A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.
Journal Article (Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Kaye, FJ; Modi, S; Ivanovska, I; Koonin, EV; Thress, K; Kubo, A; Kornbluth, S; Rose, MD
Published Date
- February 2000
Published In
Volume / Issue
- 467 / 2-3
Start / End Page
- 348 - 355
PubMed ID
- 10675567
Electronic International Standard Serial Number (EISSN)
- 1873-3468
International Standard Serial Number (ISSN)
- 0014-5793
Digital Object Identifier (DOI)
- 10.1016/s0014-5793(00)01135-2
Language
- eng