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Title: Default assembly of early adenovirus chromatin

Abstract

In adenovirus particles, the viral nucleoprotein is organized into a highly compacted core structure. Upon delivery to the nucleus, the viral nucleoprotein is very likely to be remodeled to a form accessible to the transcription and replication machinery. Viral protein VII binds to intra-nuclear viral DNA, as do at least two cellular proteins, SET/TAF-I{beta} and pp32, components of a chromatin assembly complex that is implicated in template remodeling. We showed previously that viral DNA-protein complexes released from infecting particles were sensitive to shearing after cross-linking with formaldehyde, presumably after transport of the genome into the nucleus. We report here the application of equilibrium-density gradient centrifugation to the analysis of the fate of these complexes. Most of the incoming protein VII was recovered in a form that was not cross-linked to viral DNA. This release of protein VII, as well as the binding of SET/TAF-I{beta} and cellular transcription factors to the viral chromatin, did not require de novo viral gene expression. The distinct density profiles of viral DNA complexes containing protein VII, compared to those containing SET/TAF-I{beta} or transcription factors, were consistent with the notion that the assembly of early viral chromatin requires both the association of SET/TAF-1{beta} and the releasemore » of protein VII.« less

Authors:
 [1]
  1. Department of Microbiology and Immunology, Intercollege Graduate Degree Program in Genetics, and Cellular and Molecular Biology Program, Pennsylvania State University College of Medicine, Hershey, PA 17033 (United States). E-mail: dspector@psu.edu
Publication Date:
OSTI Identifier:
20976994
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 359; Journal Issue: 1; Other Information: DOI: 10.1016/j.virol.2006.09.005; PII: S0042-6822(06)00648-9; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ADENOVIRUS; CENTRIFUGATION; CHROMATIN; CROSS-LINKING; DNA; FORMALDEHYDE; GENES; TRANSCRIPTION; TRANSCRIPTION FACTORS

Citation Formats

Spector, David J. Default assembly of early adenovirus chromatin. United States: N. p., 2007. Web. doi:10.1016/j.virol.2006.09.005.
Spector, David J. Default assembly of early adenovirus chromatin. United States. doi:10.1016/j.virol.2006.09.005.
Spector, David J. Thu . "Default assembly of early adenovirus chromatin". United States. doi:10.1016/j.virol.2006.09.005.
@article{osti_20976994,
title = {Default assembly of early adenovirus chromatin},
author = {Spector, David J.},
abstractNote = {In adenovirus particles, the viral nucleoprotein is organized into a highly compacted core structure. Upon delivery to the nucleus, the viral nucleoprotein is very likely to be remodeled to a form accessible to the transcription and replication machinery. Viral protein VII binds to intra-nuclear viral DNA, as do at least two cellular proteins, SET/TAF-I{beta} and pp32, components of a chromatin assembly complex that is implicated in template remodeling. We showed previously that viral DNA-protein complexes released from infecting particles were sensitive to shearing after cross-linking with formaldehyde, presumably after transport of the genome into the nucleus. We report here the application of equilibrium-density gradient centrifugation to the analysis of the fate of these complexes. Most of the incoming protein VII was recovered in a form that was not cross-linked to viral DNA. This release of protein VII, as well as the binding of SET/TAF-I{beta} and cellular transcription factors to the viral chromatin, did not require de novo viral gene expression. The distinct density profiles of viral DNA complexes containing protein VII, compared to those containing SET/TAF-I{beta} or transcription factors, were consistent with the notion that the assembly of early viral chromatin requires both the association of SET/TAF-1{beta} and the release of protein VII.},
doi = {10.1016/j.virol.2006.09.005},
journal = {Virology},
number = 1,
volume = 359,
place = {United States},
year = {Thu Mar 01 00:00:00 EST 2007},
month = {Thu Mar 01 00:00:00 EST 2007}
}