ArticleJournal of bacteriology2005
Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 53 citations in OpenAlex.
- The GlyGly-CTERM domain functions as an independent motif that targets proteins to rhombosortase inJournal of bacteriology · 2026Article
- The GlyGly-CTERM domain functions as an independent motif that targets proteins to rhombosortase inbioRxiv : the preprint server for biology · 2026Article
- Article
- The Type II Secretion System Utilizes AsmA-like Protein GspN to Facilitate Transport of Lipoproteins to the Cell Surface inbioRxiv : the preprint server for biology · 2025Article
- The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system inJournal of bacteriology · 2025Article
- Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024Article
- SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens.International journal of molecular sciences · 2022Review
- Genome Analysis ofAntimicrobial agents and chemotherapy · 2022Article
- A clostripain-like protease plays a major role in generating the secretome of enterotoxigenic Bacteroides fragilis.Molecular microbiology · 2021Article
- Tracking Proteins Secreted by Bacteria: What's in the Toolbox?Frontiers in cellular and infection microbiology · 2017Review
- Surface-Exposed Lipoproteins: An Emerging Secretion Phenomenon in Gram-Negative Bacteria.Trends in microbiology · 2016Review
- The Role of Bacterial Secretion Systems in the Virulence of Gram-Negative Airway Pathogens Associated with Cystic Fibrosis.Frontiers in microbiology · 2016Review
- Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond.Biochimica et biophysica acta · 2014Review
- A dodecameric ring-like structure of the N0 domain of the type II secretin from enterotoxigenic Escherichia coli.Journal of structural biology · 2013Article
- Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.PLoS pathogens · 2013Article
- Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012Review
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The type II secretion system: biogenesis, molecular architecture and mechanism.Nature reviews. Microbiology · 2012Review
- Minor pseudopilin self-assembly primes type II secretion pseudopilus elongation.The EMBO journal · 2012Article
- Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone.The Journal of biological chemistry · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pullulanase (PulA) from the gram-negative bacterium Klebsiella oxytoca is a 116-kDa surface-anchored lipoprotein of the isoamylase family that allows growth on branched maltodextrin polymers. PulA is specifically secreted via a type II secretion system. PelBsp-PulA, a nonacylated variant of PulA made by replacing the lipoprotein signal peptide (sp) with the signal peptide of pectate lyase PelB from Erwinia chrysanthemi, was efficiently secreted into the medium. Two 80-amino-acid regions of PulA, designated A and B, were previously shown to promote secretion of beta-lactamase (BlaM) and endoglucanase CelZ fused to the C terminus. We show that A and B fused to the PelB signal peptide can also promote secretion of BlaM and CelZ but not that of nuclease NucB or several other reporter proteins. However, the deletion of most of region A or all of region B, either individually or together, had only a minor effect on PelBsp-PulA secretion. Four independent linker insertions between amino acids 234 and 324 in PelBsp-PulA abolished secretion. This part of PulA, region C, could contain part of the PulA secretion signal or be important for its correct presentation. Deletion of region C abolished PelBsp-PulA secretion without dramatically affecting its stability. PelBsp-PulA-NucB chimeras were secreted only if the PulA-NucB fusion point was located downstream from region C. The data show that at least three regions of PulA contain information that influences its secretion, depending on their context, and that some reporter proteins might contribute to the secretion of chimeras of which they are a part.
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