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Rrp6 is recruited to transcribed genes and accompanies the spliced mRNA to the nuclear pore
Stockholm University, Faculty of Science, Department of Molecular Biology and Functional Genomics.
Stockholm University, Faculty of Science, Department of Molecular Biology and Functional Genomics.
Stockholm University, Faculty of Science, Department of Molecular Biology and Functional Genomics.
Stockholm University, Faculty of Science, Department of Molecular Biology and Functional Genomics.
2012 (English)In: RNA: A publication of the RNA Society, ISSN 1355-8382, E-ISSN 1469-9001, Vol. 18, no 8, 1466-1474 p.Article in journal (Refereed) Published
Abstract [en]

Rrp6 is an exoribonuclease involved in the quality control of mRNA biogenesis. We have analyzed the association of Rrp6 with the Balbiani ring pre-mRNPs of Chironomus tentans to obtain insight into the role of Rrp6 in splicing surveillance. Rrp6 is recruited to transcribed genes and its distribution along the genes does not correlate with the positions of exons and introns. In the nucleoplasm, Rrp6 is bound to both unspliced and spliced transcripts. Rrp6 is released from the mRNPs in the vicinity of the nuclear pore before nucleo-cytoplasmic translocation. We show that Rrp6 is associated with newly synthesized transcripts during all the nuclear steps of gene expression and is associated with the transcripts independently of their splicing status. These observations suggest that the quality control of pre-mRNA splicing is not based on the selective recruitment of the exoribonuclease Rrp6 to unprocessed mRNAs.

Place, publisher, year, edition, pages
2012. Vol. 18, no 8, 1466-1474 p.
Keyword [en]
pre-mRNA splicing, surveillance, exosome, Chironomus tentans, nuclear bodies
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-80609DOI: 10.1261/rna.032045.111ISI: 000306420200004OAI: oai:DiVA.org:su-80609DiVA: diva2:556882
Note

AuthorCount:4;

Available from: 2012-09-26 Created: 2012-09-25 Last updated: 2017-12-07Bibliographically approved

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