Document Detail


Radiosensitization of yeast cells by inhibition of histone h4 acetylation.
MedLine Citation:
PMID:  18959465     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Deletion of genes for proteins involved in histone H4 acetylation produces sensitivity to DNA-damaging agents in both Saccharomyces cerevisiae and mammalian cells. In the present studies, we show that treating wild-type yeast cells with histone acetyl transferase (HAT) inhibitors, which are chemicals that cause a global decrease in histone H4 acetylation, sensitizes the cells to ionizing radiation. Using HAT inhibitors, we have placed histone H4 acetylation into the RAD51-mediated homologous recombination repair pathway. We further show that yeast cells with functionally defective HAT proteins have normal phospho-H2A (gamma-H2A) induction after irradiation but a reduced rate of loss of gamma-H2A. This argues that HAT-defective cells are able to detect DNA double-strand breaks normally but have a defect in the repair of these lesions. We also show that cells treated with HAT inhibitors have intact G1 and G2 checkpoints after exposure to ionizing radiation, suggesting that G1 and G2 checkpoint activation is independent of histone H4 acetylation.
Authors:
Suisui Song; Kelly E McCann; J Martin Brown
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Radiation research     Volume:  170     ISSN:  0033-7587     ISO Abbreviation:  Radiat. Res.     Publication Date:  2008 Nov 
Date Detail:
Created Date:  2008-10-30     Completed Date:  2008-12-04     Revised Date:  2014-09-08    
Medline Journal Info:
Nlm Unique ID:  0401245     Medline TA:  Radiat Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  618-27     Citation Subset:  IM; S    
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MeSH Terms
Descriptor/Qualifier:
Acetylation
DNA Repair / drug effects
Enzyme Inhibitors / pharmacology*
G1 Phase / drug effects
G2 Phase / drug effects
Histone Acetyltransferases / antagonists & inhibitors*
Histones / metabolism*
Radiation Tolerance*
Recombination, Genetic
Saccharomyces cerevisiae / metabolism,  radiation effects*
Grant Support
ID/Acronym/Agency:
P01 CA082566/CA/NCI NIH HHS; P01 CA082566-01A1/CA/NCI NIH HHS; P01 CA082566-01A10002/CA/NCI NIH HHS; P01 CA082566-01A19001/CA/NCI NIH HHS; P01 CA082566-02/CA/NCI NIH HHS; P01 CA082566-020002/CA/NCI NIH HHS; P01 CA082566-029001/CA/NCI NIH HHS; P01 CA082566-03/CA/NCI NIH HHS; P01 CA082566-030002/CA/NCI NIH HHS; P01 CA082566-039001/CA/NCI NIH HHS; P01 CA082566-04A1/CA/NCI NIH HHS; P01 CA082566-04A10002/CA/NCI NIH HHS; P01 CA082566-04A15215/CA/NCI NIH HHS; P01 CA082566-05/CA/NCI NIH HHS; P01 CA082566-050002/CA/NCI NIH HHS; P01 CA082566-06/CA/NCI NIH HHS; P01 CA082566-060002/CA/NCI NIH HHS; P01 CA082566-07/CA/NCI NIH HHS; P01 CA082566-070002/CA/NCI NIH HHS; P01 CA082566-08/CA/NCI NIH HHS; P01 CA082566-080002/CA/NCI NIH HHS; P01 CA82566/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Enzyme Inhibitors; 0/Histones; EC 2.3.1.48/Histone Acetyltransferases
Comments/Corrections

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


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