Journal
FEBS LETTERS
Volume 467, Issue 2-3, Pages 348-352Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01135-2
Keywords
cell cycle; Hsp70; Stch; ubiquitin-like gene
Funding
- NIGMS NIH HHS [R01 GM052526, R01 GM56518] Funding Source: Medline
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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 dsk2 Delta rad23 Delta Saccharomyces cerevisiae mutants. Chap2 is a homologue for Xenopus scythe which is an essential component of reaper-induced apoptosis in egg extracts, While the S-terminal UbL domains were not essential for Stch binding, Chap1/Dsk2 contains a Sti1-like repeat sequence that is required far 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, (C) 2000 Federation of European Biochemical Societies.
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