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Dysfunctionality of a tobacco mosaic virus movement protein mutant mimicking threonine 104 phosphorylation.

Karger, E M; Frolova, O Yu; Fedorova, N V; Baratova, L A; Ovchinnikova, T V; Susi, P; Makinen, K; Rönnstrand, Lars LU ; Dorokhov, Yu L and Atabekov, J G (2003) In Journal of General Virology 84(Pt 3). p.32-727
Abstract
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 Thr104 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 Thr104 by neutral Ala or by negatively charged Asp. Mutation of Thr104 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... (More)
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 Thr104 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 Thr104 by neutral Ala or by negatively charged Asp. Mutation of Thr104 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 Thr104 phosphorylation strongly inhibited cell-to-cell movement. The possible role of Thr104 phosphorylation in TMV MP function is discussed. © 2003 Society for General Microbiology (Less)
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published
subject
keywords
Comparative Study, Support, Amino Acid Substitution, Biological Transport, Non-U.S. Gov't, Viral Proteins: metabolism, U.S. Gov't, P.H.S., Threonine: metabolism, Tobacco: virology, Tobacco Mosaic Virus: metabolism, Endoplasmic Reticulum: enzymology, Molecular Weight, Mutation, Phosphorylation, Protein Kinases: chemistry, Protein Kinases: metabolism
in
Journal of General Virology
volume
84
issue
Pt 3
pages
32 - 727
publisher
Society for General Microbiology
external identifiers
  • wos:000181237500026
  • scopus:0037371832
ISSN
1465-2099
DOI
language
English
LU publication?
no
id
0e222b1a-7882-4ec9-8abe-79100e8a88ba (old id 123079)
date added to LUP
2007-07-25 14:40:01
date last changed
2018-05-29 11:50:29
@article{0e222b1a-7882-4ec9-8abe-79100e8a88ba,
  abstract     = {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 Thr104 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 Thr104 by neutral Ala or by negatively charged Asp. Mutation of Thr104 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 Thr104 phosphorylation strongly inhibited cell-to-cell movement. The possible role of Thr104 phosphorylation in TMV MP function is discussed. © 2003 Society for General Microbiology},
  author       = {Karger, E M and Frolova, O Yu and Fedorova, N V and Baratova, L A and Ovchinnikova, T V and Susi, P and Makinen, K and Rönnstrand, Lars and Dorokhov, Yu L and Atabekov, J G},
  issn         = {1465-2099},
  keyword      = {Comparative Study,Support,Amino Acid Substitution,Biological Transport,Non-U.S. Gov't,Viral Proteins: metabolism,U.S. Gov't,P.H.S.,Threonine: metabolism,Tobacco: virology,Tobacco Mosaic Virus: metabolism,Endoplasmic Reticulum: enzymology,Molecular Weight,Mutation,Phosphorylation,Protein Kinases: chemistry,Protein Kinases: metabolism},
  language     = {eng},
  number       = {Pt 3},
  pages        = {32--727},
  publisher    = {Society for General Microbiology},
  series       = {Journal of General Virology},
  title        = {Dysfunctionality of a tobacco mosaic virus movement protein mutant mimicking threonine 104 phosphorylation.},
  url          = {http://dx.doi.org/},
  volume       = {84},
  year         = {2003},
}