Rrp6 is recruited to transcribed genes and accompanies the spliced mRNA to the nuclear pore
(2012) In RNA 18(8). p.74-1466- Abstract
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... (More)
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.
(Less)
- author
- Hessle, Viktoria ; von Euler, Anne ; González de Valdivia, Ernesto LU and Visa, Neus
- publishing date
- 2012-08
- type
- Contribution to journal
- publication status
- published
- keywords
- Animals, Blotting, Western, Cell Nucleus, Cells, Cultured, Chironomidae, Chromatin Immunoprecipitation, Cytoplasm, Drosophila Proteins, Drosophila melanogaster, Exons, Exosome Multienzyme Ribonuclease Complex, Fluorescent Antibody Technique, Introns, Nuclear Pore, Nuclear Proteins, RNA Precursors, RNA Splicing, RNA, Messenger, Rabbits, Ribonucleoproteins, Salivary Glands, Transcription, Genetic, Journal Article, Research Support, Non-U.S. Gov't
- in
- RNA
- volume
- 18
- issue
- 8
- pages
- 9 pages
- publisher
- Cold Spring Harbor Laboratory Press (CSHL)
- external identifiers
-
- pmid:22745224
- scopus:84864072645
- ISSN
- 1355-8382
- DOI
- 10.1261/rna.032045.111
- language
- English
- LU publication?
- no
- id
- 60b89f21-9b6f-4deb-9d12-c79d9bf1cc4d
- date added to LUP
- 2018-01-12 17:02:26
- date last changed
- 2024-01-29 09:29:44
@article{60b89f21-9b6f-4deb-9d12-c79d9bf1cc4d, abstract = {{<p>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.</p>}}, author = {{Hessle, Viktoria and von Euler, Anne and González de Valdivia, Ernesto and Visa, Neus}}, issn = {{1355-8382}}, keywords = {{Animals; Blotting, Western; Cell Nucleus; Cells, Cultured; Chironomidae; Chromatin Immunoprecipitation; Cytoplasm; Drosophila Proteins; Drosophila melanogaster; Exons; Exosome Multienzyme Ribonuclease Complex; Fluorescent Antibody Technique; Introns; Nuclear Pore; Nuclear Proteins; RNA Precursors; RNA Splicing; RNA, Messenger; Rabbits; Ribonucleoproteins; Salivary Glands; Transcription, Genetic; Journal Article; Research Support, Non-U.S. Gov't}}, language = {{eng}}, number = {{8}}, pages = {{74--1466}}, publisher = {{Cold Spring Harbor Laboratory Press (CSHL)}}, series = {{RNA}}, title = {{Rrp6 is recruited to transcribed genes and accompanies the spliced mRNA to the nuclear pore}}, url = {{http://dx.doi.org/10.1261/rna.032045.111}}, doi = {{10.1261/rna.032045.111}}, volume = {{18}}, year = {{2012}}, }