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PMID: 10199568 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

RNA-protein interactions in the human RNase MRP ribonucleoprotein complex.

RNA (New York, N.Y.) ·Vol. 5 ·No. 4 ·1999-04-00 ·Pages 512-24

Pluk H, van Eenennaam H, Rutjes SA, Pruijn GJ, van Venrooij WJ

Abstract

The eukaryotic nucleolus contains a large number of small RNA molecules that, in the form of small nucleolar ribonucleoprotein complexes (snoRNPs), are involved in the processing and modification of pre-rRNA. One of the snoRNPs that has been shown to possess enzymatic activity is the RNase MRP. RNase MRP is an endoribonuclease involved in the formation of the 5' end of 5.8S rRNA. In this study the association of the hPop1 protein with the RNase MRP complex was investigated. The hPop1 protein seems not to be directly bound to the RNA component, but requires nt 1-86 and 116-176 of the MRP RNA to associate with the RNase MRP complex via protein-protein interactions. UV crosslinking followed by ribonuclease treatment and immunoprecipitation with anti-Th/To antibodies revealed three human proteins of about 20, 25, and 40 kDa that can associate with the RNase MRP complex. The 20- and 25-kDa proteins appear to bind to stem-loop I of the MRP RNA whereas the 40-kDa protein requires the central part of the MRP RNA (nt 86-176) for association with the RNase MRP complex. In addition, we show that the human RNase P proteins Rpp30 and Rpp38 are also associated with the RNase MRP complex. Expression of Vesicular Stomatitis Virus- (VSV) tagged versions of these proteins in HeLa cells followed by anti-VSV immunoprecipitation resulted in coprecipitation of both RNase P and RNase MRP complexes. Furthermore, UV crosslinking followed by anti-Th/To and anti-Rpp38 immunoprecipitation revealed that the 40-kDa protein we detected in UV crosslinking is probably identical to Rpp38.

MeSH Terms
Apoptosis Regulatory Proteins Autoantigens/genetics Base Sequence Carrier Proteins Endoribonucleases/genetics,metabolism HeLa Cells Humans Molecular Sequence Data Mutation Nuclear Proteins/genetics Nucleic Acid Conformation RNA/genetics,metabolism RNA, Catalytic/genetics RNA-Binding Proteins Ribonuclease P Ribonucleoproteins/genetics,metabolism Sequence Deletion Vesicular stomatitis Indiana virus/genetics
Chemicals
Apoptosis Regulatory Proteins Autoantigens Carrier Proteins Nuclear Proteins POP1 protein, human RNA, Catalytic RNA-Binding Proteins RPP30 protein, human Ribonucleoproteins RNA Endoribonucleases mitochondrial RNA-processing endoribonuclease RPP14 protein, human RPP38 protein, human Ribonuclease P
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Pluk H
Department of Biochemistry, University of Nijmegen, The Netherlands.
van Eenennaam H
Rutjes S A
Pruijn G J
van Venrooij W J
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Article Info
Journal
RNA (New York, N.Y.)
Abbr.
RNA
ISSN
1355-8382
DOI
10.1017/s1355838299982079
Published
1999-04-00
Pages
512-24
Language
English
Region
United States
NLM ID
9509184
PMCID
PMC1369778
Subset
IM
External Links
PubMed source DOI: 10.1017/s1355838299982079 PMC Full Text View journal details
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