The polyomavirus major capsid protein VP1 interacts with the nuclear matrix regulatory protein YY1
Identifieur interne : 003637 ( Main/Exploration ); précédent : 003636; suivant : 003638The polyomavirus major capsid protein VP1 interacts with the nuclear matrix regulatory protein YY1
Auteurs : Zdena Palková [Italie, République tchèque] ; Hana Španielová [République tchèque] ; Vanesa Gottifredi [Italie, États-Unis] ; Dana Hollanderová [République tchèque] ; Jitka Forstová [République tchèque] ; Paolo Amati [Italie]Source :
- FEBS Letters [ 0014-5793 ] ; 2000.
English descriptors
- Teeft :
- Activation domain, Activation domains, Amino acids, Binding site, Broblast cells, Capsid, Capsid protein, Cell nucleus, Cerevisiae hf7c, Coding sequence, Cold spring harbor, Cold spring harbor laboratory press, Control immunoprecipitations, Czech republic, Deletion, Deletion mutants, Direct interaction, Enhancer region, Feb, Fusion protein, Gal4, Genome, His3, His3 expression, Immunoprecipitations, Insect cells, Lacz, Lacz expression, Lacz gene, Lter assay, Major capsid protein, Monoclonal antibody, Mutant, Nuclear matrix, Plasmid, Polyclonal antibody, Reporter gene, Smai site, Synthetic primers, Unpublished results, Viral, Viral genes, Viral genome, Viral life cycle, Viral replication, Virol, Yeast, Yeast colonies, Yeast factor, Yeast system.
Abstract
Abstract: Polyomavirus reaches the nucleus in a still encapsidated form, and the viral genome is readily found in association with the nuclear matrix. This association is thought to be essential for viral replication. In order to identify the protein(s) involved in the virus-nuclear matrix interaction, we focused on the possible roles exerted by the multifunctional cellular nuclear matrix protein Yin Yang 1 (YY1) and by the viral major capsid protein VP1. In the present work we report on the in vivo association between YY1 and VP1. Using the yeast two-hybrid system we demonstrate that the VP1 and YY1 proteins physically interact through the D-E region of VP1 and the activation domain of YY1.
Url:
DOI: 10.1016/S0014-5793(00)01170-4
Affiliations:
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