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 Gallois-Montbrun, S.
Right arrow Articles by Malim, M. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gallois-Montbrun, S.
Right arrow Articles by Malim, M. H.

 Previous Article  |  Next Article 

Journal of Virology, June 2008, p. 5636-5642, Vol. 82, No. 11
0022-538X/08/$08.00+0     doi:10.1128/JVI.00287-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Comparison of Cellular Ribonucleoprotein Complexes Associated with the APOBEC3F and APOBEC3G Antiviral Proteins{triangledown}

Sarah Gallois-Montbrun,1 Rebecca K. Holmes,1 Chad M. Swanson,1 Mireia Fernández-Ocaña,2 Helen L. Byers,3 Malcolm A. Ward,3 and Michael H. Malim1*

Department of Infectious Diseases, King's College London School of Medicine, London SE1 9RT, United Kingdom,1 MRC Centre for Neurodegeneration Research,2 Proteome Sciences plc, Institute of Psychiatry, King's College London, London SE5 8AF, United Kingdom3

Received 8 February 2008/ Accepted 17 March 2008

The human apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F (APOBEC3F [A3F]) and A3G proteins are effective inhibitors of infection by various retroelements and share ~50% amino acid sequence identity. We therefore undertook comparative analyses of the protein and RNA compositions of A3F- and A3G-associated ribonucleoprotein complexes (RNPs). Like A3G, A3F is found associated with a complex array of cytoplasmic RNPs and can accumulate in RNA-rich cytoplasmic microdomains known as mRNA processing bodies or stress granules. While A3F RNPs display greater resistance to disruption by RNase digestion, the major protein difference is the absence of the Ro60 and La autoantigens. Consistent with this, A3F RNPs also lack a number of small polymerase III RNAs, including the RoRNP-associated Y RNAs, as well as 7SL RNA. Alu RNA is, however, present in A3F and A3G RNPs, and both proteins suppress Alu element retrotransposition. Thus, we define a number of subtle differences between the RNPs associated with A3F and A3G and speculate that these contribute to functional differences that have been described for these proteins.


* Corresponding author. Mailing address: Department of Infectious Diseases, King's College London School of Medicine, 2nd Floor, Borough Wing, Guy's Hospital, London Bridge, London SE1 9RT, United Kingdom. Phone: (44) 20 718 80149. Fax: (44) 20 718 80147. E-mail: michael.malim{at}kcl.ac.uk

{triangledown} Published ahead of print on 26 March 2008.


Journal of Virology, June 2008, p. 5636-5642, Vol. 82, No. 11
0022-538X/08/$08.00+0     doi:10.1128/JVI.00287-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Henriet, S., Mercenne, G., Bernacchi, S., Paillart, J.-C., Marquet, R. (2009). Tumultuous Relationship between the Human Immunodeficiency Virus Type 1 Viral Infectivity Factor (Vif) and the Human APOBEC-3G and APOBEC-3F Restriction Factors. Microbiol. Mol. Biol. Rev. 73: 211-232 [Abstract] [Full Text]  
  • Petit, V., Vartanian, J.-P., Wain-Hobson, S. (2009). Powerful mutators lurking in the genome. Phil Trans R Soc B 364: 705-715 [Abstract] [Full Text]  
  • Stenglein, M. D., Matsuo, H., Harris, R. S. (2008). Two Regions within the Amino-Terminal Half of APOBEC3G Cooperate To Determine Cytoplasmic Localization. J. Virol. 82: 9591-9599 [Abstract] [Full Text]