Analysis of the presence of prtR proteinase gene in natural isolates of Lactobacillus rhamnosus
Language English Country United States Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
17455789
DOI
10.1007/bf02931617
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins chemistry genetics metabolism MeSH
- Cysteine Endopeptidases chemistry genetics metabolism MeSH
- DNA, Bacterial analysis genetics MeSH
- DNA Primers MeSH
- Catalytic Domain MeSH
- Lacticaseibacillus rhamnosus enzymology genetics isolation & purification MeSH
- Humans MeSH
- Polymerase Chain Reaction MeSH
- Food Microbiology MeSH
- Vagina microbiology MeSH
- Binding Sites genetics MeSH
- Check Tag
- Humans MeSH
- Female MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Cysteine Endopeptidases MeSH
- DNA, Bacterial MeSH
- DNA Primers MeSH
- prtR protein, Porphyromonas gingivalis W50 MeSH Browser
The region of the prtR gene coding for the active site of PrtR proteinase was detected in natural isolates of lactobacilli, previously determined as Lactobacillus rhamnosus. This region was present in all L. rhamnosus strains with proteolytic activity. The PCR primers used were constructed on the basis of the sequence of the catalytic domain of the prtR proteinase gene. These primers generated in colony-PCR procedure specific 611 1-bp product with DNA from natural isolates of L. rhamnosus. No PCR amplifications using these primers were obtained for closely related bacteria of genus Lactobacillus, regardless of their proteolytic activity. In addition, these primers could be used singly or in multiplex PCR together with the Lactobacillus genus-specific primers. Compared with the other proteinases within the genus Lactobacillus (PrtP, PrtB and PrtH) which retained the activity in cell-free proteinase extracts, PrtR proteinase showed proteolytic activity only under in vivo conditions (whole cells of the producing strains).
See more in PubMed
Antonie Van Leeuwenhoek. 1999 Jul-Nov;76(1-4):139-55 PubMed
Folia Microbiol (Praha). 2006;51(4):268-72 PubMed
J Appl Microbiol. 2001 Jan;90(1):123-30 PubMed
Arch Microbiol. 2001 Dec;177(1):54-61 PubMed
Biotechnol Genet Eng Rev. 1997;14:279-301 PubMed
Appl Environ Microbiol. 2003 Oct;69(10):5802-11 PubMed
Protein Sci. 1997 Mar;6(3):501-23 PubMed
Appl Environ Microbiol. 1991 Jun;57(6):1753-1757 PubMed
J Appl Microbiol. 1998 Apr;84(4):593-9 PubMed
Folia Microbiol (Praha). 2005;50(3):223-8 PubMed
J Bacteriol. 1996 Jun;178(11):3059-65 PubMed
Folia Microbiol (Praha). 2006;51(4):281-2 PubMed
J Bacteriol. 1999 Aug;181(15):4592-7 PubMed
Antonie Van Leeuwenhoek. 1996 Oct;70(2-4):187-221 PubMed
Folia Microbiol (Praha). 2004;49(2):203-7 PubMed
Folia Microbiol (Praha). 2004;49(2):143-6 PubMed
