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Title: 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 Ga subunit in the heterotrimeric G protein complex. Some recent evidence indicate that XLG subunits operate along with its Gbg dimer in root morphology, stress responsiveness, and cytokinin induced development, however downstream targets of activated XLG proteins in the stress pathways are rarely known. In order 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. Furthermore, the subcellular localization of the XLG proteins in the nucleus, endosome, and plasma membrane is dependent on the specific interacting partner.
 [1] ;  [2] ;  [3]
  1. Northwest A&F Univ., Xianyang (China). College of Natural Resources and Environment; Univ. of North Carolina, Chapel Hill, NC (United States). Dept. of Biology
  2. Northwest A&F Univ., Xianyang (China). College of Natural Resources and Environment
  3. Univ. of North Carolina, Chapel Hill, NC (United States). Dept. of Biology and Dept. of Pharmacology
Publication Date:
Grant/Contract Number:
FG02-05ER15671; R01GM065989; MCB-0718202
Accepted Manuscript
Journal Name:
Frontiers in Plant Science
Additional Journal Information:
Journal Volume: 8; Journal ID: ISSN 1664-462X
Frontiers Research Foundation
Research Org:
Univ. of North Carolina, Chapel Hill, NC (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; arabidopsis; extra-large G protein; XLG protein interactome; salt stress; SZF; yeast two hybrid; NaCl
OSTI Identifier: