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Membrane-association of mRNA decapping factors is independent of stress in budding yeast
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
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2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, 25477Article in journal (Refereed) Published
Abstract [en]

Recent evidence has suggested that the degradation of mRNA occurs on translating ribosomes or alternatively within RNA granules called P bodies, which are aggregates whose core constituents are mRNA decay proteins and RNA. In this study, we examined the mRNA decapping proteins, Dcp1, Dcp2, and Dhh1, using subcellular fractionation. We found that decapping factors co-sediment in the polysome fraction of a sucrose gradient and do not alter their behaviour with stress, inhibition

of translation or inhibition of the P body formation. Importantly, their localisation to the polysome fraction is independent of the RNA, suggesting that these factors may be constitutively localised to the polysome. Conversely, polysomal and post-polysomal sedimentation of the decapping proteins was abolished with the addition of a detergent, which shifts the factors to the non-translating RNP fraction and is consistent with membrane association. Using a membrane otation assay, we observed the mRNA decapping factors in the lower density fractions at the buoyant density of membrane-associated proteins. These observations provide further evidence that mRNA decapping factors interact with subcellular membranes, and we suggest a model in which the mRNA decapping factors interact with membranes to facilitate regulation of mRNA degradation. 

Place, publisher, year, edition, pages
2016. Vol. 6, 25477
National Category
Biochemistry and Molecular Biology
Research subject
Molecular Biology; cellforskning
URN: urn:nbn:se:umu:diva-120043DOI: 10.1038/srep25477ISI: 000375544400001PubMedID: 27146487OAI: diva2:926296
Carl Tryggers foundation , 11:330Swedish Research Council, 621-2010-4602
Available from: 2016-05-05 Created: 2016-05-05 Last updated: 2016-06-30Bibliographically approved

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Huch, SusanneMuppavarapu, MridulaNissan, Tracy
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