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PMID: 17412707 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Nucleic acids research ·Vol. 35 ·No. 8 ·2007-00-00 ·Pages 2564-72

Schilders G, van Dijk E, Pruijn GJ

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.

MeSH Terms
Cell Line Cell Nucleolus/chemistry,enzymology Co-Repressor Proteins Exoribonucleases/analysis,metabolism,physiology Exosome Multienzyme Ribonuclease Complex Humans Nuclear Proteins/analysis,metabolism,physiology RNA 3' End Processing RNA Helicases/analysis,metabolism,physiology RNA Precursors/metabolism RNA, Ribosomal, 5.8S/metabolism RNA-Binding Proteins/metabolism Repressor Proteins/analysis,metabolism,physiology
Chemicals
C1D protein, human Co-Repressor Proteins M-phase phosphoprotein 6, human Nuclear Proteins RNA Precursors RNA, Ribosomal, 5.8S RNA-Binding Proteins Repressor Proteins Exoribonucleases Exosome Multienzyme Ribonuclease Complex EXOSC10 protein, human MTREX protein, human RNA Helicases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Schilders Geurt
Department of Biomolecular Chemistry, Nijmegen Center for Molecular Life Sciences, Institute for Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands.
van Dijk Erwin
Pruijn Ger J M
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
DOI
10.1093/nar/gkm082
Published
2007-00-00
Epub
2007-00-04
Pages
2564-72
Language
English
Region
England
NLM ID
0411011
PMCID
PMC1885644
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/gkm082 PMC Full Text View journal details
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