Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms.
Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms.
复制标题
组蛋白 H3 磷酸化可以通过不同的启动子特异性机制促进 TBP 募集。
DOI：
10.1038/sj.emboj.7600577
复制
发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Berger,ShelleyL
中科院分区：
文献类型：
--
作者：
Lo,Wan-Sheng;Gamache,EricR;Henry,KarlW;Yang,David;Pillus,Lorraine;Berger,ShelleyL
Histone phosphorylation influences transcription, chromosome condensation, DNA repair and apoptosis. Previously, we showed that histone H3 Ser10 phosphorylation (pSer10) by the yeast Snf1 kinase regulatesINO1gene activation in part via Gcn5/SAGA complex‐mediated Lys14 acetylation (acLys14). How such chromatin modification patterns develop is largely unexplored. Here we examine the mechanisms surrounding pSer10 atINO1, and atGAL1, which herein is identified as a new regulatory target of Snf1/pSer10. Snf1 behaves as a classic coactivator in its recruitment by DNA‐bound activators, and in its role in modifying histones and recruiting TATA‐binding protein (TBP). However, one important difference in Snf1 functionin vivoat these promoters is that SAGA recruitment atINO1requires histone phosphorylation via Snf1, whereas atGAL1, SAGA recruitment is independent of histone phosphorylation. In addition, theGAL1activator physically interacts with both Snf1 and SAGA, whereas theINO1activator interacts only with Snf1. Thus, atINO1, pSer10's role in recruiting SAGA may substitute for recruitment by DNA‐bound activator. Our results emphasize that histone modifications share general functions between promoters, but also acquire distinct roles tailored for promoter‐specific requirements.
