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An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae

机译:与酿酒酵母中的转录因子IIF相互作用的C末端域磷酸酶的重要组成部分

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摘要

One of the essential components of a phos- phatase that specifically dephosphorylates the Saccharomyces cerevisiae RNA polymerase II (RPII) large subunit C-terminal domain (CTD) is a novel polypeptide encoded by an essential gene termed FCP1. The Fcp1 protein is localized to the nucleus, and it binds the largest subunit of the yeast general transcription factor IIF (Tfg1). In vitro, transcription factor IIF stimulates phosphatase activity in the presence of Fcp1 and a second complementing fraction. Two distinct regions of Fcp1 are capable of binding to Tfg1, but the C-terminal Tfg1 binding domain is dispensable for activity in vivo and in vitro.
机译:磷酸酶的主要成分之一是特异性地将酿酒酵母RNA聚合酶II(RPII)大亚基C末端结构域(CTD)磷酸去磷酸化,这是一种由称为FCP1的必需基因编码的新型多肽。 Fcp1蛋白位于细胞核中,并与酵母一般转录因子IIF(Tfg1)的最大亚基结合。在体外,转录因子IIF在Fcp1和第二个互补部分的存在下刺激磷酸酶活性。 Fcp1的两个不同区域能够与Tfg1结合,但C端Tfg1结合域对于体内和体外活性是可有可无的。

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