Document Detail


Role for the molecular chaperones Zuo1 and Ssz1 in quorum sensing via activation of the transcription factor Pdr1.
MedLine Citation:
PMID:  22203981     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Zuo1 functions as a J-protein cochaperone of its partner Hsp70. In addition, the C terminus of Zuo1 and the N terminus of Ssz1, with which Zuo1 forms a heterodimer, can independently activate the Saccharomyces cerevisiae transcription factor pleiotropic drug resistance 1 (Pdr1). Here we report that activation of Pdr1 by Zuo1 or Ssz1 causes premature growth arrest of cells during the diauxic shift, as they adapt to the changing environmental conditions. Conversely, cells lacking Zuo1 or Ssz1 overgrow, arresting at a higher cell density, an effect overcome by activation of Pdr1. Cells lacking the genes encoding plasma membrane transporters Pdr5 and Snq2, two targets of Pdr1, also overgrow at the diauxic shift. Adding conditioned medium harvested from cultures of wild-type cells attenuated the overgrowth of both zuo1Δssz1Δ and pdr5Δsnq2Δ cells, suggesting the extracellular presence of molecules that signal growth arrest. In addition, our yeast two-hybrid analysis revealed an interaction between Pdr1 and both Zuo1 and Ssz1. Together, our results support a model in which (i) membrane transporters, encoded by Pdr1 target genes act to promote cell-cell communication by exporting quorum sensing molecules, in addition to playing a role in pleiotropic drug resistance; and (ii) molecular chaperones function at promoters to regulate this intercellular communication through their activation of the transcription factor Pdr1.
Authors:
Amy J Prunuske; Jeanette K Waltner; Peter Kuhn; Bohao Gu; Elizabeth Anne Craig
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2011-12-27
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  109     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-01-11     Completed Date:  2012-03-12     Revised Date:  2013-05-22    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  472-7     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.
Data Bank Information
Bank Name/Acc. No.:
GEO/GSE31693
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MeSH Terms
Descriptor/Qualifier:
ATP-Binding Cassette Transporters / metabolism
Chromatin Immunoprecipitation
Cycloheximide
DNA-Binding Proteins / metabolism*
Drug Resistance, Fungal / physiology
Gene Expression Regulation, Fungal / physiology*
HSP70 Heat-Shock Proteins / genetics,  metabolism*
Microarray Analysis
Molecular Chaperones / genetics,  metabolism*
Mutagenesis, Site-Directed
Quorum Sensing / physiology*
Saccharomyces cerevisiae / growth & development*,  metabolism
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Transcription Factors / metabolism*
Two-Hybrid System Techniques
Grant Support
ID/Acronym/Agency:
GM080931/GM/NIGMS NIH HHS; GM31107/GM/NIGMS NIH HHS; R01 GM031107-31/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/DNA-Binding Proteins; 0/HSP70 Heat-Shock Proteins; 0/Molecular Chaperones; 0/PDR1 protein, S cerevisiae; 0/PDR5 protein, S cerevisiae; 0/SNQ2 protein, S cerevisiae; 0/SSZ1 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Transcription Factors; 0/ZUO1 protein, S cerevisiae; 66-81-9/Cycloheximide
Comments/Corrections

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