| 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 |
Related Documents
:
|
15533935 - Association of nasp with hsp90 in mouse spermatogenic cells: stimulation of atpase acti... 3753905 - N-butyrate alters chromatin accessibility to dna repair enzymes. 17405795 - Role of histone modification in chromatin dynamics. 18336735 - Expression of cd38 in human neuroblastoma sh-sy5y cells. 122545 - Modification of erythrocyte physicochemical properties by millimolar concentrations of ... 14961915 - Granular cell basal cell carcinoma. |
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: 2011-09-26 |
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 |
Affiliation:
|
Department of Radiation Oncology, Division of Radiation and Cancer Biology, Stanford University of School of Medicine, Stanford, California 94305-5152, USA. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| 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 CA082566-01A1/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
Previous Document: Radiation damage to a DNA-binding protein. Combined circular dichroism and molecular dynamics simula...
Next Document: Generation of oxygen deficiency in cell culture using a two-enzyme system to evaluate agents targeti...