UNUSUAL AGGREGATION OF A NONFUNCTIONAL TOBACCO MOSAIC VIRUS PROTEIN.

Science (New York, N.Y.) ·Vol. 143 ·No. 3613 ·1964-03-27 ·Pages 1451-2

ZAITLIN M, FERRIS WR

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.

Keywords

EXPERIMENTAL LAB STUDY PHOTOMICROGRAPHY RNA VIRAL STAINS AND STAINING TOBACCO MOSAIC VIRUS VIRAL PROTEINS

MeSH Terms

Coloring Agents Photomicrography Proteins RNA RNA, Viral Research Staining and Labeling Tobacco Mosaic Virus Viral Proteins

Chemicals

Coloring Agents Proteins RNA, Viral Viral Proteins RNA

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

ZAITLIN M

FERRIS W R

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.143.3613.1451

Published

1964-03-27

Pages

1451-2

Language

English

Region

United States

NLM ID

0404511

Subset

External Links

PubMed source DOI: 10.1126/science.143.3613.1451 View journal details

Analysis Services

UNUSUAL AGGREGATION OF A NONFUNCTIONAL TOBACCO MOSAIC VIRUS PROTEIN.

Contact

WeChat Official Account