Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (191K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (12)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Bayliss, C. D.
Right arrow Articles by Smith, G. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bayliss, C. D.
Right arrow Articles by Smith, G. L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 25, Issue 20 3984-3990, Copyright © 1997 by Oxford University Press

ARTICLES

Vaccinia virion protein VP8, the 25 kDa product of the L4R gene, binds single-stranded DNA and RNA with similar affinity

CD Bayliss and GL Smith
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.

Vaccinia virus protein VP8 is a 25 kDa product of the L4R gene and is an abundant virion protein that binds single-stranded (ss) and double- stranded (ds) DNA. Binding of ssDNA is preferred at high salt concentrations. Using a recombinant 25 kDa L4R (rL4R) protein and a gel mobility shift assay with radiolabelled oligonucleotides, the Kd for a 45mer oligonucleotide was determined to be 2 nM. The Kd was unaltered by 50 mM KCl but was reduced 35-fold by 100 mM KCl. Multiple rL4R molecules bound to a single 45mer oligonucleotide, and using oligonucleotides of different lengths it was calculated that one rL4R molecule bound every 17 nt. Binding to ssDNA was competed by both deoxyribo- and ribo-polynucleotides. RNA binding was observed for both rL4R and native VP8, purified from virions, using a gel mobility shift with a radiolabelled ssRNA of 130 nt. The Kd of rL4R for this ssRNA substrate was 3 nM in the absence of salt and binding was positively cooperative. The potential roles of L4R protein in vaccinia virus early transcription are discussed.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
M. Mallardo, S. Schleich, and J. Krijnse Locker
Microtubule-dependent Organization of Vaccinia Virus Core-derivd Early mRNAs into Distinct Cytoplasmic Structures
Mol. Biol. Cell, December 1, 2001; 12(12): 3875 - 3891.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
K. Pedersen, E. J. Snijder, S. Schleich, N. Roos, G. Griffiths, and J. K. Locker
Characterization of Vaccinia Virus Intracellular Cores: Implications for Viral Uncoating and Core Structure
J. Virol., April 15, 2000; 74(8): 3525 - 3536.
[Abstract] [Full Text]

Home page
 J. Virol.Home page
P. Traktman, K. Liu, J. DeMasi, R. Rollins, S. Jesty, and B. Unger
Elucidating the Essential Role of the A14 Phosphoprotein in Vaccinia Virus Morphogenesis: Construction and Characterization of a Tetracycline-Inducible Recombinant
J. Virol., April 15, 2000; 74(8): 3682 - 3695.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. McCraith, T. Holtzman, B. Moss, and S. Fields
Genome-wide analysis of vaccinia virus protein-protein interactions
PNAS, April 25, 2000; 97(9): 4879 - 4884.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.