Journal
DNA REPAIR
Volume 4, Issue 7, Pages 760-772Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.dnarep.2005.02.007
Keywords
xenopus; chromatin; CENP-A
Categories
Funding
- NCI NIH HHS [R37-CA43054] Funding Source: Medline
- NIGMS NIH HHS [R01GM33523, F32 GM069297-01, F32 GM069297-02, F32 GM069297-03, F32 GM069297-01] Funding Source: Medline
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CENP-A is an essential histone H3 variant found in all eukaryotes examined to date. To begin to determine how CENP-A is assembled into chromatin, we developed a binding assay using sperm chromatin in cell-free extract derived from Xenopus eggs, Our data suggest that the catalytic activities of an unidentified deoxycytidine deaminase and UNG2, a uracil DNA glycosylase, are involved in CENP-A assembly. In support of this model, inhibiting deoxycytidine deaminase with zebularine, or uracil DNA glycosylase with Ugi, uracil or UTP results in a lack of detectable CENP-A on sperm DNA. Conversely, inducing DNA damage increases the level of CENP-A detected on sperm chromatin. Our data suggest that base excision repair may be involved in assembly of this historic H3 variant, (c) 2005 Elsevier B.V. All rights reserved.
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