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

FEBS Letters

article

Zaur M. Kachaev¹  Lyubov A. Lebedeva¹  Alexander V. Shaposhnikov¹  James J. Moresco²  John R. Yates III²  Paul Schedl¹  Yulii V. Shidlovskii¹ 

[1] Institute of Gene Biology, Russian Academy of Sciences;Department of Chemical Physiology, The Scripps Research Institute;Department of Molecular Biology, Princeton University;I.M. Sechenov First Moscow State Medical University

关键词: capping;    Cbp80;    Paip2;    promoter;    protein complex;    transcription;   

DOI  :  10.1002/1873-3468.13391

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown