Literature DB >> 9501033

Functional significance of three basic N-terminal amino acids of alfalfa mosaic virus coat protein.

V Yusibov1, L S Loesch-Fries.   

Abstract

Infection of tobacco protoplasts with mutant alfalfa mosaic virus (AMV) RNAs indicated that three basic amino acids in the N-terminus of AMV coat protein are important for the biological activity of the coat protein in the beginning of infection. Substitution of alanines for lysines at position 14 or 17 in the coat protein resulted in a 5- or 10-fold reduction in the activity of the protein, respectively. However, substitution of alanine for arginine at position 18 entirely abolished activity. Arginine 18 was also required for the coat protein to bind to the 3' noncoding region of the virus RNA in vitro, whereas lysine 14 or 17 was not required. Thus, these results indicate that arginine 18 is essential for the activity of the coat protein in early infection and that binding of the coat protein to AMV RNA correlates with activity.

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Year:  1998        PMID: 9501033     DOI: 10.1006/viro.1997.8973

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  8 in total

1.  Spatial determinants of the alfalfa mosaic virus coat protein binding site.

Authors:  Siana M Laforest; Lee Gehrke
Journal:  RNA       Date:  2004-01       Impact factor: 4.942

2.  Degenerate in vitro genetic selection reveals mutations that diminish alfalfa mosaic virus RNA replication without affecting coat protein binding.

Authors:  Gail Rocheleau; Jessica Petrillo; Laura Guogas; Lee Gehrke
Journal:  J Virol       Date:  2004-08       Impact factor: 5.103

3.  Role of the 3'-untranslated regions of alfalfa mosaic virus RNAs in the formation of a transiently expressed replicase in plants and in the assembly of virions.

Authors:  A C Vlot; L Neeleman; H J Linthorst; J F Bol
Journal:  J Virol       Date:  2001-07       Impact factor: 5.103

4.  Expression of alfalfa mosaic virus coat protein in tobacco mosaic virus (TMV) deficient in the production of its native coat protein supports long-distance movement of a chimeric TMV.

Authors:  S Spitsin; K Steplewski; N Fleysh; H Belanger; T Mikheeva; S Shivprasad; W Dawson; H Koprowski; V Yusibov
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-02       Impact factor: 11.205

5.  Cofolding organizes alfalfa mosaic virus RNA and coat protein for replication.

Authors:  Laura M Guogas; David J Filman; James M Hogle; Lee Gehrke
Journal:  Science       Date:  2004-12-17       Impact factor: 47.728

6.  Viral coat protein peptides with limited sequence homology bind similar domains of alfalfa mosaic virus and tobacco streak virus RNAs.

Authors:  M M Swanson; P Ansel-McKinney; F Houser-Scott; V Yusibov; L S Loesch-Fries; L Gehrke
Journal:  J Virol       Date:  1998-04       Impact factor: 5.103

7.  N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement.

Authors:  Xiaofeng Zhang; Xiaofei Zhao; Yanjing Zhang; Shaofang Niu; Feng Qu; Yongliang Zhang; Chenggui Han; Jialin Yu; Dawei Li
Journal:  Virol J       Date:  2013-06-20       Impact factor: 4.099

8.  Functional analysis of the N-terminal basic motif of a eukaryotic satellite RNA virus capsid protein in replication and packaging.

Authors:  Venkatesh Sivanandam; Deborah Mathews; Rees Garmann; Gonca Erdemci-Tandogan; Roya Zandi; A L N Rao
Journal:  Sci Rep       Date:  2016-05-19       Impact factor: 4.379

  8 in total

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