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  • 1
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    Leucine-tRNA initiates at CUG start codons for protein synthesis and presentation by MHC class I (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-30
    Description: Effective immune surveillance by cytotoxic T cells requires newly synthesized polypeptides for presentation by major histocompatibility complex (MHC) class I molecules. These polypeptides are produced not only from conventional AUG-initiated, but also from cryptic non-AUG-initiated, reading frames by distinct translational mechanisms. Biochemical analysis of ribosomal initiation complexes at CUG versus AUG initiation codons revealed that cells use an elongator leucine-bound transfer RNA (Leu-tRNA) to initiate translation at cryptic CUG start codons. CUG/Leu-tRNA initiation was independent of the canonical initiator tRNA (AUG/Met-tRNA(i)(Met)) pathway but required expression of eukaryotic initiation factor 2A. Thus, a tRNA-based translation initiation mechanism allows non-AUG-initiated protein synthesis and supplies peptides for presentation by MHC class I molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Starck, Shelley R -- Jiang, Vivian -- Pavon-Eternod, Mariana -- Prasad, Sharanya -- McCarthy, Brian -- Pan, Tao -- Shastri, Nilabh -- New York, N.Y. -- Science. 2012 Jun 29;336(6089):1719-23. doi: 10.1126/science.1220270.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Immunology and Pathogenesis, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22745432" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen Presentation/*genetics ; Antigen-Presenting Cells/immunology ; COS Cells ; Cercopithecus aethiops ; *Codon, Initiator ; HeLa Cells ; Histocompatibility Antigens Class I/*genetics/*immunology ; Humans ; Hybridomas/immunology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Peptide Chain Initiation, Translational ; Protein Biosynthesis/*genetics ; *RNA, Transfer, Leu ; T-Lymphocytes/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Codon-usage-based inhibition of HIV protein synthesis by human schlafen 11 (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-09-25
    Description: In mammals, one of the most pronounced consequences of viral infection is the induction of type I interferons, cytokines with potent antiviral activity. Schlafen (Slfn) genes are a subset of interferon-stimulated early response genes (ISGs) that are also induced directly by pathogens via the interferon regulatory factor 3 (IRF3) pathway. However, many ISGs are of unknown or incompletely understood function. Here we show that human SLFN11 potently and specifically abrogates the production of retroviruses such as human immunodeficiency virus 1 (HIV-1). Our study revealed that SLFN11 has no effect on the early steps of the retroviral infection cycle, including reverse transcription, integration and transcription. Rather, SLFN11 acts at the late stage of virus production by selectively inhibiting the expression of viral proteins in a codon-usage-dependent manner. We further find that SLFN11 binds transfer RNA, and counteracts changes in the tRNA pool elicited by the presence of HIV. Our studies identified a novel antiviral mechanism within the innate immune response, in which SLFN11 selectively inhibits viral protein synthesis in HIV-infected cells by means of codon-bias discrimination.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3705913/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3705913/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Manqing -- Kao, Elaine -- Gao, Xia -- Sandig, Hilary -- Limmer, Kirsten -- Pavon-Eternod, Mariana -- Jones, Thomas E -- Landry, Sebastien -- Pan, Tao -- Weitzman, Matthew D -- David, Michael -- AI074967/AI/NIAID NIH HHS/ -- AI81019/AI/NIAID NIH HHS/ -- P01 AI090935/AI/NIAID NIH HHS/ -- P01AI090935/AI/NIAID NIH HHS/ -- P30AI36214/AI/NIAID NIH HHS/ -- R01 GM101982/GM/NIGMS NIH HHS/ -- R01GM101982/GM/NIGMS NIH HHS/ -- R21 AI088490/AI/NIAID NIH HHS/ -- R21AI088490/AI/NIAID NIH HHS/ -- England -- Nature. 2012 Nov 1;491(7422):125-8. doi: 10.1038/nature11433. Epub 2012 Sep 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular Biology, Division of Biological Sciences, University of California San Diego, La Jolla, California 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23000900" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cells, Cultured ; Codon/*genetics/immunology ; Gene Expression Regulation, Viral/*genetics ; HEK293 Cells ; HIV-1/*genetics/growth & development/immunology/metabolism ; Humans ; Immunity, Innate ; Nuclear Proteins/immunology/*metabolism ; Protein Biosynthesis/*genetics/immunology ; RNA, Transfer/genetics/metabolism ; RNA, Viral/genetics/metabolism ; Reverse Transcription ; Species Specificity ; Substrate Specificity ; Viral Proteins/*biosynthesis/*genetics ; Virus Integration
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Vaccinia and influenza A viruses select rather than adjust tRNAs to optimize translation (2013)
    Oxford University Press
    Details
    Publication Date: 2013-02-02
    Description: Transfer RNAs (tRNAs) are central to protein synthesis and impact translational speed and fidelity by their abundance. Here we examine the extent to which viruses manipulate tRNA populations to favor translation of their own genes. We study two very different viruses: influenza A virus (IAV), a medium-sized (13 kB genome) RNA virus; and vaccinia virus (VV), a large (200 kB genome) DNA virus. We show that the total cellular tRNA population remains unchanged following viral infection, whereas the polysome-associated tRNA population changes dramatically in a virus-specific manner. The changes in polysome-associated tRNA levels reflect the codon usage of viral genes, suggesting the existence of local tRNA pools optimized for viral translation.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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  • 4
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    Vaccinia and influenza A viruses select rather than adjust tRNAs to optimize translation (2012)
    Oxford University Press
    Details
    Publication Date: 2012-12-18
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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