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CTBP regulates the early SEC assembly prior to onset of transcription elongation
Author(s) -
Byun Jung S,
Gardner Kevin
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.837.2
Subject(s) - chromatin , histone , microbiology and biotechnology , bromodomain , transcription (linguistics) , chemistry , transcription factor , histone acetyltransferase , phd finger , nuclear protein , chromatin remodeling , gene , biology , biochemistry , zinc finger , linguistics , philosophy
The C‐terminal binding proteins (CtBP1 and CtBP2) are a dimeric family of proteins encoded by two genes, CtBP1 and CtBP2 that play various roles in cell differentiation, wound healing and EMT. One member of the dimer functions to bind numerous chromatin sequence‐specific transcription factors, while the other member recruits several different chromatin modifying complexes. In this way, CtBP has a broad potential to influence the epigenetic landscape of the nucleus. CtBP shares many amino acid homology with NADH‐dependent 2 hydroxyacid dehydrogenase and previous report suggested that CtBP has a ~ 100 fold higher nanomolar affinity for NADH than NAD+ and nuclear NADH induces conformational change in CtBP. It has been known that CtBP1 physically associates with the bromodomain of histone acetyltransferase of p300 and regulates the direct interaction between the bromodomain of p300 and acetylated histones in an NADH‐dependent manner. We found CtBP forms complexes with p300 in resting cells of HEK293ET and CtBP depletion increases early elongation complex assembly and early mRNA transcription. We also showed CtBP overexpress repressed immediate early gene expression by attenuating early elongation and CtBP depletion increased the duration of immediate early transcription.