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AID-dependent histone acetylation is detected in immunoglobulin S regions

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Title: AID-dependent histone acetylation is detected in immunoglobulin S regions
Author(s): Wang, Lili; Whang, Naree; Wuerffel, Robert; Kenter, Amy L.
Subject(s): ChIP, chromatin immunoprecipitation AID, activation-induced deaminase class-switch recombination induced cytidine deaminase
Abstract: Class switch recombination (CSR) is regulated by the expression of activation-induced deaminase ( AID) and germline transcripts (GLTs). AID-dependent double-strand breaks (DSBs) are introduced into switch ( S) regions and stimulate CSR. Although histone acetylation (Ac) has been well documented in transcription regulation, its role in DNA damage repair remains largely unexplored. The 1B4.B6 B cell line and normal splenic B cells were activated to undergo CSR and analyzed for histone Ac by chromatin immunoprecipitation (ChIP). A detailed study of the I gamma 3-S gamma 3-C gamma 3 locus demonstrated that acetylated histones are focused to the I gamma 3 exon and the S gamma 3 region but not to the intergenic areas. Histone H3 Ac is strongly correlated with GLT expression at four S regions, whereas H4 Ac was better associated with B cell activation and AID expression. To more directly examine the relationship between H4 Ac and AID, LPS-activated AID KO and WT B cells were analyzed and express comparable levels of GLTs. In AID-deficient B cells, both histones H3 and H4 are reduced where H4 is more severely affected as compared with WT cells. Our findings raise the intriguing possibility that histone H4 Ac at S regions is a marker for chromatin modifications associated with DSB repair during CSR.
Issue Date: 2006-01-17
Publisher: Rockefeller University Press
Citation Info: Wang, L. L., N. Whang, R. Wuerffel, and A. L. Kenter, 2006, AID-dependent histone acetylation is detected in immunoglobulin S regions: Journal of Experimental Medicine, v. 203, no. 1, p. 215-226.
Type: Article
Description: Copyright: [version in Indigo preceded by list of corections to production errors]
ISSN: 0022-1007
Date Available in INDIGO: 2009-06-17

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