An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae
An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae
复制标题
DOI：
10.1073/pnas.94.26.14300
复制
发表时间：
1997-12-23
影响因子：
11.1
通讯作者：
Greenblatt, J
中科院分区：
文献类型：
--
作者：
Archambault, J;Chambers, RS;Greenblatt, J
One of the essential components of a phosphatase 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, Sequence comparison reveals that residues 173-357 of Fcp1 correspond to an amino acid motif present in proteins of unknown function predicted in many organisms.
