Document Detail


A role for Saccharomyces cerevisiae histone H2A in DNA repair.
MedLine Citation:
PMID:  11140636     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Histone proteins associate with and compact eukaryotic nuclear DNA to form chromatin. The basic unit of chromatin is the nucleosome, which is made up of 146 base pairs of DNA wrapped around two of each of four core histones, H2A, H2B, H3 and H4. Chromatin structure and its regulation are important in transcription and DNA replication. We therefore thought that DNA-damage signalling and repair components might also modulate chromatin structure. Here we have characterized a conserved motif in the carboxy terminus of the core histone H2A from Saccharomyces cerevisiae that contains a consensus phosphorylation site for phosphatidylinositol-3-OH kinase related kinases (PIKKs). This motif is important for survival in the presence of agents that generate DNA double-strand breaks, and the phosphorylation of this motif in response to DNA damage is dependent on the PIKK family member Mec1. The motif is not necessary for Mec1-dependent cell-cycle or transcriptional responses to DNA damage, but is required for efficient DNA double-strand break repair by non-homologous end joining. In addition, the motif has a role in determining higher order chromatin structure. Thus, phosphorylation of a core histone in response to DNA damage may cause an alteration of chromatin structure that facilitates DNA repair.
Authors:
J A Downs; N F Lowndes; S P Jackson
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Nature     Volume:  408     ISSN:  0028-0836     ISO Abbreviation:  Nature     Publication Date:    2000 Dec 21-28
Date Detail:
Created Date:  2001-01-03     Completed Date:  2001-01-25     Revised Date:  2009-06-02    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  1001-4     Citation Subset:  IM    
Affiliation:
The Wellcome Trust and Cancer Research Campaign, Institute of Cancer and Developmental Biology, and Department of Zoology, University of Cambridge, UK.
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MeSH Terms
Descriptor/Qualifier:
1-Phosphatidylinositol 3-Kinase / metabolism
Amino Acid Motifs
Amino Acid Sequence
Animals
Chromatin / chemistry,  metabolism
DNA Repair*
DNA, Fungal / physiology
Fungal Proteins / metabolism
Histones / genetics,  physiology*
Humans
Intracellular Signaling Peptides and Proteins
Molecular Sequence Data
Mutagenesis
Phosphorylation
Protein-Serine-Threonine Kinases
Saccharomyces cerevisiae / genetics*,  physiology
Saccharomyces cerevisiae Proteins*
Chemical
Reg. No./Substance:
0/Chromatin; 0/DNA, Fungal; 0/Fungal Proteins; 0/Histones; 0/Intracellular Signaling Peptides and Proteins; 0/Saccharomyces cerevisiae Proteins; EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 2.7.11.1/MEC1 protein, S cerevisiae; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/TEL1 protein, S cerevisiae

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


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