| First Author | Bradney C | Year | 2003 |
| Journal | J Biol Chem | Volume | 278 |
| Issue | 4 | Pages | 2370-6 |
| PubMed ID | 12435739 | Mgi Jnum | J:156241 |
| Mgi Id | MGI:4419089 | Doi | 10.1074/jbc.M211464200 |
| Citation | Bradney C, et al. (2003) Regulation of E2A activities by histone acetyltransferases in B lymphocyte development. J Biol Chem 278(4):2370-6 |
| abstractText | Genetic studies have demonstrated that the basic helix-loop-helix protein E2A is an essential transcription factor in B lymphocyte lineage commitment and differentiation. However, the mechanism underlying E2A-mediated transcription regulation is not fully understood. Here, we investigated the physical and genetic interactions between E2A and co-activators histone acetyltransferases (HATs) in B cells. Gel filtration analysis of human pre-B cell nuclear extract showed that E2A co-elutes with the HATs p300, CBP, and PCAF. A co-immunoprecipitation assay further demonstrated that a fraction of endogenous E2A proteins is associated with each of the three HATs. We show that these HATs acetylate E2A in vitro, enhance E2A-mediated transcription activity, and promote nuclear retention of E2A proteins. A catalytic mutation of p300 completely abrogates the ability of p300 to acetylate E2A and to promote E2A nuclear retention in 293T cells. A breeding test between E2A heterozygous mice and p300 heterozygous mice demonstrated that these two genes interact for proper B cell development. Collectively, these results suggest that E2A and HATs collaboratively regulate B cell development. |
