resources and Environment, Northwest A&F UniversityXianyang, ChinaDepartment of Biology University of North Carolina at Chapel HillChapel Hill, NC, United StatesDepartment of Pharmacology, University of North Carolina at Chapel HillChapel Hill, NC, United StatesThe three-member family of Arabidopsis extra-large G proteins (XLG1-3) defines the prototype of an atypical Gα subunit in the heterotrimeric G protein complex. Recent evidence indicate that XLG subunits operate along with its Gβγ dimer in root morphology, stress responsiveness, and cytokinin induced development, however downstream targets of activated XLG proteins in the stress pathways are rarely known. To assemble a set of candidate XLG-targeted proteins, a yeast two-hybrid complementation-based screen was performed using XLG protein baits to query interactions between XLG and partner protein found in glucose-treated seedlings, roots, and Arabidopsis cells in culture. Seventy two interactors were identified and >60% of a test set displayed in vivo interaction with XLG proteins. Gene co-expression analysis shows that >70% of the interactors are positively correlated with the corresponding XLG partners. Gene Ontology enrichment for all the candidates indicates stress responses and posits a molecular mechanism involving a specific set of transcription factor partners to XLG. Genes encoding two of these transcription factors, SZF1 and 2, require XLG proteins for full NaCl-induced expression. The subcellular localization of the XLG proteins in the nucleus, endosome, and plasma membrane is dependent on the specific interacting partner.http://journal.frontiersin.org/article/10.3389/fpls.2017.01015/fullArabidopsisextra-large G proteinXLG protein interactomesalt stressSZFyeast two hybrid
collection DOAJ
language English
format Article
sources DOAJ
author Ying Liang
Ying Liang
Yajun Gao
Alan M. Jones
Alan M. Jones
spellingShingle Ying Liang
Ying Liang
Yajun Gao
Alan M. Jones
Alan M. Jones
Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization
Frontiers in Plant Science
Arabidopsis
extra-large G protein
XLG protein interactome
salt stress
SZF
yeast two hybrid
author_facet Ying Liang
Ying Liang
Yajun Gao
Alan M. Jones
Alan M. Jones
author_sort Ying Liang
title Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization
title_short Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization
title_full Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization
title_fullStr Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization
title_full_unstemmed Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization
title_sort extra large g-protein interactome reveals multiple stress response function and partner-dependent xlg subcellular localization
publisher Frontiers Media S.A.
series Frontiers in Plant Science
issn 1664-462X
publishDate 2017-06-01
description The three-member family of Arabidopsis extra-large G proteins (XLG1-3) defines the prototype of an atypical Gα subunit in the heterotrimeric G protein complex. Recent evidence indicate that XLG subunits operate along with its Gβγ dimer in root morphology, stress responsiveness, and cytokinin induced development, however downstream targets of activated XLG proteins in the stress pathways are rarely known. To assemble a set of candidate XLG-targeted proteins, a yeast two-hybrid complementation-based screen was performed using XLG protein baits to query interactions between XLG and partner protein found in glucose-treated seedlings, roots, and Arabidopsis cells in culture. Seventy two interactors were identified and >60% of a test set displayed in vivo interaction with XLG proteins. Gene co-expression analysis shows that >70% of the interactors are positively correlated with the corresponding XLG partners. Gene Ontology enrichment for all the candidates indicates stress responses and posits a molecular mechanism involving a specific set of transcription factor partners to XLG. Genes encoding two of these transcription factors, SZF1 and 2, require XLG proteins for full NaCl-induced expression. The subcellular localization of the XLG proteins in the nucleus, endosome, and plasma membrane is dependent on the specific interacting partner.
topic Arabidopsis
extra-large G protein
XLG protein interactome
salt stress
SZF
yeast two hybrid
url http://journal.frontiersin.org/article/10.3389/fpls.2017.01015/full
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