Document Detail


Nucleolar trafficking of the mouse mammary tumor virus gag protein induced by interaction with ribosomal protein L9.
MedLine Citation:
PMID:  23135726     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The mouse mammary tumor virus (MMTV) Gag protein directs the assembly in the cytoplasm of immature viral capsids, which subsequently bud from the plasma membranes of infected cells. MMTV Gag localizes to discrete cytoplasmic foci in mouse mammary epithelial cells, consistent with the formation of cytosolic capsids. Unexpectedly, we also observed an accumulation of Gag in the nucleoli of infected cells derived from mammary gland tumors. To detect Gag-interacting proteins that might influence its subcellular localization, a yeast two-hybrid screen was performed. Ribosomal protein L9 (RPL9 or L9), an essential component of the large ribosomal subunit and a putative tumor suppressor, was identified as a Gag binding partner. Overexpression of L9 in cells expressing the MMTV(C3H) provirus resulted in specific, robust accumulation of Gag in nucleoli. Förster resonance energy transfer (FRET) and coimmunoprecipitation analyses demonstrated that Gag and L9 interact within the nucleolus, and the CA domain was the major site of interaction. In addition, the isolated NC domain of Gag localized to the nucleolus, suggesting that it contains a nucleolar localization signal (NoLS). To determine whether L9 plays a role in virus assembly, small interfering RNA (siRNA)-mediated knockdown was performed. Although Gag expression was not reduced with L9 knockdown, virus production was significantly impaired. Thus, our data support the hypothesis that efficient MMTV particle assembly is dependent upon the interaction of Gag and L9 in the nucleoli of infected cells.
Authors:
Andrea R Beyer; Darrin V Bann; Breanna Rice; Ingrid S Pultz; Melissa Kane; Stephen P Goff; Tatyana V Golovkina; Leslie J Parent
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-11-07
Journal Detail:
Title:  Journal of virology     Volume:  87     ISSN:  1098-5514     ISO Abbreviation:  J. Virol.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-28     Completed Date:  2013-02-25     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1069-82     Citation Subset:  IM    
Affiliation:
Departments of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey, PA, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line
Cell Nucleolus / metabolism*
Epithelial Cells / virology
Fluorescence Resonance Energy Transfer
Gene Products, gag / metabolism*
Host-Pathogen Interactions*
Immunoprecipitation
Mammary Tumor Virus, Mouse / physiology*
Mice
Protein Binding
Protein Interaction Domains and Motifs
Protein Interaction Mapping
Protein Sorting Signals
Protein Transport
Ribosomal Proteins / metabolism*
Two-Hybrid System Techniques
Virus Assembly*
Grant Support
ID/Acronym/Agency:
F30 CA165774/CA/NCI NIH HHS; F30 CA165774/CA/NCI NIH HHS; R01 CA113784/CA/NCI NIH HHS; R01 CA113784/CA/NCI NIH HHS; R01 CA30488/CA/NCI NIH HHS; R01 CA76534/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Gene Products, gag; 0/Protein Sorting Signals; 0/Ribosomal Proteins; 0/ribosomal protein L9
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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