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Cited by 132RNA Research and SplicingNuclear Structure and FunctionRNA and protein synthesis mechanisms

C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing

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Schilders, G., van Dijk, E., Pruijn, G. J.M.·2007·Nucleic Acids Research
DOI 10.1093/nar/gkm082PMC PMC1885644
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Abstract

The exosome is a complex of 3'-5' exoribonucleases and RNA-binding proteins, which is involved in processing or degradation of different classes of RNA. Previously, the characterization of purified exosome complexes from yeast and human cells suggested that C1D and KIAA0052/hMtr4p are associated with the exosome and thus might regulate its functional activities. Subcellular localization experiments demonstrated that C1D and KIAA0052/hMtr4p co-localize with exosome subunit PM/Scl-100 in the nucleoli of HEp-2 cells. Additionally, the nucleolar accumulation of C1D appeared to be dependent on PM/Scl-100. Protein-protein interaction studies showed that C1D binds to PM/Scl-100, whereas KIAA0052/hMtr4p was found to interact with MPP6, a previously identified exosome-associated protein. Moreover, we demonstrate that C1D, MPP6 and PM/Scl-100 form a stable trimeric complex in vitro. Knock-down of C1D, MPP6 and KIAA0052/hMtr4p by RNAi resulted in the accumulation of 3'-extended 5.8S rRNA precursors, showing that these proteins are required for rRNA processing. Interestingly, C1D appeared to contain RNA-binding activity with a potential preference for structured RNAs. Taken together, our results are consistent with a role for the exosome-associated proteins C1D, MPP6 and KIAA052/hMtr4p in the recruitment of the exosome to pre-rRNA to mediate the 3' end processing of the 5.8S rRNA.

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Authors
Schilders, G., van Dijk, E., & Pruijn, G. J. M.
Affiliations
Radboud University Nijmegen (NL)
Corresponding author
Pruijn, G. J.M.
ORCID
Pruijn, G. J.M.
Venue
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Published
2007-03-29
Volume
35
Issue
8
Pages
2564-2572
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
DOI
10.1093/nar/gkm082
PMC
PMC1885644
OpenAlex
W1999721918
Cited by
132
References
0
Citations by year
2026: 5 · 2025: 3 · 2023: 2 · 2022: 4 · 2021: 7 · 2020: 9 · 2019: 6 · 2018: 11 · 2017: 12 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 12 · 2012: 7
FWCI
3.58
Type
journal article
Language
en
Open access
Licence
cc-by-nc
Locations
  • Nucleic Acids Research (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • Radboud Repository (Radboud University) (submittedVersion)
  • Radboud Repository (Radboud University) (submittedVersion, other-oa)
Funders
  • Radboud Universiteit
  • Nederlandse Organisatie voor Wetenschappelijk Onderzoek
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
exosomes, MPP6, pre-rRNA processing, nucleolus, RNA-binding activity, protein-protein interaction, trimeric complex, HEp-2 cells
MeSH terms
Cell Line, Cell Nucleolus, Exoribonucleases, Humans, Nuclear Proteins, Repressor Proteins, RNA Precursors, RNA, Ribosomal, 5.8S, RNA-Binding Proteins, RNA Helicases, RNA 3' End Processing, Co-Repressor Proteins, Exosome Multienzyme Ribonuclease Complex

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