Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae

Gary Flom; Jared Weekes; Jill L Johnson

doi:10.1007/s00294-005-0580-6

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Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae

Journal article

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Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae

Gary Flom, Jared Weekes and Jill L Johnson

Current genetics, Vol.47(6), pp.368-380

06/2005

DOI: https://doi.org/10.1007/s00294-005-0580-6

Handle:

https://hdl.handle.net/2376/116670

PMCID: PMC2267864

PMID: 15871019

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Abstract

Saccharomyces cerevisiae - physiology

Saccharomyces cerevisiae - genetics

DNA Repair

HSP90 Heat-Shock Proteins - physiology

Transcription, Genetic

HSP90 Heat-Shock Proteins - genetics

Saccharomyces cerevisiae Proteins - physiology

Mutation

Saccharomyces cerevisiae Proteins - genetics

Transcription Factor TFIIH

DNA Helicases - physiology

Hsp90 is an essential molecular chaperone that is critical for the activity of diverse cellular proteins. Hsp90 functions with a number of co-chaperone proteins, including Sti1/Hop. We conducted a genetic screen in Saccharomyces cerevisiae to isolate mutations that exhibit enhanced growth defects in the absence of STI1. We obtained mutations in genes encoding components of the Hsp90 chaperone machine, HSC82, CPR7 and YDJ1, and two essential genes, SSL2 and UTP21, not previously linked to Hsp90. Ssl2, the yeast homologue of XPB, is an ATP-dependent DNA helicase that is a component of the TFIIH multiprotein complex and has dual functions in transcription and DNA repair. In order to determine whether Ssl2 function is dependent on Hsp90, we further examined the interaction between Ssl2 and Hsp90. Multiple mutant alleles of SSL2 exhibited a pronounced growth defect when co-expressed with a mutant allele of Hsp90. In addition, isolation of Ssl2 protein resulted in the co-purification of Hsp90 and Sti1, suggesting that Ssl2 and Hsp90 are in the same protein complexes in vivo. These results suggest a novel role for Hsp90 in the essential cellular functions of transcription and DNA repair.

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Title: Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae
Creators: Gary Flom - Department of Microbiology, Molecular Biology and Biochemistry, Center for Reproductive Biology, University of Idaho, Moscow, ID 83844-3052, USA
Jared Weekes
Jill L Johnson
Publication Details: Current genetics, Vol.47(6), pp.368-380
Academic Unit: UNKNOWN
Publisher: United States
Grant note: P20 RR016454 / NCRR NIH HHS P20 RR015587-050010 / NCRR NIH HHS P20 RR015587-060010 / NCRR NIH HHS P20 RR015587 / NCRR NIH HHS P20 RR16454 / NCRR NIH HHS P20 RR15587 / NCRR NIH HHS
Identifiers: 99900547758101842
Language: English
Resource Type: Journal article