The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins

Victoria R Tenge; Jared Knowles; Jill L Johnson

doi:10.1371/journal.pone.0092569

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The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins

Journal article

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The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins

Victoria R Tenge, Jared Knowles and Jill L Johnson

PloS one, Vol.9(3), pp.e92569-e92569

2014

DOI: https://doi.org/10.1371/journal.pone.0092569

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https://hdl.handle.net/2376/104963

PMCID: PMC3960262

PMID: 24647762

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Abstract

Saccharomyces cerevisiae - metabolism

Ribosomal Proteins - genetics

Saccharomyces cerevisiae - genetics

Saccharomyces cerevisiae Proteins - metabolism

HSP90 Heat-Shock Proteins - metabolism

Protein Binding

Immunoblotting

Nuclear Proteins - metabolism

HSP90 Heat-Shock Proteins - genetics

Saccharomyces cerevisiae Proteins - genetics

Nuclear Proteins - genetics

Ribosomal Proteins - metabolism

The molecular chaperone Hsp90 buffers the effects of genetic variation by assisting the stabilization and folding of multiple clients critical for cell signaling and growth. We identified an interaction of Hsp90 and associated proteins with the essential nucleolar protein, Utp21, part of a large complex required for biogenesis of the small ribosomal subunit. The utp21-S602F mutation, which causes minor defects in otherwise wild-type yeast, exhibited severe or lethal growth defects when combined with mutations in Hsp90 or co-chaperones. WT Utp21 and Utp21-S602F exhibited similar interactions with Hsp90, and steady-state levels of WT Utp21 were reduced upon Hsp90 mutation or inhibition. Mutations in the human homolog of UTP21, WDR36, have been associated with adult-onset primary open-angle glaucoma, a leading cause of blindness worldwide. Three different mutant forms of Utp21 analogous to glaucoma-associated WDR36 mutations exhibit reduced levels in yeast cells expressing mutations in Hsp90 or associated chaperones, suggesting that Hsp90 and co-chaperones buffer the effects of those mutations.

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Title: The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins
Creators: Victoria R Tenge - Department of Biological Sciences and the Center for Reproductive Biology, University of Idaho, Moscow, Idaho, United States of America
Jared Knowles - Department of Biological Sciences and the Center for Reproductive Biology, University of Idaho, Moscow, Idaho, United States of America
Jill L Johnson - Department of Biological Sciences and the Center for Reproductive Biology, University of Idaho, Moscow, Idaho, United States of America
Publication Details: PloS one, Vol.9(3), pp.e92569-e92569
Academic Unit: UNKNOWN
Publisher: United States
Grant note: P20 GM103408 / NIGMS NIH HHS P20 RR016454 / NCRR NIH HHS
Identifiers: 99900546725301842
Language: English
Resource Type: Journal article