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In vivo phosphorylation of the 30‐kDa protein of tobacco mosaic virus
Author(s) -
Watanabe Yuichiro,
Ogawa Toshiya,
Okada Yoshimi
Publication year - 1992
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 - 10.1016/0014-5793(92)81440-w
Subject(s) - tobacco mosaic virus , phosphorylation , in vivo , chemistry , virology , virus , biochemistry , biology , microbiology and biotechnology
The 30‐kDa protein of tobacco mosaic virus, which is involved in cell‐to‐cell movement function, is phosphorylated in tobacco protoplasts. To investigate which portion of the protein is phosphorylated we inoculated several truncated 30‐kDa protein mutants into protoplasts and determined whether or not those truncated proteins are phosphorylated. The results showed that amino acid residues 234–261 of the 30‐kDa protein are required for this phosphorylation.