Literature DB >> 14107452

UNUSUAL AGGREGATION OF A NONFUNCTIONAL TOBACCO MOSAIC VIRUS PROTEIN.

M ZAITLIN, W R FERRIS.   

Abstract

The nonfunctional virus protein isolated from plants infected with the PM2 strain of tobacco mosaic virus aggregates to form elongated, two-stranded, open helical structures, in marked contrast with functional tobacco mosaic virus protein which aggregates into rods. This unique type of aggregation may explain why the PM2 protein is unable to combine with viral nucleic acid to form stable infectious virus particles.

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Keywords:  EXPERIMENTAL LAB STUDY; PHOTOMICROGRAPHY; RNA, VIRAL; STAINS AND STAINING; TOBACCO MOSAIC VIRUS; VIRAL PROTEINS

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Year:  1964        PMID： 14107452     DOI： 10.1126/science.143.3613.1451

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  3 in total

1.  Interaction of TMV-proteins during electrophoretic separation in polyacrylamide gels.

Authors:  S Sarkar; L Schilde-Rentschler
Journal:  Mol Gen Genet       Date:  1968

2.  [Amino acid sequence and physico-chemical behavior of coat proteins of wild strain tobacco mosaic virus. II. Aggregation behavior and electric charge distribution in comparison to the strains vulgare and dahlemense].

Authors:  L Rentschler
Journal:  Mol Gen Genet       Date:  1967

3.  [The protein structure of the defective mutant PM 2 of the tobacco mosaic virus].

Authors:  H G Wittmann
Journal:  Z Vererbungsl       Date:  1965
  3 in total

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