Premium
Phosphorylation of cucumber mosaic virus RNA polymerase 2a protein inhibits formation of replicase complex
Author(s) -
Kim Sang Hyon,
Palukaitis Peter,
Park Young In
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/21.9.2292
Subject(s) - biology , phosphorylation , rna dependent rna polymerase , cucumber mosaic virus , polymerase , protein phosphorylation , rna polymerase , microbiology and biotechnology , autophagy related protein 13 , protein kinase a , virology , rna , biochemistry , gene
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.