JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Goatley, L. C.
Right arrow Articles by Dixon, L. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Goatley, L. C.
Right arrow Articles by Dixon, L. K.

 Previous Article  |  Next Article 

Journal of Virology, October 2002, p. 9991-9999, Vol. 76, No. 19
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.19.9991-9999.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The African Swine Fever Virus Protein j4R Binds to the Alpha Chain of Nascent Polypeptide-Associated Complex

Lynnette C. Goatley,1 Steve R. F. Twigg,2,{dagger} James E. Miskin,1,{ddagger} Paul Monaghan,1 René St-Arnaud,3 Geoffrey L. Smith,2 and Linda K. Dixon1*

Institute for Animal Health, Pirbright, Woking, Surrey GU24 ONF,1 Faculty of Medicine, Wright Fleming Institute, Imperial CollegeSt. Mary's Campus, London W2 1PG 3, United Kingdom,2 Genetics Unit, Shriners Hospital for Children, Montreal, H3G 1A6 Quebec, Canada3

Received 5 June 2002/ Accepted 19 June 2002

The African swine fever virus (ASFV) j4R protein is expressed late during the virus replication cycle and is present in both the nucleus and the cytoplasm of infected cells. By using the yeast two-hybrid system, direct binding, and coprecipitation from cells, we showed that the j4R protein binds to the alpha chain of nascent polypeptide-associated complex ({alpha}NAC). Confocal microscopy indicated that a proportion of j4R and {alpha}NAC interact in areas close to the plasma membrane, as well as through the cytoplasm in cells. In vitro binding studies suggested that binding of j4R to {alpha}NAC did not interfere with the binding of {alpha}- and ßNAC subunits (the BTF3 transcription factor).


* Corresponding author. Mailing address: Institute for Animal Health, Pirbright Laboratory, Ash Rd., Pirbright, Woking, Surrey GU24 ONF, United Kingdom. Phone: 44(0)1483-232441. Fax: 44(0)1483-232448. E-mail: Linda.dixon{at}bbsrc.ac.uk.

{dagger} Present address: Institute of Molecular Medicine, John Radcliffe Hospital, Oxford OX3 9DS, United Kingdom.

{ddagger} Present address: Oxford BioMedica, Oxford OX4 4GA, United Kingdom.


Journal of Virology, October 2002, p. 9991-9999, Vol. 76, No. 19
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.19.9991-9999.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2002 by the American Society for Microbiology. All rights reserved.