Dysfunctionality of a tobacco mosaic virus movement protein mutant mimicking threonine 104 phosphorylation.
Författare
Summary, in English
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
Publiceringsår
2003
Språk
Engelska
Sidor
32-727
Publikation/Tidskrift/Serie
Journal of General Virology
Volym
84
Issue
Pt 3
Fulltext
- Available as PDF - 318 kB
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Dokumenttyp
Artikel i tidskrift
Förlag
Microbiology Society
Ämne
- Medicinal Chemistry
Nyckelord
- 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
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1465-2099