Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10

A novel proteinase, PrtR, produced by the human vaginal isolate Lactobacillus rhamnosus strain BGT10 was identified and genetically characterized. The prtR gene and flanking regions were cloned and sequenced. The deduced amino acid sequence of PrtR shares characteristics that are common for other ce...

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Main Authors: Pastar, Irena, Tonic, Ivana, Golic, Natasa, Kojic, Milan, van Kranenburg, Richard, Kleerebezem, Michiel, Topisirovic, Ljubisa, Jovanovic, Goran
Formato: Artigo
Idioma:en
Publicado em: American Society for Microbiology 2003
Assuntos:
Genetics and Molecular Biology
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC201213/
https://ncbi.nlm.nih.gov/pubmed/14532028
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.69.10.5802-5811.2003
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spelling pubmed-2012132003-12-02 Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10 Pastar, Irena Tonic, Ivana Golic, Natasa Kojic, Milan van Kranenburg, Richard Kleerebezem, Michiel Topisirovic, Ljubisa Jovanovic, Goran Appl Environ Microbiol Genetics and Molecular Biology A novel proteinase, PrtR, produced by the human vaginal isolate Lactobacillus rhamnosus strain BGT10 was identified and genetically characterized. The prtR gene and flanking regions were cloned and sequenced. The deduced amino acid sequence of PrtR shares characteristics that are common for other cell envelope proteinases (CEPs) characterized to date, but in contrast to the other cell surface subtilisin-like serine proteinases, it has a smaller and somewhat different B domain and lacks the helix domain, and the anchor domain has a rare sorting signal sequence. Furthermore, PrtR lacks the insert domain, which otherwise is situated inside the catalytic serine protease domain of all CEPs, and has a different cell wall spacer (W) domain similar to that of the cell surface antigen I and II polypeptides expressed by oral and vaginal streptococci. Moreover, the PrtR W domain exhibits significant sequence homology to the consensus sequence that has been shown to be the hallmark of human intestinal mucin protein. According to its α(S1)- and β-casein cleavage efficacy, PrtR is an efficient proteinase at pH 6.5 and is distributed throughout all L. rhamnosus strains tested. Proteinase extracts of the BGT10 strain obtained with Ca(2+)-free buffer at pH 6.5 were proteolytically active. The prtR promoter-like sequence was determined, and the minimal promoter region was defined by use of prtR-gusA operon fusions. The prtR expression is Casitone dependent, emphasizing that nitrogen depletion elevates its transcription. This is in correlation with the catalytic activity of the PrtR proteinase. American Society for Microbiology 2003-10 /pmc/articles/PMC201213/ /pubmed/14532028 http://dx.doi.org/10.1128/AEM.69.10.5802-5811.2003 Text en Copyright © 2003, American Society for Microbiology
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Genetics and Molecular Biology
spellingShingle Genetics and Molecular Biology
Pastar, Irena
Tonic, Ivana
Golic, Natasa
Kojic, Milan
van Kranenburg, Richard
Kleerebezem, Michiel
Topisirovic, Ljubisa
Jovanovic, Goran
Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10
description A novel proteinase, PrtR, produced by the human vaginal isolate Lactobacillus rhamnosus strain BGT10 was identified and genetically characterized. The prtR gene and flanking regions were cloned and sequenced. The deduced amino acid sequence of PrtR shares characteristics that are common for other cell envelope proteinases (CEPs) characterized to date, but in contrast to the other cell surface subtilisin-like serine proteinases, it has a smaller and somewhat different B domain and lacks the helix domain, and the anchor domain has a rare sorting signal sequence. Furthermore, PrtR lacks the insert domain, which otherwise is situated inside the catalytic serine protease domain of all CEPs, and has a different cell wall spacer (W) domain similar to that of the cell surface antigen I and II polypeptides expressed by oral and vaginal streptococci. Moreover, the PrtR W domain exhibits significant sequence homology to the consensus sequence that has been shown to be the hallmark of human intestinal mucin protein. According to its α(S1)- and β-casein cleavage efficacy, PrtR is an efficient proteinase at pH 6.5 and is distributed throughout all L. rhamnosus strains tested. Proteinase extracts of the BGT10 strain obtained with Ca(2+)-free buffer at pH 6.5 were proteolytically active. The prtR promoter-like sequence was determined, and the minimal promoter region was defined by use of prtR-gusA operon fusions. The prtR expression is Casitone dependent, emphasizing that nitrogen depletion elevates its transcription. This is in correlation with the catalytic activity of the PrtR proteinase.
author Pastar, Irena
Tonic, Ivana
Golic, Natasa
Kojic, Milan
van Kranenburg, Richard
Kleerebezem, Michiel
Topisirovic, Ljubisa
Jovanovic, Goran
author_facet Pastar, Irena
Tonic, Ivana
Golic, Natasa
Kojic, Milan
van Kranenburg, Richard
Kleerebezem, Michiel
Topisirovic, Ljubisa
Jovanovic, Goran
author_sort Pastar, Irena
title Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10
title_short Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10
title_full Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10
title_fullStr Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10
title_full_unstemmed Identification and Genetic Characterization of a Novel Proteinase, PrtR, from the Human Isolate Lactobacillus rhamnosus BGT10
title_sort identification and genetic characterization of a novel proteinase, prtr, from the human isolate lactobacillus rhamnosus bgt10
publisher American Society for Microbiology
publisher_facet American Society for Microbiology
publishDate 2003
url https://ncbi.nlm.nih.gov/pmc/articles/PMC201213/
https://ncbi.nlm.nih.gov/pubmed/14532028
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.69.10.5802-5811.2003
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