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PMID: 2214022 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The E2 signal sequence of rubella virus remains part of the capsid protein and confers membrane association in vitro.

Journal of virology ·Vol. 64 ·No. 11 ·1990-11-00 ·Pages 5500-9

Suomalainen M, Garoff H, Baron MD

Abstract

The capsid (C) protein of rubella virus is translated from a 24S subgenomic mRNA as the first part of a polyprotein containing all three structural proteins of the virus. It is separated from the following protein (E2) by signal peptidase, which cleaves after the E2 signal sequence. We raised an antipeptide antiserum directed against the signal sequence and used the antiserum to show that this sequence is still a part of the C protein in the mature virion. Furthermore, we also showed that, when the C protein is synthesized by in vitro transcription and translation, the resultant protein is membrane associated. This association is not seen with a variant C protein which lacks the signal sequence, and a normally soluble protein (dihydrofolate reductase) becomes membrane associated when the signal sequence is placed at its carboxy terminus.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Capsid/genetics,metabolism Cell Compartmentation Cell Membrane/metabolism Cloning, Molecular DNA Mutational Analysis In Vitro Techniques Membrane Glycoproteins/genetics Molecular Sequence Data Oligonucleotides Protein Sorting Signals/genetics Rubella virus/genetics Species Specificity Vero Cells
Chemicals
Membrane Glycoproteins Oligonucleotides Protein Sorting Signals
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Suomalainen M
Department of Molecular Biology, Karolinska Institute, Novum, Huddinge, Sweden.
Garoff H
Baron M D
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1990-11-00
Pages
5500-9
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC248602
Subset
IM
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