Literature DB >> 2695751

Secretion, processing and activation of bacterial extracellular proteases.

C Wandersman1.   

Abstract

Many different bacteria secrete proteases into the culture medium. Extracellular proteases produced by Gram-positive bacteria are secreted by a signal-peptide-dependent pathway and have a propeptide located between the signal peptide and the mature protein. Many extracellular proteases synthesized by Gram-negative bacteria are also produced as precursors with a signal peptide. However, at least two species of Gram-negative bacteria secrete one or more proteases via a novel signal-peptide-independent route. Most proteases secreted by Gram-negative bacteria also have a propeptide whose length and location vary according to the protease. Specific features of protease secretion pathways and the mechanisms of protease activation are discussed with particular reference to some of the best-characterized extracellular proteases produced by Gram-positive and Gram-negative bacteria.

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Year:  1989        PMID: 2695751     DOI: 10.1111/j.1365-2958.1989.tb00169.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  59 in total

1.  The vimE gene downstream of vimA is independently expressed and is involved in modulating proteolytic activity in Porphyromonas gingivalis W83.

Authors:  Elaine Vanterpool; Francis Roy; Hansel M Fletcher
Journal:  Infect Immun       Date:  2004-10       Impact factor: 3.441

2.  A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion.

Authors:  J K Gustin; E Kessler; D E Ohman
Journal:  J Bacteriol       Date:  1996-11       Impact factor: 3.490

Review 3.  Determinants of extracellular protein secretion in gram-negative bacteria.

Authors:  S Lory
Journal:  J Bacteriol       Date:  1992-06       Impact factor: 3.490

4.  Inactivation of vimF, a putative glycosyltransferase gene downstream of vimE, alters glycosylation and activation of the gingipains in Porphyromonas gingivalis W83.

Authors:  Elaine Vanterpool; Francis Roy; Hansel M Fletcher
Journal:  Infect Immun       Date:  2005-07       Impact factor: 3.441

5.  Pseudomonas aeruginosa alkaline protease: evidence for secretion genes and study of secretion mechanism.

Authors:  J Guzzo; J M Pages; F Duong; A Lazdunski; M Murgier
Journal:  J Bacteriol       Date:  1991-09       Impact factor: 3.490

6.  Modulation of the Bacillus anthracis secretome by the immune inhibitor A1 protease.

Authors:  Kathryn J Pflughoeft; Michelle C Swick; David A Engler; Hye-Jeong Yeo; Theresa M Koehler
Journal:  J Bacteriol       Date:  2013-11-08       Impact factor: 3.490

7.  Characterization, genetic analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50.

Authors:  J Aduse-Opoku; J Muir; J M Slaney; M Rangarajan; M A Curtis
Journal:  Infect Immun       Date:  1995-12       Impact factor: 3.441

8.  Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases.

Authors:  Florian Veillard; Maryta Sztukowska; Danuta Mizgalska; Mirosław Ksiazek; John Houston; Barbara Potempa; Jan J Enghild; Ida B Thogersen; F Xavier Gomis-Rüth; Ky-Anh Nguyen; Jan Potempa
Journal:  Biochim Biophys Acta       Date:  2013-04-10

9.  In silico characterization of the global Geobacillus and Parageobacillus secretome.

Authors:  Pedro H Lebre; Habibu Aliyu; Pieter De Maayer; Don A Cowan
Journal:  Microb Cell Fact       Date:  2018-10-03       Impact factor: 5.328

10.  Biochemical properties of a novel metalloprotease from Staphylococcus hyicus subsp. hyicus involved in extracellular lipase processing.

Authors:  S Ayora; P E Lindgren; F Götz
Journal:  J Bacteriol       Date:  1994-06       Impact factor: 3.490

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