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- Title
End-joining of reconstituted histone H2AX-containing chromatin in vitro by soluble nuclear proteins from human cells
- Authors
Siino, Joseph S.; Nazarov, Igor B.; Zalenskaya, Irina A.; Yau, Peter M.; Bradbury, E. Morton; Tomilin, Nikolai V.
- Abstract
Non-homologous end-joining is an important pathway for the repair of DNA double-strand breaks. This type of DNA break is followed by the rapid phosphorylation of Ser-139 in the histone variant H2AX to form γ-H2AX. Here we report efficient in vitro end-joining of reconstituted chromatin containing nucleosomes made with either H2A or H2AX. This reaction is catalyzed by nuclear extracts from human cells and this end-joining is not suppressed by the PI-3 kinase inhibitor wortmannin. During the end-joining reaction H2AX is phosphorylated at Ser-139 as detected by immunoblot with specific antibodies and this phosphorylation is inhibited by wortmannin. Therefore, in vitro the DNA end-joining reaction appears to be independent of H2AX phosphorylation.
- Subjects
PHOSPHORYLATION; ATOMIC force microscopy
- Publication
FEBS Letters, 2002, Vol 527, Issue 1-3, p105
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)03176-9