TY - JOUR
T1 - Regulation of histone H4 acetylation by transcription factor E2A in Ig gene conversion
AU - Kitao, Hiroyuki
AU - Kimura, Masayo
AU - Yamamoto, Kazuhiko
AU - Seo, Hidetaka
AU - Namikoshi, Keiko
AU - Agata, Yasutoshi
AU - Ohta, Kunihiro
AU - Takata, Minoru
PY - 2008/2
Y1 - 2008/2
N2 - Recent studies implicate the transcription factor E2A in Ig diversification such as somatic hypermutation or gene conversion (GCV). GCV also requires active Ig transcription, expression of the activation-induced deaminase (AID) and a set of homologous recombination factors. We have disrupted the E2A gene in the chicken B-cell line DT40 and found greatly diminished rate of GCV without changes in the levels of transcripts from AID and Ig heavy chain or Ig light chain (IgL) genes. However, chromatin immunoprecipitation analysis revealed that the loss of E2A accompanies drastically reduced acetylation levels of the histone H4 in rearranged IgL locus. Furthermore, the defects in GCV were restored by trichostatin A treatment, which raised H4 acetylation to the normal levels. Thus, E2A may contribute to GCV by maintaining histone acetylation, which could be a prerequisite for targeting or full deaminase function of AID.
AB - Recent studies implicate the transcription factor E2A in Ig diversification such as somatic hypermutation or gene conversion (GCV). GCV also requires active Ig transcription, expression of the activation-induced deaminase (AID) and a set of homologous recombination factors. We have disrupted the E2A gene in the chicken B-cell line DT40 and found greatly diminished rate of GCV without changes in the levels of transcripts from AID and Ig heavy chain or Ig light chain (IgL) genes. However, chromatin immunoprecipitation analysis revealed that the loss of E2A accompanies drastically reduced acetylation levels of the histone H4 in rearranged IgL locus. Furthermore, the defects in GCV were restored by trichostatin A treatment, which raised H4 acetylation to the normal levels. Thus, E2A may contribute to GCV by maintaining histone acetylation, which could be a prerequisite for targeting or full deaminase function of AID.
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U2 - 10.1093/intimm/dxm140
DO - 10.1093/intimm/dxm140
M3 - Article
C2 - 18182382
AN - SCOPUS:39049130844
SN - 0953-8178
VL - 20
SP - 277
EP - 284
JO - International immunology
JF - International immunology
IS - 2
ER -