TY - JOUR
AU - 
AB - Downloaded from genesdev.cshlp.org on October 31, 2021 - Published by Cold Spring Harbor Laboratory Press Pin1 modulates the structure and function of human RNA polymerase II 1 2 3 3 1,4 Yu-Xin Xu, Yutaka Hirose, Xiao Zhen Zhou, Kun Ping Lu, and James L. Manley 1 2 Department of Biological Sciences, Columbia University, New York, New York 10027, USA; Department of Molecular and Cellular Biology, Kanazawa University, Kanazawa 920-0934, Japan; Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA The C-terminal domain of the RNA polymerase (RNAP) II largest subunit (CTD) plays critical roles both in transcription of mRNA precursors and in the processing reactions needed to form mature mRNAs. The CTD undergoes dynamic changes in phosphorylation during the transcription cycle, and this plays a significant role in coordinating its multiple activities. But how these changes themselves are regulated is not well understood. Here we show that the peptidyl-prolyl isomerase Pin1 influences the phosphorylation status of the CTD in vitro by inhibiting the CTD phosphatase FCP1 and stimulating CTD phosphorylation by cdc2/cyclin B. This −/− is reflected in vivo by accumulation of hypophosphorylated RNAP II in pin1 cells, and of a novel hyper-hyperphosphorylated 
TI - Pin1 modulates the structure and function of human RNA polymerase II
JF - Genes & Development
DO - 10.1101/gad.1135503
DA - 2003-01-01
UR - https://www.deepdyve.com/lp/unpaywall/pin1-modulates-the-structure-and-function-of-human-rna-polymerase-ii-34QuvbF6Sm
DP - DeepDyve
ER -