The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa

No abstract is available for this paper.

• Publication year

  1995

• Venue

  Molecular Microbiology

• Publication date

  1995-12-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1111/j.1365-2958.1995.18050877.xPMID 8825092
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor.

  1994cited by this paper
• The prosequence of Rhizopus niveus aspartic proteinase-I supports correct folding and secretion of its mature part in Saccharomyces cerevisiae.

  1994cited by this paper
• Requirement of the propeptide for in vivo formation of active yeast carboxypeptidase Y.

  1994cited by this paper
• The complete general secretory pathway in gram-negative bacteria.

  1993cited by this paper
• The propeptide is required for in vivo formation of stable active yeast proteinase A and can function even when not covalently linked to the mature region.

  1993cited by this paper
• Pseudomonas aeruginosa lasB1 mutants produce an elastase, substituted at active-site His-223, that is defective in activity, processing, and secretion

  1993cited by this paper
• Intramolecular chaperones and protein folding.

  1993cited by this paper
• Bacterial extracellular zinc-containing metalloproteases.

  1993cited by this paper
• Secreted LasA of Pseudomonas aeruginosa is a staphylolytic protease.

  1993cited by this paper
• Protease pro region required for folding is a potent inhibitor of the mature enzyme

  1992cited by this paper
• Efficient production and processing of elastase and LasA by Pseudomonas aeruginosa require zinc and calcium ions

  1992cited by this paper
• Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase

  1992cited by this paper
• Chaperones and protein folding.

  1992cited by this paper
• Identification of cleavage sites involved in proteolytic processing of Pseudomonas aeruginosa preproelastase

  1992cited by this paper
• Intracellular transit of a yeast protease is rescued by trans-complementation with its prodomain.

  1992cited by this paper
• Correct folding of alpha-lytic protease is required for its extracellular secretion from Escherichia coli

  1992cited by this paper
• The role of the pro‐sequence in the processing and secretion of the thermolysin‐like neutral protease from Bacillus cereus

  1992cited by this paper
• Pro‐peptide as an intermolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro‐peptide

  1991cited by this paper
• Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity.

  1991cited by this paper
• Intramolecular chaperone: the role of the pro-peptide in protein folding.

  1991cited by this paper
• Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide [corrected].

  1991cited by this paper
• Pseudomonas aeruginosa LasA: a second elastase under the transcriptional control of lasR

  1991cited by this paper
• Pseudomonas aeruginosa LasB mutant constructed by insertional mutagenesis reveais elastolytic activity due to alkaline proteinase and the LasA fragment

  1991cited by this paper
• Escherichia-Pseudomonas shuttle vectors derived from pUC18/19.

  1991cited by this paper
• Role of the proregion in the production and secretion of the Yarrowia lipolytica alkaline extracellular protease.

  1991cited by this paper
• Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase

  1991cited by this paper
• The αlytic protease pro-region does not require a physical linkage to activate the protease domain in vivo

  1989cited by this paper
• Molecular cloning : a laboratory manual. Cold Spring Harbor, NY

  1989cited by this paper
• Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity

  1989cited by this paper
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  1989cited by this paper
• Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process

  1989cited by this paper
• Nucleotide sequence and expression in Escherichia coli of the Pseudomonas aeruginosa lasA gene

  1988cited by this paper
• Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting information

  1988cited by this paper
• Use of a gene replacement cosmid vector for cloning alginate conversion genes from mucoid and nonmucoid Pseudomonas aeruginosa strains: algS controls expression of algT

  1988cited by this paper
• Synthesis, processing, and transport of Pseudomonas aeruginosa elastase

  1988cited by this paper
• Partial purification and characterization of an inactive precursor of Pseudomonas aeruginosa elastase

  1988cited by this paper
• Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli.

  1987cited by this paper
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  1984cited by this paper
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  1984cited by this paper
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  1984cited by this paper
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  1982cited by this paper
• Isolation and characterization of Pseudomonas aeruginosa PAO mutant that produces altered elastase

  1980cited by this paper
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

  1970cited by this paper

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