Rrp36 is a conserved nucleolar ribosome-biogenesis factor associated with the 90S preribosome. It supports early processing of the small-subunit rRNA precursor and production of the 40S ribosomal subunit. Comparative experiments in budding yeast and human cells establish a conserved requirement for early pre-rRNA cleavages, while fission yeast localization and curated phylogenetic evidence support the corresponding role of Rrp36. An intrinsic RNA-cleaving activity has not been established.
Existing Annotations Review
GO Term
Evidence
Action
Reason
GO:0000462 maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
IBA GO_REF:0000033
ACCEPT
Summary: maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
Reason: Rrp36 participates in preribosome assembly and processing, but the reviewed experiments do not establish an intrinsic enzymatic or specific binding activity. Retain the ND molecular-function root instead of inventing an rRNA nuclease activity.
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...
ACCEPT
Summary: nucleus is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...
ACCEPT
Summary: nucleolus is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
Core Functions
Nucleolar 90S preribosome factor supporting early small-subunit rRNA maturation; function transferred from characterized RRP36 orthologs.
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
Rrp36 is a conserved 90S preribosome factor supporting small-subunit rRNA maturation. Both predictions are supported but less precise than the established process and complex assignments.
Review rationale: The specific RRP36 domain and target nucleolar localization support the conserved preribosome role inferred by PAINT. Purification and depletion in budding yeast establish 90S/pre-40S association and early small-subunit rRNA maturation; human depletion supports conservation across eukaryotes. GOA already records maturation of SSU-rRNA from tricistronic rRNA transcript (GO:0000462). The broad rRNA-processing prediction is supported but loses small-subunit specificity; no intrinsic RNase chemistry is implied.
Supporting Evidence:
PMID:20038530: "We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels."
Review rationale: Rrp36 belongs to a specifically identified ribosome-biogenesis family; characterized ortholog copurification with RNA-containing 90S and pre-40S particles establishes the relevant complex type. Curated ancestral inference already places fission yeast Rrp36 in the 90S preribosome (GO:0030686), consistent with its nucleolar localization. A ribonucleoprotein complex is a broader description of that supported complex membership. The prediction is correct but less precise than the existing 90S assignment.
Supporting Evidence:
PMID:20038530: "We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels."