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 Brentano, L.
Right arrow Articles by Sherry, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Brentano, L.
Right arrow Articles by Sherry, B.

 Previous Article  |  Next Article 

Journal of Virology, October 1998, p. 8354-8357, Vol. 72, No. 10
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Reovirus Protein µ2, Encoded by the M1 Gene, Is an RNA-Binding Protein

Liana Brentano,1,dagger Diana L. Noah,1 Earl G. Brown,2 and Barbara Sherry1,*

Department of Microbiology, Pathology, and Parasitology, College of Veterinary Medicine, North Carolina State University, Raleigh, North Carolina 27606,1 and Department of Microbiology and Immunology, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada2

Received 20 May 1998/Accepted 1 July 1998

The reovirus M1, L1, and L2 genes encode proteins found at each vertex of the viral core and are likely to form a structural unit involved in RNA synthesis. Genetic analyses have implicated the M1 gene in viral RNA synthesis and core nucleoside triphosphatase activity, but there have been no direct biochemical studies of µ2 function. Here, we expressed µ2 in vitro and assessed its RNA-binding activity. The expressed µ2 binds both poly(I-C)- and poly(U)-Sepharose, and binding activity is greater in Mn2+ than in Mg2+. Heterologous RNA competes for µ2 binding to reovirus RNA transcripts as effectively as homologous reovirus RNA does, providing no evidence for sequence-specific RNA binding by µ2. Protein µ2 is now the sixth reovirus protein demonstrated to have RNA-binding activity.

* Corresponding author. Mailing address: Department of Microbiology, Pathology, and Parasitology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606. Phone: (919) 515-4480. Fax: (919) 515-3044. E-mail: barbara_sherry{at}ncsu.edu.

dagger Present address: EMBRAPA, Concordia-SC, Brazil.

Journal of Virology, October 1998, p. 8354-8357, Vol. 72, No. 10
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Kobayashi, T., Ooms, L. S., Chappell, J. D., Dermody, T. S. (2009). Identification of Functional Domains in Reovirus Replication Proteins {micro}NS and {micro}2. J. Virol. 83: 2892-2906 [Abstract] [Full Text]  
  • Zurney, J., Kobayashi, T., Holm, G. H., Dermody, T. S., Sherry, B. (2009). Reovirus {micro}2 Protein Inhibits Interferon Signaling through a Novel Mechanism Involving Nuclear Accumulation of Interferon Regulatory Factor 9. J. Virol. 83: 2178-2187 [Abstract] [Full Text]  
  • Murray, K. E., Nibert, M. L. (2007). Guanidine Hydrochloride Inhibits Mammalian Orthoreovirus Growth by Reversibly Blocking the Synthesis of Double-Stranded RNA. J. Virol. 81: 4572-4584 [Abstract] [Full Text]  
  • Miller, C. L., Parker, J. S. L., Dinoso, J. B., Piggott, C. D. S., Perron, M. J., Nibert, M. L. (2004). Increased Ubiquitination and Other Covariant Phenotypes Attributed to a Strain- and Temperature-Dependent Defect of Reovirus Core Protein {micro}2. J. Virol. 78: 10291-10302 [Abstract] [Full Text]  
  • Hermann, L. L., Coombs, K. M. (2004). Inhibition of Reovirus by Mycophenolic Acid Is Associated with the M1 Genome Segment. J. Virol. 78: 6171-6179 [Abstract] [Full Text]  
  • Nibert, M. L., Kim, J. (2004). Conserved Sequence Motifs for Nucleoside Triphosphate Binding Unique to Turreted Reoviridae Members and Coltiviruses. J. Virol. 78: 5528-5530 [Full Text]  
  • Kim, J., Parker, J. S. L., Murray, K. E., Nibert, M. L. (2004). Nucleoside and RNA Triphosphatase Activities of Orthoreovirus Transcriptase Cofactor {micro}2. J. Biol. Chem. 279: 4394-4403 [Abstract] [Full Text]  
  • Broering, T. J., Parker, J. S. L., Joyce, P. L., Kim, J., Nibert, M. L. (2002). Mammalian Reovirus Nonstructural Protein {micro}NS Forms Large Inclusions and Colocalizes with Reovirus Microtubule-Associated Protein {micro}2 in Transfected Cells. J. Virol. 76: 8285-8297 [Abstract] [Full Text]  
  • Parker, J. S. L., Broering, T. J., Kim, J., Higgins, D. E., Nibert, M. L. (2002). Reovirus Core Protein {micro}2 Determines the Filamentous Morphology of Viral Inclusion Bodies by Interacting with and Stabilizing Microtubules. J. Virol. 76: 4483-4496 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»