Evidence map›Paper›PMID 9017604›Full record

ArticleMolecular biology of the cell1997

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1.

K Kominami, N Okura, M Kawamura, G N DeMartino, C A Slaughter, N Shimbara, C H Chung, M Fujimuro, H Yokosawa, Y Shimizu and 3 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 94 citations in OpenAlex.

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  12. Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2002
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 1 institution in 1 country.

K KominamiDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Japan.
N Okura
M Kawamura
G N DeMartino
C A Slaughter
N Shimbara
C H Chung
M Fujimuro
H Yokosawa
Y Shimizu
N Tanahashi
K Tanaka
A Toh-e
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nin1p, a component of the 26S proteasome of Saccharomyces cerevisiae, is required for activation of Cdc28p kinase at the G1-S-phase and G2-M boundaries. By exploiting the temperature-sensitive phenotype of the nin1-1 mutant, we have screened for genes encoding proteins with related functions to Nin1p and have cloned and characterized two new multicopy suppressors, SUN1 and SUN2, of the nin1-1 mutation. SUN1 can suppress a null nin1 mutation, whereas SUN2, an essential gene, does not. Sun1p is a 268-amino acid protein which shows strong similarity to MBP1 of Arabidopsis thaliana, a homologue of the S5a subunit of the human 26S proteasome. Sun1p binds ubiquitin-lysozyme conjugates as do S5a and MBP1. Sun2p (523 amino acids) was found to be homologous to the p58 subunit of the human 26S proteasome. cDNA encoding the p58 component was cloned. Furthermore, expression of a derivative of p58 from which the N-terminal 150 amino acids had been removed restored the function of a null allele of SUN2. During glycerol density gradient centrifugation, both Sun1p and Sun2p comigrated with the known proteasome components. These results, as well as other structural and functional studies, indicate that both Sun1p and Sun2p are components of the regulatory module of the yeast 26S proteasome.

Indexed as

Carrier ProteinsCell Cycle ProteinsGenes, SuppressorProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceBinding SitesCentrifugationFungal ProteinsGlycerolHumansMolecular Sequence DataMuramidaseMutationOpen Reading FramesATP dependent 26S proteaseCarrier ProteinsCell Cycle ProteinsFungal ProteinsGlycerolMBP1 protein, S cerevisiaeMuramidasePeptide HydrolasesProteasome Endopeptidase ComplexPSMD4 protein, humanRecombinant Fusion ProteinsRepressor ProteinsRNA-Binding ProteinsRPN10 protein, S cerevisiaeRPN12 protein, S cerevisiaeRPN3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinsNon-programmatic

Identifiers

PMID9017604
PMCPMC276068
OpenAlexW2083399536

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.