Evidence map›Paper›PMID 18625069›Full record

ArticleBMC microbiology2008

Processing of predicted substrates of fungal Kex2 proteinases from Candida albicans, C. glabrata, Saccharomyces cerevisiae and Pichia pastoris.

Oliver Bader, Yannick Krauke, Bernhard Hube

Abstract read
In one paragraph

Article in BMC microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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

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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

51 citing papers in PubMed.

  1. Article
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    Article
  6. Genetic and environmental control of parasexual reproduction in the pathogenicMicrobiology and molecular biology reviews : MMBR · 2025
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  14. Article
  15. The secretorymLife · 2023
    Article
  16. Article
  17. Article
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  19. Article
  20. Article
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

3 authors.

Oliver BaderFG16, Robert Koch-Institut, Nordufer 20, D-13353 Berlin, Germany. obader@gwdg.de
Yannick Krauke
Bernhard Hube

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundKexin-like proteinases are a subfamily of the subtilisin-like serine proteinases with multiple regulatory functions in eukaryotes. In the yeast Saccharomyces cerevisiae the Kex2 protein is biochemically well investigated, however, with the exception of a few well known proteins such as the alpha-pheromone precursors, killer toxin precursors and aspartic proteinase propeptides, very few substrates are known. Fungal kex2 deletion mutants display pleiotropic phenotypes that are thought to result from the failure to proteolytically activate such substrates.

resultsIn this study we have aimed at providing an improved assembly of Kex2 target proteins to explain the phenotypes observed in fungal kex2 deletion mutants by in vitro digestion of recombinant substrates from Candida albicans and C. glabrata. We identified CaEce1, CA0365, one member of the Pry protein family and CaOps4-homolog proteins as novel Kex2 substrates.

conclusionStatistical analysis of the cleavage sites revealed extended subsite recognition of negatively charged residues in the P1', P2' and P4' positions, which is also reflected in construction of the respective binding pockets in the ScKex2 enzyme. Additionally, we provide evidence for the existence of structural constrains in potential substrates prohibiting proteolysis. Furthermore, by using purified Kex2 proteinases from S. cerevisiae, P. pastoris, C. albicans and C. glabrata, we show that while the substrate specificity is generally conserved between organisms, the proteinases are still distinct from each other and are likely to have additional unique substrate recognition.

Indexed as

Amino Acid SequenceCandida albicansCandida glabrataGene Expression Regulation, FungalModels, MolecularMolecular Sequence DataPhenotypePichiaProprotein ConvertasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Analysis, ProteinSubstrate SpecificityKEX2 protein, S cerevisiaeProprotein ConvertasesSaccharomyces cerevisiae Proteins

Identifiers

PMID18625069
PMCPMC2515848

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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.