The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome

Victoria R Tenge; Abbey D Zuehlke; Neelima Shrestha; Jill L Johnson

doi:10.1128/EC.00170-14

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The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome

Journal article

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The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome

Victoria R Tenge, Abbey D Zuehlke, Neelima Shrestha and Jill L Johnson

Eukaryotic cell, Vol.14(1), pp.55-63

01/2015

DOI: https://doi.org/10.1128/EC.00170-14

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https://hdl.handle.net/2376/106173

PMCID: PMC4279014

PMID: 25380751

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Abstract

Protein Structure, Tertiary

Amino Acid Sequence

Molecular Chaperones - metabolism

Saccharomyces cerevisiae - genetics

Molecular Chaperones - genetics

Molecular Sequence Data

Ribosomes - metabolism

Saccharomyces cerevisiae - drug effects

Cyclophilins - genetics

Cyclophilins - metabolism

Molecular Chaperones - chemistry

Saccharomyces cerevisiae Proteins - genetics

Cinnamates - pharmacology

Saccharomyces cerevisiae - metabolism

Hygromycin B - pharmacology

Saccharomyces cerevisiae Proteins - metabolism

Protein Binding

Hygromycin B - analogs & derivatives

Cyclophilins - chemistry

Saccharomyces cerevisiae Proteins - chemistry

The abundant molecular chaperone Hsp90 is essential for the folding and stabilization of hundreds of distinct client proteins. Hsp90 is assisted by multiple cochaperones that modulate Hsp90's ATPase activity and/or promote client interaction, but the in vivo functions of many of these cochaperones are largely unknown. We found that Cpr6, Cpr7, and Cns1 interact with the intact ribosome and that Saccharomyces cerevisiae lacking CPR7 or containing mutations in CNS1 exhibited sensitivity to the translation inhibitor hygromycin. Cpr6 contains a peptidyl-prolyl isomerase (PPIase) domain and a tetratricopeptide repeat (TPR) domain flanked by charged regions. Truncation or alteration of basic residues near the carboxy terminus of Cpr6 disrupted ribosome interaction. Cns1 contains an amino-terminal TPR domain and a poorly characterized carboxy-terminal domain. The isolated carboxy-terminal domain was able to interact with the ribosome. Although loss of CPR6 does not cause noticeable growth defects, overexpression of CPR6 results in enhanced growth defects in cells expressing the temperature-sensitive cns1-G90D mutation (the G-to-D change at position 90 encoded by cns1). Cpr6 mutants that exhibit reduced ribosome interaction failed to cause growth defects, indicating that ribosome interaction is required for in vivo functions of Cpr6. Together, these results represent a novel link between the Hsp90 molecular-chaperone machine and protein synthesis.

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Title: The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome
Creators: Victoria R Tenge - Department of Biological Sciences, University of Idaho, Moscow, Idaho, USA
Abbey D Zuehlke - Department of Biological Sciences, University of Idaho, Moscow, Idaho, USA
Neelima Shrestha - Department of Biological Sciences, University of Idaho, Moscow, Idaho, USA
Jill L Johnson - Department of Biological Sciences, University of Idaho, Moscow, Idaho, USA jilljohn@uidaho.edu
Publication Details: Eukaryotic cell, Vol.14(1), pp.55-63
Academic Unit: UNKNOWN
Publisher: United States
Grant note: P30 GM103324 / NIGMS NIH HHS P30GM103324 / NIGMS NIH HHS
Identifiers: 99900546571001842
Language: English
Resource Type: Journal article