Two ABC transport systems carry out peptide uptake in Enterococcus faecalis : their roles in growth and in uptake of sex pheromones

2021 ◽  
Author(s):  
Takaya Segawa ◽  
Christopher M. Johnson ◽  
Ronnie P‐A. Berntsson ◽  
Gary M. Dunny
Keyword(s):  
Enterococcus Faecalis ◽  
Sex Pheromones ◽  
Transport Systems ◽  
Abc Transport ◽  
Peptide Uptake

scholarly journals Functional Characterization of the Proteolytic System of Lactobacillus sanfranciscensis DSM 20451T during Growth in Sourdough

2005 ◽  
Vol 71 (10) ◽  
pp. 6260-6266 ◽  
Author(s):  
Nicoline Vermeulen ◽  
Melanie Pavlovic ◽  
Matthias A. Ehrmann ◽  
Michael G. Gänzle ◽  
Rudi F. Vogel
Keyword(s):  
Amino Acid ◽  
Proteolytic Activity ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Peptide Transport ◽  
Transport Systems ◽  
Peptide Hydrolysis ◽  
Degenerate Primers ◽  
Lactobacillus Sanfranciscensis ◽  
Peptide Uptake

ABSTRACT Protein hydrolysis and amino acid metabolism contribute to the beneficial effects of sourdough fermentation on bread quality. In this work, genes of Lactobacillus sanfranciscensis strain DSM 20451 involved in peptide uptake and hydrolysis were identified and their expression during growth in sourdough was determined. Screening of the L. sanfranciscensis genome with degenerate primers targeting prt and analysis of proteolytic activity in vitro provided no indication for proteolytic activity. Proteolysis in aseptic doughs and sourdoughs fermented with L. sanfranciscensis was inhibited upon the addition of an aspartic protease inhibitor. These results indicate that proteolysis was not linked to the presence of L. sanfranciscensis DSM 20451 and that this strain does not harbor a proteinase. Genes encoding the peptide transport systems Opp and DtpT and the intracellular peptidases PepT, PepR, PepC, PepN, and PepX were identified. Both peptide uptake systems and the genes pepN, pepX, pepC, and pepT were expressed by L. sanfranciscensis growing exponentially in sourdough, whereas pepX was not transcribed. The regulation of the expression of Opp, DtpT, and PepT during growth of L. sanfranciscensis in sourdough was investigated. Expression of Opp and DtpT was reduced approximately 17-fold when the peptide supply in dough was increased. The expression of PepT was dependent on the peptide supply to a lesser extent. Thus, the accumulation of amino nitrogen by L. sanfranciscensis in dough is attributable to peptide hydrolysis rather than proteolysis and amino acid metabolism by L. sanfranciscensis during growth in sourdough is limited by the peptide availability.

scholarly journals A Molecular Basis for Tungstate Selectivity in Prokaryotic ABC Transport Systems

2011 ◽  
Vol 193 (18) ◽  
pp. 4999-5001 ◽  
Author(s):  
L. E. Bevers ◽  
G. Schwarz ◽  
W. R. Hagen
Keyword(s):  
Molecular Basis ◽  
Transport Systems ◽  
Abc Transport

scholarly journals The LysR-type PcaQ protein regulates expression of a protocatechuate-inducible ABC-type transport system in Sinorhizobium meliloti

Microbiology ◽  
2011 ◽  
Vol 157 (9) ◽  
pp. 2522-2533 ◽  
Author(s):  
Allyson M. MacLean ◽  
Wilfried Haerty ◽  
G. Brian Golding ◽  
Turlough M. Finan
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Gene Cluster ◽  
Transport System ◽  
Sinorhizobium Meliloti ◽  
Transcriptional Start Site ◽  
Transport Systems ◽  
Insertion Mutation ◽  
Abc Transport ◽  
Dna Binding Site

The LysR protein PcaQ regulates the expression of genes encoding products relevant to the degradation of the aromatic acid protocatechuate (3,4-dihydroxybenzoate), and we have previously defined a PcaQ DNA-binding site located upstream of the target pcaDCHGB operon in Sinorhizobium meliloti. In this work, we show that PcaQ also regulates the expression of the S. meliloti smb20568-smb20787-smb20786-smb20785-smb20784 gene cluster, which is predicted to encode an ABC transport system. ABC transport systems have not been shown before to transport protocatechuate, and we have designated this gene cluster pcaMNVWX. The transcriptional start site of pcaM was mapped, and the predicted PcaQ DNA-binding site was located at −73 to −58 relative to this site. Results from electrophoretic mobility shift assays with purified PcaQ and from expression assays indicated that PcaQ activates expression of the transport system in the presence of protocatechuate. To investigate this transport system further, we generated a pcaM deletion mutant (predicted to encode the substrate-binding protein) and introduced a polar insertion mutation into pcaN, a gene that is predicted to encode a permease. These mutants grew poorly on protocatechuate, presumably because they fail to transport protocatechuate. Genome analyses revealed PcaQ-like DNA-binding sites encoded upstream of ABC transport systems in other members of the α-proteobacteria, and thus it appears likely that these systems are involved in the uptake of protocatechuate.

scholarly journals Sex pheromones and plasmid transfer in Enterococcus faecalis

Plasmid ◽  
1989 ◽  
Vol 21 (3) ◽  
pp. 175-184 ◽  
Author(s):  
Don B. Clewell ◽  
Keith E. Weaver
Keyword(s):  
Enterococcus Faecalis ◽  
Sex Pheromones ◽  
Plasmid Transfer

scholarly journals Characterization of a class of nonformylated Enterococcus faecalis-derived neutrophil chemotactic peptides: the sex pheromones.

1990 ◽  
Vol 87 (1) ◽  
pp. 66-70 ◽  
Author(s):  
P. Sannomiya ◽  
R. A. Craig ◽  
D. B. Clewell ◽  
A. Suzuki ◽  
M. Fujino ◽  
...  
Keyword(s):  
Enterococcus Faecalis ◽  
Sex Pheromones ◽  
Chemotactic Peptides

scholarly journals Hierarchy of Iron Uptake Systems: Yfu and Yiu Are Functional in Yersinia pestis

2006 ◽  
Vol 74 (11) ◽  
pp. 6171-6178 ◽  
Author(s):  
Olga Kirillina ◽  
Alexander G. Bobrov ◽  
Jacqueline D. Fetherston ◽  
Robert D. Perry
Keyword(s):  
Yersinia Pestis ◽  
Iron Uptake ◽  
Disease Process ◽  
Transport Systems ◽  
Growth Defect ◽  
Uptake System ◽  
Outer Membrane Receptor ◽  
Abc Transport ◽  
Iron Deficient ◽  
Additional Iron

ABSTRACT In addition to the yersiniabactin (Ybt) siderophore-dependent system, two inorganic iron ABC transport systems of Yersinia pestis, Yfe and Yfu, have been characterized. Here we show that the Yfu system functions in Y. pestis: a Ybt− Yfe− Yfu− mutant exhibited a greater growth defect under iron-deficient conditions than its Ybt− Yfe− parental strain. We also demonstrate that another putative Y. pestis iron uptake system, Yiu, which potentially encodes an outer membrane receptor, YiuR, and an ABC iron transport cassette, YiuABC, is functional. The cloned yiuABC operon restored growth of an enterobactin-deficient mutant Escherichia coli strain, 1017, under iron-chelated conditions. Iron uptake by the Yiu system in Y. pestis was demonstrated only when the Ybt, Yfe, and Yfu systems were mutated. Using a yiuA::lacZ fusion, we show that the yiuABC promoter is repressed by iron through Fur. A mouse model of bubonic plague failed to show a significant role for the Yiu system in the disease process. These results demonstrate that two additional iron transporters are functional in Y. pestis and indicate that there is a hierarchy of iron transporters, with Ybt being most effective and Yiu being the least effective of those systems which have been characterized.

scholarly journals ScoC Regulates Peptide Transport and Sporulation Initiation in Bacillus subtilis

1999 ◽  
Vol 181 (13) ◽  
pp. 4114-4117 ◽  
Author(s):  
Akiko Koide ◽  
Marta Perego ◽  
James A. Hoch
Keyword(s):  
Bacillus Subtilis ◽  
Negative Regulation ◽  
Negative Regulator ◽  
Peptide Transport ◽  
Transport Systems ◽  
Protease Production ◽  
Multicopy Plasmid ◽  
Abc Transport ◽  
Transcription Regulators ◽  
Sporulation Initiation

ABSTRACT Oligopeptides are transported into Bacillus subtilis by two ABC transport systems, App and Opp. Transcription of the operon encoding the Opp system was found to occur during exponential growth, whereas the app operon was induced at the onset of stationary phase. Transcription of both operons was completely curtailed by overproduction of the ScoC regulator from a multicopy plasmid and was enhanced in strains with the scoC locus deleted. ScoC, a member of the MarR family of transcription regulators, is known from previous studies to be a negative regulator of sporulation and of protease production that acts by binding directly to the promoters of the genes it regulates. Since peptide transport is essential for inactivation of the negative regulation of sporulation by Rap phosphatases, the control of ScoC transcription repression activity plays a crucial role in the initiation of sporulation.

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