Document Detail


Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1.
MedLine Citation:
PMID:  11172707     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The evolutionarily conserved yeast checkpoint protein kinase Rad53 regulates cell cycle progression, transcription, and DNA repair in response to DNA damage. To uncover potential regulatory targets of Rad53, we identified proteins physically associated with it in vivo using protein affinity purification and tandem mass spectrometry. Here we report that Rad53 interacts in a dynamic functional manner with Asf1, a chromatin assembly factor recently shown to mediate deposition of acetylated histones H3 and H4 onto newly replicated DNA. Biochemical and molecular genetic studies suggest that Asf1 is an important target of the Rad53-dependent DNA damage response and that Rad53 may directly regulate chromatin assembly during DNA replication and repair.
Authors:
A Emili; D M Schieltz; J R Yates; L H Hartwell
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular cell     Volume:  7     ISSN:  1097-2765     ISO Abbreviation:  Mol. Cell     Publication Date:  2001 Jan 
Date Detail:
Created Date:  2001-02-22     Completed Date:  2001-03-22     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  13-20     Citation Subset:  IM    
Affiliation:
Division of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA. andrew.emili@utoronto.ca
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MeSH Terms
Descriptor/Qualifier:
Cell Cycle / genetics
Cell Cycle Proteins / metabolism*
Chromatin / genetics,  metabolism*
DNA Damage / physiology*
DNA Replication / physiology
DNA, Fungal / physiology
Genes, cdc / physiology*
Histones / metabolism
Molecular Chaperones
Phosphorylation
Protein Binding / genetics
Protein Kinases / metabolism*
Protein-Serine-Threonine Kinases*
Saccharomyces cerevisiae Proteins*
Yeasts
Grant Support
ID/Acronym/Agency:
P41RR11823/RR/NCRR NIH HHS; R37-GM11823-02/GM/NIGMS NIH HHS; R37-GM17709/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/ASF1 protein, S cerevisiae; 0/Cell Cycle Proteins; 0/Chromatin; 0/DNA, Fungal; 0/Histones; 0/Molecular Chaperones; 0/Saccharomyces cerevisiae Proteins; EC 2.7.-/Protein Kinases; EC 2.7.1.-/RAD53 protein, S cerevisiae; EC 2.7.11.1/Protein-Serine-Threonine Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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