Open AccessDysfunctionality of a tobacco mosaic virus movement protein mutant mimicking threonine 104 phosphorylation
Author(s) -
Е. М. Каргер,
Olga Frolova,
N. V. Fedorova,
L. A. Baratova,
Т. В. Овчинникова,
Petri Susi,
Kristiina Mäkinen,
Lars Rönnstrand,
Yu. L. Dorokhov,
J.G. Atabekov
Publication year - 2003
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/vir.0.18972-0
Subject(s) - tobacco mosaic virus , biology , phosphorylation , mutant , nicotiana tabacum , endoplasmic reticulum , movement protein , mutation , threonine , virology , microbiology and biotechnology , virus , tobamovirus , mutagenesis , gene , kinase , wild type , genetics , serine , rna , coat protein
Replication of tobacco mosaic virus (TMV) is connected with endoplasmic reticulum (ER)-associated membranes at early stages of infection. This study reports that TMV movement protein (MP)-specific protein kinases (PKs) associated with the ER of tobacco were capable of phosphorylating Thr(104) in TMV MP. The MP-specific PKs with apparent molecular masses of about 45-50 kDa and 38 kDa were revealed by gel PK assays. Two types of mutations were introduced in TMV MP gene of wild-type TMV U1 genome to substitute Thr(104) by neutral Ala or by negatively charged Asp. Mutation of Thr(104) to Ala did not affect the size of necrotic lesions induced by the mutant virus in Nicotiana tabacum Xanthi nc. plants. Conversely, mutation of Thr to Asp mimicking Thr(104) phosphorylation strongly inhibited cell-to-cell movement. The possible role of Thr(104) phosphorylation in TMV MP function is discussed.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom