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PMID: 11980726 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Phosphorylation of cucumber mosaic virus RNA polymerase 2a protein inhibits formation of replicase complex.

The EMBO journal ·Vol. 21 ·No. 9 ·2002-05-01 ·Pages 2292-300

Kim SH, Palukaitis P, Park YI

Abstract

The 2a (polymerase) protein of cucumber mosaic virus (CMV) was shown to be phosphorylated both in vivo and in vitro. In vitro assays using 2a protein mutants and tobacco protein kinases showed that the 2a protein has at least three phosphorylation sites, one of which is located within the N-terminal 126 amino acid region. This region is essential and sufficient for interaction with the CMV 1a protein. When phosphorylated in vitro, the 2a protein N-terminal region failed to interact with the 1a protein. Since the 1a-2a interaction is essential for the replication of CMV, this suggests that phosphorylation of the N-terminal region of the 2a protein negatively modulates the interaction in vivo, and may have a regulatory role acting directly in viral infection.

MeSH Terms
Cucumovirus/enzymology,physiology Macromolecular Substances Phosphorylation Protein Kinases/physiology RNA Polymerase I/physiology RNA Polymerase II/physiology RNA-Dependent RNA Polymerase/metabolism
Chemicals
Macromolecular Substances Protein Kinases RNA Polymerase II RNA-Dependent RNA Polymerase RNA Polymerase I
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kim Sang Hyon
Division of Life Sciences, and Graduate School of Biotechnology, Korea University, 1, 5-ga, Anam-dong, Sungbuk-gu, Seoul 136-701, Korea.
Palukaitis Peter
Park Young In
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
2002-05-01
Pages
2292-300
Language
English
Region
England
NLM ID
8208664
PMCID
PMC125983
Subset
IM
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