Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis

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Published inJournal of Bacteriology Vol. 175; no. 23; pp. 7523 - 7532
Main Authors TYNKKYNEN, S, BUIST, G, KUNJI, E, KOK, J, POOLMAN, B, VENEMA, G, HAANDRIKMAN, A
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.12.1993
Subjects
Amino Acid Sequence
Amino Acids - metabolism
Animals
Bacterial Proteins - genetics
Bacteriology
Base Sequence
Biological and medical sciences
Biological Transport
Biotechnology
Carrier Proteins - genetics
Deoxyribonucleic acid
DNA
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Genetics
Glycolysis
Lactococcus lactis
Lactococcus lactis - genetics
Lactococcus lactis - growth & development
Lactococcus lactis - metabolism
Lipoproteins - genetics
Metalloendopeptidases - genetics
Microbiology
Milk - metabolism
Molecular Sequence Data
Mutagenesis, Insertional
Oligopeptides - metabolism
Plasmids - genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Streptococcaceae
Gene
Lactococcus lactis subsp. lactis
Oligopeptides
Transportation system
Membrane transport
Bacteria
Micrococcales
Uptake
Structural analysis
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Abstract Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
AbstractList Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
The nucleotide sequence of a chromosomal DNA fragment of Lactococcus lactis subspecies lactis SSL135, previously implicated in peptide utilization, has been determined. The sequence is presented.
The nucleotide sequence of a chromosomal DNA fragment of Lactococcus lactis subsp. lactis SSL135, previously implicated in peptide utilization, has been determined. The genes oppDFBCA, encoding the oligopeptide transport system (Opp), and that encoding the endopeptidase PepO were located on this 8.9-kb DNA fragment. The oppDFBCA and pepO genes are probably organized in an operon. Analysis of the deduced amino acid sequences of the genes indicated that the oligopeptide transport system consists of two ATP-binding proteins OppD and OppF, two integral membrane proteins OppB and OppC, and a substrate-binding protein OppA. On the basis of the homology of OppF and OppD of L. lactis with other ABC (ATP-binding cassette) transporter proteins, the L. lactis Opp system can be classified as a member of this group. Two integration mutants, one defective in OppA and the other defective in PepO, were constructed. Growth of these mutants in a chemically defined medium with oligopeptides showed that the transport system, but not the endopeptidase, is essential for the utilization of peptides longer than three residues. Uptake of the pentapeptide Leu-enkephalin in glycolyzing lactococcal cells was followed by rapid hydrolysis of the peptide intracellularly. Importantly, extracellular hydrolysis of Leu-enkephalin is not observed. The OppA-deficient mutant was unable to transport Leu-enkephalin. Growth experiments with pasteurized milk revealed that transport of oligopeptides forms an essential part of the proteolytic system in lactococci.
Author G Buist
J Kok
A Haandrikman
B Poolman
E Kunji
G Venema
S Tynkkynen
AuthorAffiliation Research and Development Centre, Valio Ltd., Helsinki, Finland
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  organization: Valio Ltd, res. development cent., 00101 Helsinki, Finland
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Issue 23
Keywords Streptococcaceae
Gene
Lactococcus lactis subsp. lactis
Oligopeptides
Transportation system
Membrane transport
Bacteria
Micrococcales
Uptake
Structural analysis
Language English
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– name: United States
– name: Washington
PublicationTitle Journal of Bacteriology
PublicationTitleAlternate J Bacteriol
PublicationYear 1993
Publisher American Society for Microbiology
Publisher_xml – name: American Society for Microbiology
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The nucleotide sequence of a chromosomal DNA fragment of Lactococcus lactis subsp. lactis SSL135, previously implicated in peptide utilization, has been...
The nucleotide sequence of a chromosomal DNA fragment of Lactococcus lactis subspecies lactis SSL135, previously implicated in peptide utilization, has been...
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SubjectTerms Amino Acid Sequence
Amino Acids - metabolism
Animals
Bacterial Proteins - genetics
Bacteriology
Base Sequence
Biological and medical sciences
Biological Transport
Biotechnology
Carrier Proteins - genetics
Deoxyribonucleic acid
DNA
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Genetics
Glycolysis
Lactococcus lactis
Lactococcus lactis - genetics
Lactococcus lactis - growth & development
Lactococcus lactis - metabolism
Lipoproteins - genetics
Metalloendopeptidases - genetics
Microbiology
Milk - metabolism
Molecular Sequence Data
Mutagenesis, Insertional
Oligopeptides - metabolism
Plasmids - genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Title Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis
URI http://jb.asm.org/content/175/23/7523.abstract
https://www.ncbi.nlm.nih.gov/pubmed/8244921
https://www.proquest.com/docview/227066528
https://search.proquest.com/docview/16729044
https://pubmed.ncbi.nlm.nih.gov/PMC206908
Volume 175
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