Peptide transport and chemotaxis in <i>Escherichia coli</i> and <i>Salmonella typhimurium</i>: characterization of the dipeptide permease (Dpp) and the dipeptide‐binding protein

Abouhamad, Walid N.; Manson, Michael D.; Gibson, M. M.; Higgins, Christopher F.

doi:10.1111/j.1365-2958.1991.tb01876.x

Cited by 147 publications

(129 citation statements)

References 61 publications

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“…In strains unable to transport dipeptides, but containing wild-type levels of the dipeptide binding protein (DppA), the chemotaxic response towards peptides is comparable to that in the wild type. This is consistent with the notion that only the dipeptide binding protein of Dpp is involved in chemotaxis [1]. Later research showed that at least five different receptors (methyl-accepting chemotaxis proteins (MCPs)) are present in the cytoplasmic membrane of enteric bacteria to recognize attractants.…”

Section: Chemotaxissupporting

confidence: 81%

Peptides and ATP binding cassette peptide transporters

Detmers

Lanfermeijer

Poolman

2001

Research in Microbiology

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-In this review our knowledge of ATP binding cassette (ABC) transporters specific for peptides is discussed. Besides serving a role in nutrition of the cell, the systems participate in various signaling processes that allow (micro)organisms to monitor the local environment. In bacteria, these include regulation of gene expression, competence development, sporulation, DNA transfer by conjugation, chemotaxis, and virulence development, and the role of ABC transporters in each of these processes is discussed. Particular attention is paid to the specificity determinants of peptide receptors and transporters in relation to their structure and to the mechanisms of peptide binding.

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Section: Chemotaxissupporting

confidence: 81%

Peptides and ATP binding cassette peptide transporters

Detmers

Lanfermeijer

Poolman

2001

Research in Microbiology

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“…The dpp operon has been shown to be maximally expressed in the stationary phase of growth, with expression driven from the promoter region upstream of the first gene, dppA (Abouhamad & Manson, 1994). In Salmonella typhimurium and Escherichia coli, dppA has been shown to play a role in chemotaxis (Abouhamad et al, 1991). The role of the dpp transport machinery in utilizing haem iron has also been shown in E. coli.…”

Section: Introductionmentioning

confidence: 96%

Genetic analysis of genes involved in dipeptide metabolism and cytotoxicity in Pseudomonas aeruginosa PAO1

et al. 2008

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The dipeptide transport operon in bacteria comprises genes for the transport and metabolism of amino acids and dipeptides, as well as haem and haem precursors such as aminolaevulinic acid. Such nutrient and mineral sources are vital for bacteria to survive in and colonize a range of niches. In silico analysis of the dipeptide transport systems in sequenced Pseudomonas species identified the presence of two genes in P. aeruginosa strains that were absent in other sequenced pseudomonads. These genes encode a putative metallopeptidase, PA4498, and a putative transcriptional regulator, PA4499. Proteomic profiling of wild-type PAO1 and a PA4499 mutant strain indicated that PA4499 negatively regulated the putative peptidase, PA4498. Transcriptional fusion analysis verified that expression of PA4498 (mdpA, metallo-dipeptidase aeruginosa) was negatively regulated by the downstream putative transcriptional regulator PA4499 (psdR, Pseudomonas dipeptide regulator). Transcriptional fusion analysis also showed that the dppABCDF operon was under the negative control of psdR. Functional genomic analysis of mdpA indicated that it is required for the metabolism of a range of dipeptides and that it contributes to the cytotoxicity of PAO1 on an epithelial cell line.

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“…DBP is a 507-residue periplasmic protein involved in chemotaxis toward, and transport of, many dipeptides and some tripeptides (Manson et al, 1986;Abouhamad et al, 1991;Olson et al, 1991). This protein has also been shown to be related to periplasmic receptors for oligopeptides (Guyer et al, 1985;Tame et al, 1994) and nickel (Navarro et al, 1993).…”

mentioning

confidence: 99%

Modeling of the structure of the Haemophilus influenzae heme‐binding protein suggests a mode of heme interaction

Dunten¹,

Mowbray²

1995

Protein Science

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The structure and function of the periplasmic heme-binding protein HbpA ofHaemophilus influenzae were investigated. This protein is involved in the import of heme into the bacteria through the inner membrane, and thus is a key element of the organism's ability to survive in blood. A high degree of sequence similarity between HbpA and the dipeptide-binding protein of Escherichia coli is suggested to be the result of a functional relationship. An HbpA model built using the dipeptide-binding protein suggests a mode of heme binding that is distinct from those known in proteins of the human host. These results provide a starting point for rational drug design.Keywords: heme; modeling; periplasmic binding protein; protein structure; transport Haemophilus influenzae is an important cause of meningitis, as well as a major agent of lower respiratory tract and other diseases. The organism has an absolute requirement for exogenously supplied heme, the import of which utilizes a periplasmic lipoprotein, HbpA (Hanson & Hansen, 1991). This heme(haemin)-binding protein is the primary receptor for a heme transport system in the cytoplasmic membrane and, as a key element of the organism's ability to survive in blood, is a desirable target for drugs that would inhibit heme transport. As part of a transport system, it could also be used as a means of selective delivery of toxic compounds into the bacterial cell. The sequence is strongly conserved among various Haemophilus strains (Hanson et al., 1992). A similar protein has also been found in Yersinia enterocolitica (Stojiljkovic & Hantke, 1994) and proposed to exist in Neisseria meningitidis (Stojiljkovic et al., 1995), other hemerequiring pathogens. These facts suggest that drugs aimed at HbpA might be generally useful for a variety of disease-causing bacteria. The success of such a strategy depends largely on the ability to design drugs that do not interfere with the normal roles of heme in the host, and thus also on a knowledge of the modes of heme binding in the protein structures involved. The X-ray Reprint requests to: Sherry L. Mowbray, Department of Molecular Biology, BioMedical Center, Box 590, Swedish University of Agricultural Sciences, 75124 Uppsala, Sweden; e-mail: mowbray@xray.bmc.uu.se.Abbreviations: HbpA, the heme-binding protein of Haemophilus influenzae; DBP, the dipeptide-binding protein of Escherichia coli.

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Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide‐binding protein

Cited by 147 publications

References 61 publications

Peptides and ATP binding cassette peptide transporters

Peptides and ATP binding cassette peptide transporters

Genetic analysis of genes involved in dipeptide metabolism and cytotoxicity in Pseudomonas aeruginosa PAO1

Modeling of the structure of the Haemophilus influenzae heme‐binding protein suggests a mode of heme interaction

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