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Nuclear processing of nascent transcripts determines synthesis of full-length proteins and antigenic peptides
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2019 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 47, no 6, p. 3086-3100Article in journal (Refereed) Published
Abstract [en]

Peptides presented on major histocompatibility (MHC) class I molecules form an essential part of the immune system's capacity to detect virus-infected or transformed cells. Earlier works have shown that pioneer translation peptides (PTPs) for the MHC class I pathway are as efficiently produced from introns as from exons, or from mRNAs targeted for the nonsense-mediated decay pathway. The production of PTPs is a target for viral immune evasion but the underlying molecular mechanisms that govern this non-canonical translation are unknown. Here, we have used different approaches to show how events taking place on the nascent transcript control the synthesis of PTPs and full-length proteins. By controlling the subcellular interaction between the G-quadruplex structure (G4) of a gly-ala encoding mRNA and nucleolin (NCL) and by interfering with mRNA maturation using multiple approaches, we demonstrate that antigenic peptides derive from a nuclear non-canonical translation event that is independently regulated from the synthesis of full-length proteins. Moreover, we show that G4 are exploited to control mRNA localization and translation by distinguishable mechanisms that are targets for viral immune evasion.

Place, publisher, year, edition, pages
Oxford University Press, 2019. Vol. 47, no 6, p. 3086-3100
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Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-159621DOI: 10.1093/nar/gky1296ISI: 000467964800033PubMedID: 30624716OAI: oai:DiVA.org:umu-159621DiVA, id: diva2:1324163
Available from: 2019-06-13 Created: 2019-06-13 Last updated: 2019-06-13Bibliographically approved

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Martins, Rodrigo PradoBlondel, MarcFåhraeus, Robin
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