PNO1

UniProt ID: Q99216
Organism: Saccharomyces cerevisiae
Review Status: COMPLETE
Aliases:
DIM2 RRP20 YOR145C
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Gene Description

PNO1 encodes Pno1/Dim2/Rrp20, a conserved KH-domain ribosome biogenesis factor required for small ribosomal subunit synthesis. Pno1 binds pre-rRNA, especially the ITS1 region, participates in early SSU processome and 90S to pre-40S transitions, supports pre-40S export from the nucleus, and works with Nob1 and Rio1 during late cytoplasmic 20S pre-rRNA to 18S rRNA maturation. The coherent core function is RNA-binding regulation of SSU/pre-40S assembly and processing; older proteasome and generic chaperone annotations appear secondary or overextended.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005634 nucleus
IBA
GO_REF:0000033
ACCEPT
Summary: PANTHER IBA to nucleus is consistent with Pno1's conserved role as a nuclear/nucleolar and nucleocytoplasmic ribosome biogenesis factor.
Reason: Pno1 acts in nuclear and nucleolar stages of SSU biogenesis and has direct experimental nuclear/nucleolar localization support.
GO:0003723 RNA binding
IEA
GO_REF:0000120
ACCEPT
Summary: Automated RNA-binding annotation is supported by Pno1 KH domains and by direct evidence for binding pre-rRNA/ITS1.
Reason: RNA binding is a core molecular function for Pno1, though the more specific rRNA primary transcript binding term is preferred when available.
Supporting Evidence:
file:yeast/PNO1/PNO1-deep-research-falcon.md
binds pre-rRNA (ITS1 region) via its KH domain
GO:0005730 nucleolus
IEA
GO_REF:0000120
ACCEPT
Summary: UniProt/ARBA nucleolus mapping is consistent with Pno1 function in early nucleolar SSU processome assembly and pre-rRNA processing.
Reason: The nucleolus is a supported compartment for Pno1 during early ribosome biogenesis.
GO:0005737 cytoplasm
IEA
GO_REF:0000044
ACCEPT
Summary: Cytoplasmic localization is consistent with Pno1 shuttling and late cytoplasmic pre-40S maturation.
Reason: Pno1 functions after pre-40S export as part of late 18S rRNA maturation and quality-control gating.
GO:0042254 ribosome biogenesis
IEA
GO_REF:0000120
ACCEPT
Summary: Broad automated ribosome biogenesis annotation accurately summarizes the experimentally supported Pno1 role in SSU/pre-40S assembly and maturation.
Reason: Pno1 is a ribosome biogenesis factor; more specific annotations capture SSU-rRNA maturation, pre-40S export, and ribosome assembly.
GO:0005730 nucleolus
IDA
PMID:27980088
Architecture of the yeast small subunit processome.
ACCEPT
Summary: ComplexPortal direct assay evidence places Pno1 in the nucleolus/SSU processome context.
Reason: Nucleolar localization matches Pno1's early SSU processome and pre-rRNA processing roles.
Supporting Evidence:
PMID:27980088
Architecture of the yeast small subunit processome.
GO:0030490 maturation of SSU-rRNA
NAS
PMID:15489292
RNA polymerase I transcription and pre-rRNA processing are l...
ACCEPT
Summary: Curated statement evidence supports Pno1 as a specific SSU processome component linked to SSU-rRNA maturation.
Reason: The annotation is consistent with multiple yeast studies showing defects in pre-rRNA processing when Pno1/Dim2/Rrp20 is perturbed.
Supporting Evidence:
PMID:15489292
RNA polymerase I transcription and pre-rRNA processing are linked by specific SSU processome components.
GO:0000056 ribosomal small subunit export from nucleus
IMP
PMID:18755838
TOR regulates the subcellular distribution of DIM2, a KH dom...
ACCEPT
Summary: Mutant phenotype evidence supports Dim2/Pno1 involvement in pre-40S export from the nucleus.
Reason: Pno1 contains a conserved export-related region and perturbation causes pre-40S export defects, making this a core process annotation.
Supporting Evidence:
PMID:18755838
pre-40S ribosome export
GO:0042134 rRNA primary transcript binding
IDA
PMID:18755838
TOR regulates the subcellular distribution of DIM2, a KH dom...
ACCEPT
Summary: Direct assay evidence shows Dim2/Pno1 binds pre-rRNA through its KH domain at the 5' end of ITS1.
Reason: This is the most specific experimentally supported molecular function for Pno1 and should be considered core.
Supporting Evidence:
PMID:18755838
DIM2 binds pre-rRNAs directly through its KH domain
GO:0042255 ribosome assembly
IMP
PMID:18755838
TOR regulates the subcellular distribution of DIM2, a KH dom...
ACCEPT
Summary: Mutant phenotype evidence supports Dim2/Pno1 function in cotranscriptional ribosome assembly and pre-40S maturation.
Reason: Pno1 coordinates pre-rRNA binding, pre-40S export, and later maturation, so ribosome assembly is appropriate.
Supporting Evidence:
PMID:18755838
cotranscriptional ribosome assembly
GO:0030686 90S preribosome
HDA
PMID:12150911
90S pre-ribosomes include the 35S pre-rRNA, the U3 snoRNP, a...
ACCEPT
Summary: High-throughput direct assay evidence identifies Pno1/Rrp20 with 90S preribosomal particles.
Reason: This component annotation is consistent with Pno1's early SSU processome role.
Supporting Evidence:
PMID:12150911
90S pre-ribosomes include the 35S pre-rRNA
GO:0043248 proteasome assembly
IMP
PMID:12502737
Nob1p is required for biogenesis of the 26S proteasome and d...
MARK AS OVER ANNOTATED
Summary: The 2002 Nob1/Pno1 study connected pno1 defects with Pre6p accumulation and proteasome maturation, but subsequent literature and UniProt support a primary SSU ribosome biogenesis role for Pno1.
Reason: PMID:12502737 directly reports pno1 mutant proteasome maturation defects, but later Pno1/Dim2 literature supports ribosome biogenesis, pre-rRNA processing, and pre-40S maturation as the conserved core function. This proteasome assembly annotation is therefore retained only as a non-core/over-annotated phenotype from an older model.
Supporting Evidence:
PMID:12502737
A defect in either NOB1 or PNO1 caused accumulation of newly formed Pre6p
GO:0043248 proteasome assembly
IPI
PMID:12502737
Nob1p is required for biogenesis of the 26S proteasome and d...
MARK AS OVER ANNOTATED
Summary: The protein-interaction basis for proteasome assembly is not sufficient to override the now well-supported Pno1 role in SSU/pre-40S maturation.
Reason: The original paper did observe proteasome assembly defects in pno1 mutants, but the current weight of evidence places Pno1 as a Dim2/Rrp20 ribosome biogenesis factor. The proteasome annotation should therefore be treated as an over-annotated non-core phenotype rather than a primary molecular role.
Supporting Evidence:
PMID:12502737
temperature-sensitive nob1 and pno1 mutants exhibited defects in the processing of the beta subunits and in the assembly of the 20S and the 26S proteasomes
GO:0000447 endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
IMP
PMID:12736301
RRP20, a component of the 90S preribosome, is required for p...
ACCEPT
Summary: RRP20/PNO1 mutant phenotypes impair early pre-rRNA cleavages, including ITS1 processing that separates SSU from LSU rRNA precursors.
Reason: Pno1 is required for proper pre-rRNA processing as part of the SSU maturation pathway, although it is not itself the nuclease.
Supporting Evidence:
PMID:12736301
RRP20, a component of the 90S preribosome, is required for pre-18S rRNA processing
GO:0000472 endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
IMP
PMID:12736301
RRP20, a component of the 90S preribosome, is required for p...
ACCEPT
Summary: PNO1/RRP20 mutant evidence supports a requirement for proper pre-18S rRNA processing and mature SSU-rRNA formation.
Reason: The annotation captures a core process consequence of Pno1 function in SSU maturation.
Supporting Evidence:
PMID:12736301
defective in ribosomal RNA processing
GO:0005634 nucleus
IDA
PMID:12502737
Nob1p is required for biogenesis of the 26S proteasome and d...
ACCEPT
Summary: Direct assay evidence supports nuclear localization of Pno1.
Reason: Nuclear localization is consistent with Pno1's early pre-rRNA processing and pre-40S export roles.
Supporting Evidence:
PMID:12502737
Nob1p is a nuclear protein that forms a complex with the 19S regulatory particle of the 26S proteasome and with uncharacterized nuclear protein Pno1p
GO:0005730 nucleolus
IDA
PMID:10923024
Functional analysis of six genes from chromosomes XIV and XV...
ACCEPT
Summary: Direct GFP localization evidence places Yor145c/Pno1 in the nucleolus.
Reason: Nucleolar localization is appropriate for an early SSU processome and pre-rRNA processing factor.
Supporting Evidence:
PMID:10923024
Yor145-GFP concentrating in the nucleolus
GO:0051082 unfolded protein binding
IDA
PMID:12502737
Nob1p is required for biogenesis of the 26S proteasome and d...
MARK AS OVER ANNOTATED
Summary: The unfolded-protein binding annotation is not well aligned with Pno1's demonstrated KH-domain pre-rRNA binding and ribosome biogenesis functions.
Reason: Pno1 should not be curated as a generic protein-folding chaperone. Its supported molecular function is rRNA/pre-rRNA binding and assembly-factor regulation with Nob1/Rio1.

Core Functions

Pno1/Dim2 is a KH-domain rRNA-binding assembly factor that binds pre-rRNA, supports SSU processome and pre-40S maturation, contributes to pre-40S export, and coordinates late 18S rRNA processing with Nob1/Rio1-associated quality control.

Supporting Evidence:
  • PMID:18755838
    DIM2 binds pre-rRNAs directly through its KH domain
  • PMID:12736301
    required for pre-18S rRNA processing
  • file:yeast/PNO1/PNO1-deep-research-falcon.md
    binds pre-rRNA (ITS1 region) via its KH domain

References

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Suggested Questions for Experts

Q: Should the legacy PNO1 proteasome assembly annotations be retired or replaced by updated pre-40S/Nob1 maturation annotations in upstream SGD/GO curation?

Suggested Experiments

Experiment: Revisit proteasome assembly phenotypes in pno1/dim2 mutants using acute degron depletion and ribosome-processing rescue constructs to distinguish direct proteasome effects from secondary consequences of impaired ribosome biogenesis.

Hypothesis: The reported proteasome maturation defects are indirect consequences of perturbed Nob1/Pno1 ribosome biogenesis or pleiotropic essential-gene stress.

Type: conditional depletion/rescue

Deep Research

Falcon

(PNO1-deep-research-falcon.md)

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