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The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation

So far it has been demonstrated that the signal sequence of proteins which are made at the ER functions both at the level of protein targeting to the ER and in initiation of chain translocation across the ER membrane. However, its possible role in completing the process of chain transfer (see Singer...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1990
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116283/
https://www.ncbi.nlm.nih.gov/pubmed/2391367
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collection PubMed
description So far it has been demonstrated that the signal sequence of proteins which are made at the ER functions both at the level of protein targeting to the ER and in initiation of chain translocation across the ER membrane. However, its possible role in completing the process of chain transfer (see Singer, S. J., P. A. Maher, and M. P. Yaffe. Proc. Natl. Acad. Sci. USA. 1987. 84:1015-1019) has remained elusive. In this work we show that the p62 protein of Semliki Forest virus contains an uncleaved signal sequence at its NH2-terminus and that this becomes glycosylated early during synthesis and translocation of the p62 polypeptide. As the glycosylation of the signal sequence most likely occurs after its release from the ER membrane our results suggest that this region has no role in completing the transfer process.
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spelling pubmed-21162832008-05-01 The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation J Cell Biol Articles So far it has been demonstrated that the signal sequence of proteins which are made at the ER functions both at the level of protein targeting to the ER and in initiation of chain translocation across the ER membrane. However, its possible role in completing the process of chain transfer (see Singer, S. J., P. A. Maher, and M. P. Yaffe. Proc. Natl. Acad. Sci. USA. 1987. 84:1015-1019) has remained elusive. In this work we show that the p62 protein of Semliki Forest virus contains an uncleaved signal sequence at its NH2-terminus and that this becomes glycosylated early during synthesis and translocation of the p62 polypeptide. As the glycosylation of the signal sequence most likely occurs after its release from the ER membrane our results suggest that this region has no role in completing the transfer process. The Rockefeller University Press 1990-09-01 /pmc/articles/PMC2116283/ /pubmed/2391367 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation
title The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation
title_full The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation
title_fullStr The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation
title_full_unstemmed The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation
title_short The signal sequence of the p62 protein of Semliki Forest virus is involved in initiation but not in completing chain translocation
title_sort signal sequence of the p62 protein of semliki forest virus is involved in initiation but not in completing chain translocation
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116283/
https://www.ncbi.nlm.nih.gov/pubmed/2391367