Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila.

TitlePaip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila.
Publication TypeJournal Article
Year of Publication2019
AuthorsKachaev, ZM, Lebedeva, LA, Shaposhnikov, AV, Moresco, JJ, Yates, JR, Schedl, P, Shidlovskii, YV
JournalFEBS Lett
Volume593
Issue10
Pagination1102-1112
Date Published2019 05
ISSN1873-3468
KeywordsAnimals, Cell Line, DNA, Drosophila melanogaster, Drosophila Proteins, Gene Expression Regulation, Nuclear Cap-Binding Protein Complex, Phosphorylation, Poly(A)-Binding Proteins, Promoter Regions, Genetic, Protein Processing, Post-Translational, RNA Polymerase II
Abstract

<p>The Paip2 protein is a factor regulating mRNA translation and stability in the cytoplasm. It has also been found in the nuclei of several cell types in Drosophila. Here, we aim to elucidate the functions of Paip2 in the cell nucleus. We find that nuclear Paip2 is a component of an ~300-kDa protein complex. Paip2 interacts with mRNA capping factor and factors of RNA polymerase II (Pol II) transcription initiation and early elongation. Paip2 functionally cooperates with the Cbp80 subunit of the cap-binding complex, with both proteins ensuring proper Pol II C-terminal domain (CTD) Ser5 phosphorylation at the promoter. Thus, Paip2 is a novel player at the stage of mRNA capping and early Pol II elongation.</p>
DOI10.1002/1873-3468.13391
Alternate JournalFEBS Lett.
PubMed ID31001806
PubMed Central IDPMC6538421
Grant ListP41 GM103533 / GM / NIGMS NIH HHS / United States
16-14-10346 / / Russian Science Foundation / International
R35 GM126975 / GM / NIGMS NIH HHS / United States