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

Published

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

Pubmed Central 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