dimeric ribonuclease P complex

GO:0030680 · Ribonucleoprotein · Ribonucleoprotein complex · Proposed

A ribonuclease P complex that contains a single RNA molecule that is necessary and usually sufficient for catalysis, and a single protein molecule. [GO:0030680]

Synonyms: dimeric RNase P complex

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

Components

Component	Type	Part of / acts on	Grounding	Genes	Stoichiometry	Essential	Role
RNase P RNA	Rna	part of	`SO:0000386`	rnpB	1 RNA molecule	ESSENTIAL	Catalytic RNA subunit that forms the bacterial RNase P ribozyme core. `GO:0030680` GO:0030680 defines the dimeric ribonuclease P complex as containing a single RNA molecule that is necessary and usually sufficient for catalysis. `SO:0000386` SO:0000386 is the Sequence Ontology term for RNase P RNA. `PMID:6197186` Guerrier-Takada et al. 1983 showed that the RNA moiety of bacterial RNase P is the catalytic subunit.
Ribonuclease P protein component	Protein	part of	`InterPro:IPR000100`	rnpA	1 protein molecule	ESSENTIAL	Small RnpA protein constituent that associates with RNase P RNA in the bacterial dimeric holoenzyme. `GO:0030680` GO:0030680 defines the dimeric ribonuclease P complex as containing a single protein molecule. `InterPro:IPR000100` InterPro IPR000100 is a family entry for RNase P protein components that includes the bacterial rnpA HAMAP and NCBIfam member models. `DOI:10.1038/nrmicro1491` Kazantsev and Pace 2006 reviewed bacterial RNase P as a two-component holoenzyme with an RNA subunit and an RnpA protein subunit.

Organism-specific protein examples

Named proteins in which each component's role was established, with the organism the evidence comes from. The component above is the taxon-agnostic family; these are the specific entries behind it.

Ribonuclease P protein component

Accession	Protein	Gene	Organism	Entry
`UniProtKB:P0A7Y8`	Ribonuclease P protein component	rnpA	Escherichia coli K-12 (`NCBITaxon:83333`)	REVIEWED
Role and evidence (2 references) Reviewed E. coli K-12 RnpA entry mapped by UniProtKB to InterPro:IPR000100. `UniProtKB:P0A7Y8` UniProtKB P0A7Y8 is the reviewed Escherichia coli K-12 RNase P protein component entry for gene rnpA. `InterPro:IPR000100` UniProtKB maps the E. coli K-12 RnpA entry to InterPro family IPR000100.

Canonical examples

NCBITaxon:562 Escherichia coli — Model bacterium whose RNase P M1 RNA established the RNA moiety as a catalytic subunit. [PMID:6197186]

Functions

ribonuclease P activity GO:0004526 — The bacterial dimeric RNase P complex cleaves RNA endonucleolytically to remove 5-prime extra nucleotides from precursor tRNA.
- GO:0004526 GO:0004526 is the Gene Ontology molecular-function term for ribonuclease P activity.
- PMID:6197186 Guerrier-Takada et al. 1983 assayed bacterial RNase P RNA cleavage of precursor RNA substrates.
tRNA 5'-leader removal GO:0001682 — The RNase P complex generates mature tRNA 5-prime ends by cleaving 5-prime leader sequences from pre-tRNAs.
- GO:0001682 GO:0001682 is the Gene Ontology biological-process term for tRNA 5'-leader removal.
- DOI:10.1038/nrmicro1491 Kazantsev and Pace 2006 reviewed tRNA 5-prime leader removal as the canonical bacterial RNase P activity.

Mechanism graphs

Dimeric RNase P cleaves pre-tRNA leaders (FUNCTION)

In bacterial dimeric RNase P, the RNase P RNA and RnpA protein form a ribonucleoprotein holoenzyme that cleaves 5-prime leaders from precursor tRNAs.

Subject	Predicate	Object	Evidence
RNase P RNA	assembles with	Ribonuclease P protein component	`GO:0030680` GO:0030680 defines the dimeric ribonuclease P complex by one RNA molecule and one protein molecule. `DOI:10.1038/nrmicro1491` Kazantsev and Pace 2006 reviewed the two-component bacterial RNase P holoenzyme.
RNase P RNA	contributes to	ribonuclease P activity	`PMID:6197186` Guerrier-Takada et al. 1983 established bacterial RNase P RNA as a catalytic subunit.
dimeric ribonuclease P complex	cleaves	precursor tRNA	`GO:0004526` GO:0004526 defines ribonuclease P activity as endonucleolytic removal of 5-prime extra nucleotides from tRNA precursor. `DOI:10.1038/nrmicro1491` Kazantsev and Pace 2006 reviewed pre-tRNA leader cleavage as the canonical bacterial RNase P reaction.
dimeric ribonuclease P complex	supports	tRNA 5'-leader removal	`GO:0030680` GO:0030680 defines the ribonuclease P complex by its cleavage of pre-tRNA leader sequences. `DOI:10.1038/nrmicro1491` Kazantsev and Pace 2006 reviewed bacterial RNase P as an RNA-plus-protein particle that catalyzes tRNA 5-prime maturation. `GO:0001682` GO:0001682 is the biological-process term for tRNA 5'-leader removal.

Discussions

CURATION_TODO (OPEN): Keep this record scoped to the bacterial dimeric RNase P complex and curate multimeric archaeal, nucleolar and mitochondrial RNase P complexes separately. GO separates the single-RNA/single-protein dimeric complex from multimeric and organellar RNase P variants. This first record intentionally models only GO:0030680.

Evidence

GO:0030680 Gene Ontology cellular-component term for the dimeric ribonuclease P complex.
GO:0030677 Gene Ontology cellular-component term for the broader ribonuclease P complex parent.
GO:0004526 Gene Ontology molecular-function term for ribonuclease P activity.
GO:0001682 Gene Ontology biological-process term for tRNA 5'-leader removal.
SO:0000386 Sequence Ontology term for RNase P RNA.
InterPro:IPR000100 InterPro family for RNase P protein components.
UniProtKB:P0A7Y8 UniProtKB reviewed Escherichia coli K-12 RnpA protein entry.
PMID:6197186 Guerrier-Takada et al. 1983, The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme, Cell.
DOI:10.1038/nrmicro1491 Kazantsev and Pace 2006, Bacterial RNase P: a new view of an ancient enzyme, Nature Reviews Microbiology.
PMID:16980936 PubMed identifier for Kazantsev and Pace 2006 as reported by PubMed.

Curation history

2026-09-24T11:36:39Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-09-24T11:37:53Z codex · EXPANDED_RECORD — Added RNase P synonymy, ribonuclease P parentage, SO-grounded RNase P RNA and InterPro-grounded RnpA components, bacterial distribution, an Escherichia coli canonical example, GO function terms, GO/SO/InterPro/UniProt/PubMed/DOI evidence, a compact pre-tRNA cleavage graph and a scope TODO for non-dimeric RNase P variants.
2026-09-24T11:50:21Z codex · ADDRESS_REVIEW — #1483: added GO:0030680 and DOI:10.1038/nrmicro1491 to the RNase P tRNA 5-prime leader-removal graph edge so the edge evidence supports the subject structure as well as the biological-process node; #1484: removed the broad Bacteria COMMON taxonomic-distribution row until a source directly supports that clade-level frequency.

Source: data/structures/ribonucleoprotein/dimeric_ribonuclease_p_complex.yaml