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

Zaur M. Kachaev; Lyubov A. Lebedeva; Alexander V. Shaposhnikov; James J. Moresco; John R. Yates; Paul Schedl; Yulii V. Shidlovskii

doi:10.1002/1873-3468.13391

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

Zaur M. Kachaev, Lyubov A. Lebedeva, Alexander V. Shaposhnikov, James J. Moresco, John R. Yates, Paul Schedl, Yulii V. Shidlovskii

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	1102-1112
Number of pages	11
Journal	FEBS Letters
Volume	593
Issue number	10
DOIs	https://doi.org/10.1002/1873-3468.13391
State	Published - May 2019
Externally published	Yes

Keywords

Cbp80
Paip2
capping
promoter
protein complex
transcription

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1002/1873-3468.13391

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

abstract = "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.",

keywords = "Cbp80, Paip2, capping, promoter, protein complex, transcription",

author = "Kachaev, {Zaur M.} and Lebedeva, {Lyubov A.} and Shaposhnikov, {Alexander V.} and Moresco, {James J.} and Yates, {John R.} and Paul Schedl and Shidlovskii, {Yulii V.}",

note = "Publisher Copyright: {\textcopyright} 2019 Federation of European Biochemical Societies.",

year = "2019",

month = may,

doi = "10.1002/1873-3468.13391",

language = "English (US)",

volume = "593",

pages = "1102--1112",

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T1 - Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila

AU - Kachaev, Zaur M.

AU - Lebedeva, Lyubov A.

AU - Shaposhnikov, Alexander V.

AU - Moresco, James J.

AU - Yates, John R.

AU - Schedl, Paul

AU - Shidlovskii, Yulii V.

PY - 2019/5

Y1 - 2019/5

N2 - 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.

AB - 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.

KW - Cbp80

KW - Paip2

KW - capping

KW - promoter

KW - protein complex

KW - transcription

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JO - FEBS Letters

JF - FEBS Letters

IS - 10

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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