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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/123079
- author
- 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
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- 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
- Microbiology Society
- external identifiers
-
- wos:000181237500026
- scopus:0037371832
- ISSN
- 1465-2099
- DOI
- 10.1099/vir.0.18972-0
- language
- English
- LU publication?
- no
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
- id
- 0e222b1a-7882-4ec9-8abe-79100e8a88ba (old id 123079)
- date added to LUP
- 2016-04-01 16:31:03
- date last changed
- 2022-01-28 20:17:41
@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}},
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}},
language = {{eng}},
number = {{Pt 3}},
pages = {{32--727}},
publisher = {{Microbiology Society}},
series = {{Journal of General Virology}},
title = {{Dysfunctionality of a tobacco mosaic virus movement protein mutant mimicking threonine 104 phosphorylation.}},
url = {{https://lup.lub.lu.se/search/files/4696683/624006.pdf}},
doi = {{10.1099/vir.0.18972-0}},
volume = {{84}},
year = {{2003}},
}