ribonuclease MRP complex

GO:0000172 · Ribonucleoprotein · Ribonucleoprotein complex · Proposed

A ribonucleoprotein complex that contains an RNA molecule of the snoRNA family, and cleaves the rRNA precursor as part of rRNA transcript processing. It also has other roles: In S. cerevisiae it is involved in cell cycle-regulated degradation of daughter cell-specific mRNAs, while in mammalian cells it also enters the mitochondria and processes RNAs to create RNA primers for DNA replication. [GO:0000172]

Synonyms: RNase MRP complex; ribonuclease mitochondrial RNA processing complex

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Essential	Role
RNase MRP RNA	Rna	part of	`SO:0000385`	NME1, RMRP	ESSENTIAL	Essential RNA subunit that distinguishes RNase MRP from the related RNase P ribonucleoprotein. `GO:0000172` GO:0000172 defines the ribonuclease MRP complex as a ribonucleoprotein complex containing an RNA molecule of the snoRNA family. `SO:0000385` SO:0000385 is the Sequence Ontology term for RNase MRP RNA. `DOI:10.1128/MCB.24.3.945-953.2004` Gill et al. 2004 describe NME1 as the Saccharomyces cerevisiae gene for MRP RNA.
shared RNase P/MRP protein subunits	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1	UNKNOWN	Protein constituents shared by the yeast RNase MRP and nuclear RNase P ribonucleoproteins that form the protein-rich eukaryotic catalytic architecture. `DOI:10.1093/nar/gkm553` Aspinall et al. 2007 analyzed all ten known S. cerevisiae RNase MRP protein subunits and reported direct protein-protein and protein-RNA interactions among them. `DOI:10.1261/rna.2214510` Esakova and Krasilnikov 2010 reviewed the shared eukaryotic RNase P/MRP proteins and the evolutionarily related RNase P/MRP architecture.
RNase MRP-specific protein subunits	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	SNM1, RMP1	UNKNOWN	Protein constituents that distinguish budding-yeast RNase MRP from the related nuclear RNase P complex. `DOI:10.1093/nar/gkm553` Aspinall et al. 2007 describe Snm1p and Rmp1p as S. cerevisiae RNase MRP protein subunits outside the eight proteins shared with RNase P. `DOI:10.1128/MCB.24.3.945-953.2004` Gill et al. 2004 describe SNM1 as encoding an RNA-binding protein associated with RNase MRP RNA but not RNase P RNA.

Taxonomic distribution

NCBITaxon:4932 Saccharomyces cerevisiae — COMMON: The RNase MRP complex is directly evidenced in budding yeast; broader eukaryotic distribution is left for follow-up curation. [DOI:10.1093/nar/gkm553]

Canonical examples

NCBITaxon:4932 Saccharomyces cerevisiae — Model eukaryote in which RNase MRP NME1 RNA, Snm1p and shared RNase P/MRP proteins have been studied as constituents of the RNase MRP ribonucleoprotein. [DOI:10.1093/nar/gkm553]

Functions

ribonuclease MRP activity GO:0000171 — The ribonuclease MRP complex cleaves RNA substrates by a catalytic RNA-mediated endoribonuclease mechanism.
- GO:0000171 GO:0000171 is the Gene Ontology molecular-function term for ribonuclease MRP activity.
- DOI:10.1093/nar/gkm553 Aspinall et al. 2007 studied yeast RNase MRP as an endonuclease complex and mapped interactions between protein subunits, MRP RNA and pre-rRNA.
endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) GO:0000479 — Budding-yeast RNase MRP cleaves the internal transcribed spacer 1 of pre-rRNA at the A3 site to promote formation of the mature 5-prime end of 5.8S rRNA.
- GO:0000479 GO:0000479 covers endonucleolytic cleavage of tricistronic rRNA transcripts during rRNA processing.
- DOI:10.1128/mcb.13.12.7935-7941.1993 Schmitt and Clayton 1993 connected nuclear RNase MRP to pre-5.8S rRNA processing in S. cerevisiae.
- DOI:10.1073/pnas.91.2.659 Chu et al. 1994 showed that the NME1-encoded RNase MRP RNA is required for normal yeast rRNA processing.

Mechanism graphs

Yeast RNase MRP cleaves pre-rRNA and CLB2 mRNA (FUNCTION)

In Saccharomyces cerevisiae, MRP RNA assembles with shared RNase P/MRP proteins and MRP-specific proteins into an RNase MRP ribonucleoprotein that cleaves pre-rRNA and CLB2 mRNA substrates.

Subject	Predicate	Object	Evidence
RNase MRP RNA	assembles with	shared RNase P/MRP protein subunits	`DOI:10.1093/nar/gkm553` Aspinall et al. 2007 mapped direct interactions among the yeast RNase MRP proteins and MRP RNA.
RNase MRP-specific protein subunits	assembles with	RNase MRP RNA	`DOI:10.1093/nar/gkm553` Aspinall et al. 2007 confirmed Rmp1p as an integral S. cerevisiae RNase MRP subunit through interactions with Snm1p and MRP RNA.
RNase MRP RNA	contributes to	ribonuclease MRP activity	`GO:0000172` GO:0000172 defines the complex as an RNA-containing ribonucleoprotein. `DOI:10.1261/rna.2214510` Esakova and Krasilnikov 2010 reviewed eukaryotic RNase P/MRP RNA components as the ribonucleoprotein catalytic cores.
ribonuclease MRP complex	cleaves	pre-rRNA	`DOI:10.1128/mcb.13.12.7935-7941.1993` Schmitt and Clayton 1993 implicated nuclear RNase MRP in pre-5.8S rRNA processing. `DOI:10.1073/pnas.91.2.659` Chu et al. 1994 connected the NME1 RNase MRP RNA to normal ribosomal RNA processing.
ribonuclease MRP complex	cleaves	CLB2 mRNA	`DOI:10.1128/MCB.24.3.945-953.2004` Gill et al. 2004 assayed RNase MRP-dependent CLB2 mRNA cleavage in vitro and in vivo.
ribonuclease MRP complex	supports	endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)	`GO:0000479` GO:0000479 covers endonucleolytic cleavage of the eukaryotic tricistronic rRNA precursor. `DOI:10.1128/mcb.13.12.7935-7941.1993` Schmitt and Clayton 1993 showed that nuclear RNase MRP is required for correct pre-5.8S rRNA processing in S. cerevisiae.

Discussions

CURATION_TODO (OPEN): Resolve exact source-neutral InterPro, Pfam, NCBIfam, GO or Complex Portal groundings for individual RNase MRP protein families; decide whether Snm1p and Rmp1p should remain a yeast-specific cohort or be split. The initial GO:0000172 record captures the MRP RNA, the eight budding-yeast proteins shared with nuclear RNase P and the Snm1p/Rmp1p MRP-specific proteins at cohort granularity. Exact family boundaries and cross-eukaryotic orthology should be resolved before assigning protein groundings.

Evidence

GO:0000172 Gene Ontology cellular-component term for the ribonuclease MRP complex and its exact synonyms.
GO:1902555 Gene Ontology cellular-component parent term for endoribonuclease complex.
GO:0000171 Gene Ontology molecular-function term for ribonuclease MRP activity.
GO:0000479 Gene Ontology biological-process term for endonucleolytic cleavage of tricistronic rRNA transcript.
SO:0000385 Sequence Ontology term for RNase MRP RNA.
DOI:10.1093/nar/gkm553 Aspinall et al. 2007, Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture, Nucleic Acids Research.
DOI:10.1261/rna.2214510 Esakova and Krasilnikov 2010, Of proteins and RNA: the RNase P/MRP family, RNA.
DOI:10.1128/mcb.13.12.7935-7941.1993 Schmitt and Clayton 1993, Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae, Molecular and Cellular Biology.
DOI:10.1073/pnas.91.2.659 Chu et al. 1994, The RNA of RNase MRP is required for normal processing of ribosomal RNA, Proceedings of the National Academy of Sciences.
DOI:10.1128/MCB.24.3.945-953.2004 Gill et al. 2004, RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression, Molecular and Cellular Biology.

Curation history

2026-09-24T12:13:59Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-09-24T12:15:30Z codex · EXPANDED_RECORD — Added RNase MRP synonymy, an endoribonuclease-complex parent, SO-grounded RNase MRP RNA plus label-only shared and MRP-specific protein cohorts, budding-yeast distribution, GO ribonuclease MRP and rRNA-cleavage functions, GO/SO/PubMed/DOI evidence, a yeast RNA-cleavage graph and a component-grounding TODO.
2026-09-24T12:27:05Z codex · ADDRESS_REVIEW — #1486: reworded the Snm1p/Rmp1p causal-graph edge so the grouped MRP-specific protein cohort is not described as self-associated; #1487: softened the RNase MRP RNA component role and graph edge to avoid assigning an unqualified catalytic/scaffold role at component granularity.

Source: data/structures/ribonucleoprotein/ribonuclease_mrp_complex.yaml