Ansari Aseem Z, Ogirala Anuja, Ptashne Mark
Department of Biochemistry and Genome Center, University of Wisconsin, Madison, WI 53706, USA.
Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2346-9. doi: 10.1073/pnas.0409671102. Epub 2005 Feb 1.
The yeast cyclin-dependent kinase Srb10 phosphorylates various transcriptional activators as they activate transcription, and acidic transcriptional activating domains found on several activators directly bind Srb10. Here we show that the interaction between Srb10 (with its associated cyclin Srb11) and each of several different activating regions, in vitro, leads to the phosphorylation of peptide sequences attached to but outside of the activating regions themselves. In some cases, residues within the activating regions are also phosphorylated. The results define a mechanism by which a kinase is recruited to alternate substrates with diverse physiological consequences.
酵母细胞周期蛋白依赖性激酶Srb10在多种转录激活因子激活转录时对其进行磷酸化,并且在几种激活因子上发现的酸性转录激活结构域可直接结合Srb10。我们在此表明,Srb10(及其相关的细胞周期蛋白Srb11)与几个不同激活区域中的每一个之间的体外相互作用,会导致连接在激活区域本身之外但与之相连的肽序列发生磷酸化。在某些情况下,激活区域内的残基也会被磷酸化。这些结果确定了一种机制,通过该机制激酶被招募到具有不同生理后果的替代底物上。