Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 282, Issue 2, Pages 956-967Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M511451200
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Funding
- FIC NIH HHS [R03 TW008143] Funding Source: Medline
- NICHD NIH HHS [T32-HD07505] Funding Source: Medline
- NIDDK NIH HHS [DK074377-01, 5P60 DK20572, DK46072] Funding Source: Medline
- NIGMS NIH HHS [T32-GM07315] Funding Source: Medline
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Transcription factor function can be modulated by post-translational modifications. Because the transcription factor CCAAT/enhancer-binding protein (C/EBP) beta associates with the nuclear coactivator p300, which contains acetyltransferase activity, acetylation of C/EBP beta was examined to understand its regulation and function. C/EBP beta is acetylated by acetyltransferases p300 and p300/CREB-binding protein associated factor. Endogenous C/EBP beta in 3T3-F442A preadipocytes is also recognized by an acetyl-lysine-specific antibody. Analysis of truncations of C/EBP beta and peptides based on C/EBP beta sequences identified multiple lysines within C/EBP beta that can be acetylated. Among these, a novel acetylation site at lysine 39 of C/EBP beta was identified. Mutation of Lys-39 to arginine or alanine impairs its acetylation and the ability of C/EBP beta to activate transcription at the promoters for C/EBP beta and c-fos. Different C/EBP beta-responsive promoters require different patterns of acetylated lysines in C/EBP beta for transcription activation. Furthermore, C/EBP beta acetylation was increased by growth hormone, and mutation of Lys-39 impaired growth hormone-stimulated c-fos promoter activation. These data suggest that acetylation of Lys-39 of C/EBP beta, alone or in combination with acetylation at other lysines, may play a role in C/EBP beta-mediated transcriptional activation.
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