Evidence map›Paper›PMID 1898763›Full record

ArticleMolecular and cellular biology1991

Molecular cloning and functional analysis of three subunits of yeast proteasome.

Y Emori, T Tsukahara, H Kawasaki, S Ishiura, H Sugita, K Suzuki

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
13.0field-weighted citation impact, top 1% 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

27 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Yeast PI31 inhibits the proteasome by a direct multisite mechanism.Nature structural & molecular biology · 2022
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  13. Subunit arrangement in the human 20S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  14. Article
  15. Roles of proteasomes in cell growth.Molecular biology reports · 1995
    Review
  16. Review
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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

6 authors at 1 institution in 1 country.

Y EmoriDepartment of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Japan.
T Tsukahara
H Kawasaki
S Ishiura
H Sugita
K Suzuki
Tokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The genes encoding three subunits of Saccharomyces cerevisiae proteasome were cloned and sequenced. The deduced amino acid sequences were homologous not only to each other (30 to 40% identity) but also to those of rat and Drosophila proteasomes (25 to 65% identity). However, none of these sequences showed any similarity to any other known sequences, including various proteases, suggesting that these proteasome subunits may constitute a unique gene family. Gene disruption analyses revealed that two of the three subunits (subunits Y7 and Y8) are essential for growth, indicating that the proteasome and its individual subunits play an indispensable role in fundamental biological processes. On the other hand, subunit Y13 is not essential; haploid cells with a disrupted Y13 gene can proliferate, although the doubling time is longer than that of cells with nondisrupted genes. In addition, biochemical analysis revealed that proteasome prepared from the Y13 disrupted cells contains tryptic and chymotryptic activities equivalent to those of nondisrupted cells, indicating that the Y13 subunit is not essential for tryptic or chymotryptic activity. However, the chymotryptic activity of the Y13 disrupted cells is not dependent on sodium dodecyl sulfate (SDS), an activator of proteasome, since nearly full activity was observed in the absence of SDS. Thus, the activity in proteasome of the Y13 disrupted cells might result in unregulated intracellular proteolysis, thus leading to the prolonged cell cycle. These results indicate that cloned proteasome subunits having similar sequences to the yeast Y13 subunit are structural, but not catalytic, components of proteasome. It is also suggested that two subunits (Y7 and Y8) might occupy positions essential to proteasome structure or activity, whereas subunit Y13 is in a nonessential but important position.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBlotting, NorthernCloning, MolecularCysteine EndopeptidasesDrosophila melanogasterGenes, FungalMolecular Sequence DataMultienzyme ComplexesOligonucleotidesPeptide FragmentsProteasome Endopeptidase ComplexRatsRestriction MappingRibonuclease PCysteine EndopeptidasesMultienzyme ComplexesOligonucleotidesPeptide FragmentsProteasome Endopeptidase ComplexRibonuclease PRNA, FungalRNA, MessengerRPM2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID1898763
PMCPMC359626
OpenAlexW2270560834

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.