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

被引：128

作者：

Archambault, J

Chambers, RS

Kobor, MS

Ho, Y

Cartier, M

Bolotin, D

Andrews, B

Kane, CM ^{[1
]}

Greenblatt, J

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Div Biochem & Mol Biol, Berkeley, CA 94720 USA

[2] Univ Toronto, Banting & Best Dept Med Res, Toronto, ON M5G 1L6, Canada

[3] Univ Toronto, Dept Mol & Med Genet, Toronto, ON M5G 1L6, Canada

[4] Hosp Sick Children, Res Inst, Dept Genet, Toronto, ON M5G 1X8, Canada

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1997年 / 94卷 / 26期

关键词：

D O I：

10.1073/pnas.94.26.14300

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：14300 / 14305

页数：6

共 53 条

[1]

[Anonymous], METHOD ENZYMOL

[2] A SUPPRESSOR OF A HIS4 TRANSCRIPTIONAL DEFECT ENCODES A PROTEIN WITH HOMOLOGY TO THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASES [J].