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A family of ubiquitin‐like proteins binds the ATPase domain of Hsp70‐like Stch
Author(s) -
Kaye Frederic J.,
Modi Sanjay,
Ivanovska Irena,
Koonin Eugene V.,
Thress Kenneth,
Kubo Akihito,
Kornbluth Sally,
Rose Mark D.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01135-2
Subject(s) - biology , saccharomyces cerevisiae , xenopus , ubiquitin , gene , complementary dna , hsp70 , microbiology and biotechnology , atpase , mutant , cell cycle , binding domain , peptide sequence , genetics , binding site , biochemistry , heat shock protein , enzyme
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 Δ rad23 Δ 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.