Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair
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منابع مشابه
Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair
The presence of phosphorylated histone H2AX (γ-H2AX) is associated with the local activation of DNA-damage repair pathways. Although γ-H2AX deregulation in cancer has previously been reported, the molecular mechanism involved and its relationship with other histone modifications remain largely unknown. Here we find that the histone methyltransferase SUV39H2 methylates histone H2AX on lysine 134...
متن کاملHistone H2AX in DNA repair
In eucaryotic cells, DNA is bound to various proteins and forms a complex nucleoprotein structure called chromatin. Indispensable and ubiquitous chromatin components are histones, small proteins of highly conserved primary structure. Two molecules of each H2A, H2B, H3 and H4 type, form the nucleosomal core around which a 146 base pair (bp) stretch of DNA is wrapped. Histone H1 is bound to about...
متن کاملDNA Repair: The Importance of Phosphorylating Histone H2AX
How phosphorylated histone H2AX, known as gamma-H2AX, functions in the cellular response to DNA double-strand breaks is the subject of intensive investigation. Recent research in yeast and mammalian cells shows that gamma-H2AX facilitates post-replicational DNA repair by recruiting cohesin, a protein complex that holds sister chromatids together.
متن کاملA critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
BACKGROUND The response of eukaryotic cells to double-strand breaks in genomic DNA includes the sequestration of many factors into nuclear foci. Recently it has been reported that a member of the histone H2A family, H2AX, becomes extensively phosphorylated within 1-3 minutes of DNA damage and forms foci at break sites. RESULTS In this work, we examine the role of H2AX phosphorylation in focus...
متن کاملHistone H2AX is phosphorylated at sites of retroviral DNA integration but is dispensable for postintegration repair.
The histone variant H2AX is rapidly phosphorylated (denoted gammaH2AX) in large chromatin domains (foci) flanking double strand DNA (dsDNA) breaks that are produced by ionizing radiation or genotoxic agents and during V(D)J recombination. H2AX-deficient cells and mice demonstrate increased sensitivity to dsDNA break damage, indicating an active role for gammaH2AX in DNA repair; however, gammaH2...
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ژورنال
عنوان ژورنال: Nature Communications
سال: 2014
ISSN: 2041-1723
DOI: 10.1038/ncomms6691