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Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila
Author(s) -
Kachaev Zaur M.,
Lebedeva Lyubov A.,
Shaposhnikov Alexander V.,
Moresco James J.,
Yates John R.,
Schedl Paul,
Shidlovskii Yulii V.
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13391
Subject(s) - rna polymerase ii , microbiology and biotechnology , phosphorylation , messenger rna , elongation factor , protein subunit , transcription factor ii d , cytoplasm , transcription (linguistics) , biology , chemistry , rna , gene expression , biochemistry , rna polymerase , promoter , gene , ribosome , linguistics , philosophy
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‐ kD a 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.