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PMID: 1203319 Published · ppublish English Journal Article

Location of the cistron of the tobacco mosaic virus coat protein.

Biochimie ·Vol. 57 ·No. 6-7 ·1975-00-00 ·Pages 749-55

Richards KE, Morel MC, Nicolaieff A, Lebeurier G, Hirth L

Abstract

Treatment of tobacco mosaic virus (TMV) RNA with T1 RNase under mild conditions cuts the RNA molecule into a large number of fragments, only a few of which may be specifically recognized by disks of TMV protein. It has been shown elsewhere that these specifically recognized RNA fragments are a part of the coat protein cistron, the portion coding for amino acids 95 to 129 of the coat protein. It is reported that different size classes of partially uncoated virus particles were prepared by limited reconstitution between TMV RNA and protein or by partial stripping of intact virus with DMSO. Both procedures produce nucleoprotein rods in which the 5'-terminal portion of the RNA is encapsidated and the 3'-terminal region is free. The free and the encapsidated portions of the RNA were each tested for the ability to give rise to the aforesaid specifically recognized fragments of the coat protein cistron upon partial T1 RNase digestion. It was found that only the 3'-terminal third of the virus particle need to be uncoated in order to expose the portion of the RNA molecule from which these fragments are derived. We conclude, therefore, that the coat protein cistron is situated upon the 3'-terminal third of the RNA chain, i.e. within 2000 nucleotides of the 3'-end.

MeSH Terms
Genes Genetic Code Microscopy, Electron Molecular Weight Nucleic Acid Conformation RNA, Viral/analysis Ribonucleases Tobacco Mosaic Virus/analysis,ultrastructure Viral Proteins/analysis
Chemicals
RNA, Viral Viral Proteins Ribonucleases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Richards K E
Morel M C
Nicolaieff A
Lebeurier G
Hirth L
Article Info
Journal
Biochimie
Abbr.
Biochimie
ISSN
0300-9084
Published
1975-00-00
Pages
749-55
Language
English
Region
France
NLM ID
1264604
Subset
IM
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