Quantitative SUMO-1 modification of a vaccinia virus protein is required for its specific localization and prevents its self-association

Détails

ID Serval
serval:BIB_8FF90D3B7DD3
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Quantitative SUMO-1 modification of a vaccinia virus protein is required for its specific localization and prevents its self-association
Périodique
Mol Biol Cell
Auteur(s)
Palacios S., Perez L. H., Welsch S., Schleich S., Chmielarska K., Melchior F., Locker J. K.
ISSN
1059-1524 (Print)
1059-1524
Statut éditorial
Publié
Date de publication
06/2005
Volume
16
Numéro
6
Pages
2822-35
Langue
anglais
Notes
Palacios, Silvia
Perez, Laurent H
Welsch, Sonja
Schleich, Sibylle
Chmielarska, Katarzyna
Melchior, Frauke
Locker, Jacomine Krijnse
Journal Article
Research Support, Non-U.S. Gov't
Mol Biol Cell. 2005 Jun;16(6):2822-35. doi: 10.1091/mbc.e04-11-1005. Epub 2005 Mar 30.
Résumé
Vaccinia virus (VV), the prototype member of the Poxviridae, a family of large DNA viruses, carries out DNA replication in specialized cytoplasmic sites that are enclosed by the rough endoplasmic reticulum (ER). We show that the VV gene product of A40R is quantitatively modified by SUMO-1, which is required for its localization to the ER-enclosed replication sites. Expression of A40R lacking SUMO-1 induced the formation of rod-shaped cytoplasmic aggregates. The latter likely consisted of polymers of nonsumoylated protein, because unmodified A40R interacted with itself, but not with the SUMO-1-conjugated protein. Using a bacterial sumoylation system, we furthermore show that unmodified A40R is mostly insoluble, whereas the modified form is completely soluble. By electron microscopy, the A40R rods seen in cells were associated with the cytosolic side of the ER and induced the apposition of several ER cisternae. A40R is the first example of a poxvirus protein to acquire SUMO-1. Its quantitative SUMO-1 modification is required for its proper localization to the viral "mini-nuclei" and prevents its self-association. The ability of the nonsumoylated A40R to bring ER membranes close together could suggest a role in the fusion of ER cisternae when these coalesce to enclose the VV replication sites.
Mots-clé
Blotting, Western, DNA, Viral/genetics/metabolism, Endoplasmic Reticulum/metabolism/ultrastructure, Green Fluorescent Proteins/metabolism, HeLa Cells, Humans, Lysine/chemistry, Membrane Glycoproteins/chemistry/genetics/*metabolism/ultrastructure, Molecular Weight, Mutagenesis, Site-Directed, Precipitin Tests, Protein Binding, Protein Biosynthesis, SUMO-1 Protein/chemistry/*metabolism, Vaccinia virus/genetics/*metabolism/*physiology, Viral Nonstructural Proteins/chemistry/genetics/*metabolism/ultrastructure, Virus Assembly, Virus Replication
Création de la notice
04/09/2020 20:03
Dernière modification de la notice
07/09/2020 6:26
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