FEBS Lett. 2000 Feb 11;467(2-3):348-55.

A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.

Kaye FJ, Modi S, Ivanovska I, Koonin EV, Thress K, Kubo A, Kornbluth S, Rose MD.

Source

Medicine Branch, Division of Clinical Sciences, National Cancer Institute and National Naval Medical Center, Bethesda, MD, USA. fkaye@helix.nih.gov

Abstract

We have isolated two human ubiquitin-like (UbL) proteins that bind to a short peptide within the ATPase domain of the Hsp70-like Stch protein. Chap1 is a duplicated homologue of the yeast Dsk2 gene that is required for transit through the G2/M phase of the cell cycle and expression of the human full-length cDNA restored viability and suppressed the G2/M arrest phenotype of dsk2Delta rad23Delta Saccharomyces cerevisiae mutants. Chap2 is a homologue for Xenopus scythe which is an essential component of reaper-induced apoptosis in egg extracts. While the N-terminal UbL domains were not essential for Stch binding, Chap1/Dsk2 contains a Sti1-like repeat sequence that is required for binding to Stch and is also conserved in the Hsp70 binding proteins, Hip and p60/Sti1/Hop. These findings extend the association between Hsp70 members and genes encoding UbL sequences and suggest a broader role for the Hsp70-like ATPase family in regulating cell cycle and cell death events.

PMID:: 10675567; [PubMed - indexed for MEDLINE]

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GENBANK/AF189009

Grant Support

R01 GM56518/GM/NIGMS NIH HHS/United States

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A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.
A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.
FEBS Lett. 2000 Feb 11 ;467(2-3):348-55.

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