Spt5 Phosphorylation and the Rtf1 Plus3 Domain Promote Rtf1 Function through Distinct Mechanisms-Reference-Cited by-同舟云学术

Spt5 Phosphorylation and the Rtf1 Plus3 Domain Promote Rtf1 Function through Distinct Mechanisms

Published:2020-07-14 Issue:15 Volume:40 Page:
ISSN:0270-7306
Container-title:Molecular and Cellular Biology
language:en
Short-container-title:Mol Cell Biol

Author:

Chen Jennifer J.¹,Mbogning Jean¹,Hancock Mark A.¹²,Majdpour Dorsa¹,Madhok Manan¹,Nassour Hassan³,Dallagnol Juliana C.³,Pagé Viviane¹,Chatenet David³,Tanny Jason C.¹

Affiliation:

1. Department of Pharmacology and Therapeutics, McGill University, Montreal, Canada

2. McGill SPR-MS Facility, McGill University, Montreal, Canada

3. INRS-Centre Armand-Frappier, Groupe de Recherche en Ingénierie des Peptides et en Pharmacothérapie, Ville de Laval, Canada

Abstract

Rtf1 is a conserved RNA polymerase II (RNAPII) elongation factor that promotes cotranscriptional histone modification, RNAPII transcript elongation, and mRNA processing. Rtf1 function requires the phosphorylation of Spt5, an essential RNAPII processivity factor. Spt5 is phosphorylated within its C-terminal domain (CTD) by cyclin-dependent kinase 9 (Cdk9), the catalytic component of positive transcription elongation factor b (P-TEFb). Rtf1 recognizes phosphorylated Spt5 (pSpt5) through its Plus3 domain.

Funder

Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada

Gouvernement du Canada | Canadian Institutes of Health Research

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

Link

https://journals.asm.org/doi/pdf/10.1128/MCB.00150-20

Reference48 articles.

1. HIV-1 Tat Assembles a Multifunctional Transcription Elongation Complex and Stably Associates with the 7SK snRNP

2. Pharmacological targeting of CDK9 in cardiac hypertrophy