A characterisation of the peptide transport system in barley seeds

1995 ◽  
Vol 23 (4) ◽  
pp. 558S-558S ◽  
Author(s):  
WANDA M. WATERWORTH ◽  
CHRIS E. WEST ◽  
DAVID J. HARDY ◽  
CLIFFORD M. BRAY
Keyword(s):  
Transport System ◽  
Peptide Transport

scholarly journals The Adherence-Associated Lipoprotein P100, Encoded by an opp Operon Structure, Functions as the Oligopeptide-Binding Domain OppA of a Putative Oligopeptide Transport System in Mycoplasma hominis

1999 ◽  
Vol 181 (16) ◽  
pp. 4873-4878 ◽  
Author(s):  
Birgit Henrich ◽  
Miriam Hopfe ◽  
Annette Kitzerow ◽  
Ulrich Hadding
Keyword(s):  
Transport System ◽  
Peptide Binding ◽  
Mycoplasma Hominis ◽  
Initiation Site ◽  
Genomic Region ◽  
Binding Domain ◽  
Terminal Region ◽  
Peptide Transport ◽  
Operon Structure ◽  
Active Transport System

ABSTRACT Mycoplasma hominis, a cell-wall-less prokaryote, was shown to be cytoadherent by the participation of a 100-kDa membrane protein (P100). To identify the gene encoding P100, peptides of P100 were partially sequenced to enable the synthesis of P100-specific oligonucleotides suitable as probes for the detection of the P100 gene. With this strategy, we identified a genomic region of about 10.4 kb inM. hominis FBG carrying the P100 gene. Analysis of the complete deduced protein sequence suggests that P100 is expressed as a pre-lipoprotein with a structure in the N-terminal region common to peptide-binding proteins and an ATP- or GTP-binding P-loop structure in the C-terminal region. Downstream of the P100 gene, an additional four open reading frames putatively encoding the four core domains of an active transport system, OppBCDF, were localized. The organization of the P100 gene and oppBCDF in a transcriptionally active operon structure was demonstrated in Northern blot and reverse transcription-PCR analyses, as all gene-specific probes detected a common RNA of 9.5 kb. Primer extension analysis revealed that the transcriptional initiation site was localized 323 nucleotides upstream of the methionine-encoding ATG of the P100 gene. The peptide-binding character of the P100 protein was confirmed by fluorescence spectroscopy and strongly suggests that the cytoadherence-mediating lipoprotein P100 represents OppA, the substrate-binding domain of a peptide transport system in M. hominis.

scholarly journals Utilization of Oligopeptides by Listeria monocytogenes Scott A

1998 ◽  
Vol 64 (3) ◽  
pp. 1059-1065 ◽  
Author(s):  
Annette Verheul ◽  
Frank M. Rombouts ◽  
Tjakko Abee
Keyword(s):  
Listeria Monocytogenes ◽  
Transport System ◽  
Growth Stimulation ◽  
Sole Source ◽  
Fermented Milk ◽  
Defined Medium ◽  
Peptide Transport ◽  
Transport Systems ◽  
Oligopeptide Transport System ◽  
Oligopeptide Transport

ABSTRACT For effective utilization of peptides, Listeria monocytogenes possesses two different peptide transport systems. The first one is the previously described proton motive force (PMF)-driven di- and tripeptide transport system (A. Verheul, A. Hagting, M.-R. Amezaga, I. R. Booth, F. M. Rombouts, and T. Abee, Appl. Environ. Microbiol. 61:226–233, 1995). The present results reveal that L. monocytogenes possesses an oligopeptide transport system, presumably requiring ATP rather than the PMF as the driving force for translocation. Experiments to determine growth in a defined medium containing peptides of various lengths suggested that the oligopeptide permease transports peptides of up to 8 amino acid residues. Peptidase activities towards several oligopeptides were demonstrated in cell extract from L. monocytogenes, which indicates that upon internalization, the oligopeptides are hydrolyzed to serve as sources of amino acids for growth. The peptide transporters of the nonproteolytic L. monocytogenes might play an important role in foods that harbor indigenous proteinases and/or proteolytic microorganisms, since Pseudomonas fragi as well as Bacillus cereus was found to enhance the growth ofL. monocytogenes to a large extent in a medium in which the milk protein casein was the sole source of nitrogen. In addition, growth stimulation was elicited in this medium when casein was hydrolyzed by using purified protease from Bacillus licheniformis. The possible contribution of the oligopeptide transport system in the establishment of high numbers of L. monocytogenes cells in fermented milk products is discussed.

Stereospecific transport of Tyr-MIF-1 across the blood-brain barrier by peptide transport system-1

1990 ◽  
Vol 25 (4) ◽  
pp. 589-592 ◽  
Author(s):  
William A. Banks ◽  
Abba J. Kastin ◽  
Edward A. Michals ◽  
Carlos M. Barrera
Keyword(s):  
Blood Brain Barrier ◽  
Transport System ◽  
Brain Barrier ◽  
Peptide Transport ◽  
Blood Brain ◽  
System 1

scholarly journals Mechanism of Action of Nikkomycin and the Peptide Transport System of Candida albicans

Microbiology ◽  
1985 ◽  
Vol 131 (4) ◽  
pp. 775-780 ◽  
Author(s):  
P. J. McCARTHY ◽  
P. F. TROKE ◽  
K. GULL
Keyword(s):  
Candida Albicans ◽  
Transport System ◽  
Mechanism Of Action ◽  
Peptide Transport

Peptide transport system-1 (PTS-1) for Tyr-MIF-1 and Met-enkephalin differs from the receptors for either

1999 ◽  
Vol 839 (2) ◽  
pp. 336-340 ◽  
Author(s):  
Grace A Maresh ◽  
Abba J Kastin ◽  
Terry T Brown ◽  
James E Zadina ◽  
William A Banks
Keyword(s):  
Transport System ◽  
Peptide Transport ◽  
System 1

scholarly journals The peptide transport system Opt is involved in both nutrition and environmental sensing during growth of Lactococcus lactis in milk

Microbiology ◽  
2011 ◽  
Vol 157 (6) ◽  
pp. 1612-1619 ◽  
Author(s):  
Mauld Lamarque ◽  
Dominique Aubel ◽  
Jean-Christophe Piard ◽  
Christophe Gilbert ◽  
Vincent Juillard ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Transport System ◽  
Binding Proteins ◽  
Peptide Binding ◽  
Peptide Transport ◽  
Dual Function ◽  
Peptide Transporters ◽  
Transport Mutants ◽  
Dependent Transport ◽  
Distinct Peptide

Lactococcus lactis is known to take up extracellular peptides via at least three distinct peptide transporters. The well-described oligopeptide transporter Opp alone is able to ensure the growth of L. lactis in milk, while the di- and tripeptide transporter DtpT is involved in a peptide-dependent signalling mechanism. The oligopeptide Opt transporter displays two peptide-binding proteins, OptA and OptS. We previously demonstrated that OptA-dependent transport is dedicated to nutritional peptides, as an optABCDF mutant (of a strain devoid of Opp) has an impaired capacity to grow in milk. Using isogenic peptide transport mutants, this study shows that biosynthesis of the Opt transporter is much less sensitive to downregulation that is dependent on extracellular peptides taken up by DtpT than is Opp biosynthesis; this peptide-dependent regulation relies on the transcriptional repressor CodY. We demonstrate the dual function of the Opt system; while OptA contributes to the bacterial nutrition during growth in milk, OptS is involved in the transport of signalling peptides derived from milk and controlling opp expression. So, these results shed new light on the peptide-dependent regulation relying on two peptide transporters with different specificities: DtpT and Opt (via OptS).

Peptide Transport System-1

1995 ◽  
pp. 111-117 ◽  
Author(s):  
William A. Banks ◽  
Abba J. Kastin
Keyword(s):  
Transport System ◽  
Peptide Transport ◽  
System 1
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