期刊
EMBO JOURNAL
卷 29, 期 14, 页码 2342-2357出版社
WILEY
DOI: 10.1038/emboj.2010.121
关键词
human exosome; ribonuclease; RNA degradation; RNase II/R enzymes; RNB domain
资金
- Polish Ministry of Science and Higher Education [N N301 250836]
- EU
- Operational Program Innovative Economy
- EMBO
- Faculty of Biology, University of Warsaw [BW-179110]
- Foundation for Polish Science
- Danish National Research Foundation
- Danish Cancer Society
- Danish Council for Independent Research (Natural Sciences)
- European Science Foundation (ESF)
- European Commission [HEALTH-F4-2008-201648/PROSPECTS]
The eukaryotic RNA exosome is a ribonucleolytic complex involved in RNA processing and turnover. It consists of a nine-subunit catalytically inert core that serves a structural function and participates in substrate recognition. Best defined in Saccharomyces cerevisiae, enzymatic activity comes from the associated subunits Dis3p (Rrp44p) and Rrp6p. The former is a nuclear and cytoplasmic RNase II/R-like enzyme, which possesses both processive exo- and endonuclease activities, whereas the latter is a distributive RNase D-like nuclear exonuclease. Although the exosome core is highly conserved, identity and arrangements of its catalytic subunits in different vertebrates remain elusive. Here, we demonstrate the association of two different Dis3p homologs-hDIS3 and hDIS3L-with the human exosome core. Interestingly, these factors display markedly different intracellular localizations: hDIS3 is mainly nuclear, whereas hDIS3L is strictly cytoplasmic. This compartmental distribution reflects the substrate preferences of the complex in vivo. Both hDIS3 and hDIS3L are active exonucleases; however, only hDIS3 has retained endonucleolytic activity. Our data suggest that three different ribonucleases can serve as catalytic subunits for the exosome in human cells. The EMBO Journal (2010) 29, 2342-2357. doi:10.1038/emboj.2010.121; Published online 8 June 2010
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