Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms

Jill L Johnson; Celeste Brown

doi:10.1007/s12192-008-0058-9

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Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms

Journal article

Open access

Peer reviewed

Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms

Jill L Johnson and Celeste Brown

Cell stress & chaperones, Vol.14(1), pp.83-94

01/2009

DOI: https://doi.org/10.1007/s12192-008-0058-9

Handle:

https://hdl.handle.net/2376/109844

PMCID: PMC2673905

PMID: 18636345

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https://doi.org/10.1007/s12192-008-0058-9View

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Abstract

Amino Acid Sequence

Humans

Genome - genetics

Molecular Sequence Data

Eukaryotic Cells - metabolism

Phylogeny

Parasites - genetics

Genetic Variation

Sequence Homology, Amino Acid

Animals

HSP90 Heat-Shock Proteins - chemistry

HSP90 Heat-Shock Proteins - metabolism

Binding Sites

Proteome - metabolism

Hsp90 is critical for the regulation and activation of numerous client proteins critical for diverse functions such as cell growth, differentiation, and reproduction. Cytosolic Hsp90 function is dependent on a battery of co-chaperone proteins that regulate the ATPase activity of Hsp90 function or direct Hsp90 to interact with specific client proteins. Little is known about how Hsp90 complexes vary between different organisms and how this affects the scope of clients that are activated by Hsp90. This study determined whether ten distinct Hsp90 co-chaperones were encoded by genes in 19 disparate eukaryotic organisms. Surprisingly, none of the co-chaperones were present in all organisms. The co-chaperone Hop/Sti1 was most widely dispersed (18 out of 19 species), while orthologs of Cdc37, which is critical for the stability and activation of diverse protein kinases in yeast and mammals, were identified in only nine out of 19 species examined. The organism with the smallest proteome, Encephalitozoon cuniculi, contained only three of these co-chaperones, suggesting a correlation between client diversity and the complexity of the Hsp90 co-chaperone machine. Our results suggest co-chaperones are critical for cytosolic Hsp90 function in vivo, but that the composition of Hsp90 complexes varies depending on the specialized protein folding requirements of divergent species.

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Details

Title: Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
Creators: Jill L Johnson - Department of Microbiology, Molecular Biology and Biochemistry and the Center for Reproductive Biology, Moscow, ID 83844-3052, USA. jilljohn@uidaho.edu
Celeste Brown
Publication Details: Cell stress & chaperones, Vol.14(1), pp.83-94
Academic Unit: UNKNOWN
Publisher: Netherlands
Grant note: P20 RR015587 / NCRR NIH HHS P20 RR15587 / NCRR NIH HHS
Identifiers: 99900547179601842
Language: English
Resource Type: Journal article