The
            <i>Escherichia coli tppB</i>
            (
            <i>ydgR</i>
            ) Gene Represents a New Class of OmpR-Regulated Genes

Goh, Ee-Been; Siino, Dominic F.; Igo, Michèle M.

doi:10.1128/jb.186.12.4019-4024.2004

Cited by 31 publications

(31 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…74 Nutrient starvation also induces the expression of YehU/YehT, the only 2 component system known to regulate cst genes, in E. coli as well as in Salmonella. 72,75 TppB is transcriptionally regulated by leucine and anaerobiosis in Salmonella, 76 whereas in E. coli, the tppB homolog ydgR is regulated by EnvZ/OmpR 2 component system, 77 showing its involvement in stress response. The stationary phase specific sigma factor RpoS, which is known to regulate several virulence factors required in mammalian host, induces the expression of OppA2 in B. burgdorferi.…”

Section: Regulatory Network Of Peptide Transporters In Pathogenic Bacmentioning

confidence: 99%

Bacterial peptide transporters: Messengers of nutrition to virulence

2016

View full text Add to dashboard Cite

Bacteria possess numerous peptide transporters for importing peptides as nutrients. However, these peptide transporters are now consistently reported to play a role in the virulence of various bacterial pathogens. Their ability to transport peptides has implications in antibacterial therapy as well. Therefore, it would be instrumental to have complete knowledge about the role of peptide transporters in mediating this cross connection between metabolism and pathogenesis. Studies on various peptide transporters in bacterial pathogens have improved our understanding of this field. In this review, we have given an overview of the functioning of bacterial peptide transporters and their contribution in virulence of major bacterial pathogens.

show abstract

Section: Regulatory Network Of Peptide Transporters In Pathogenic Bacmentioning

confidence: 99%

Bacterial peptide transporters: Messengers of nutrition to virulence

2016

View full text Add to dashboard Cite

show abstract

“…The non-porin-associated functions of OmpR include regulation of the permease encoded by tppB in S. enterica (41) and E. coli (42), the maltose regulator encoded by malT (23), and the murein regulator encoded by bolA (160). A recent microarray study (97) identified 125 OmpR-dependent genes.…”

Section: The Regulatorsmentioning

confidence: 99%

A Complex Transcription Network Controls the Early Stages of Biofilm Development byEscherichia coli

et al. 2006

View full text Add to dashboard Cite

3Historically, researchers have studied bacterial signaling as if it functioned as a set of isolated, linear pathways. More recent studies, however, have demonstrated that many signaling pathways interact and that these interacting pathways should be construed as an intricate network. This network integrates diverse signals, both extracellular and intracellular, to ensure that the the correct amount of the appropriate subset of genes is expressed at the proper time. Complete delineation of this complex signal transduction network and use of the network to predict the full range of cellular behaviors are major goals of systems biology.Despite considerable progress, we remain near the beginning of this process, which thus far has been dominated by the development of enabling technologies and the compilation of gene lists. Although development and compilation will continue to be essential, the next critical step must be to organize the copious data compiled over 5 decades of pregenomics research and the massive amount of postgenomics data generated over the last decade. This minireview, in which we describe a portion of the overall network of Escherichia coli, is an attempt to perform part of this next step. THE NETWORKAs the model organism for this network, we chose the enterobacterium E. coli. We focused specifically on the common laboratory strain K-12 in order to mine the wealth of information available for it. When appropriate, we included observations made with other E. coli variants (e.g., enterohemorragic E. coli [EHEC] or uropathogenic E. coli) or with the close relative Salmonella enterica. With easy to moderate effort, the network can be adapted to other enterobacterial relatives. However, more distantly related species may lack some of the global regulators discussed here.As a unifying theme, we chose the early stages of biofilm development. Defined as a sessile community of bacteria encased in a matrix, a biofilm tends to develop on a surface or an interface in a series of ordered steps, designated reversible attachment, irreversible attachment, maturation-1, maturation-2, and dispersion (121). Each step requires reprogramming of gene expression that occurs in response to the changing environment (122). The reprogramming associated with the earliest steps of biofilm development can be identified easily by the distinct organelles that decorate the bacterial surface. For example, reversible attachment often involves flagella that permit individual planktonic cells to swim toward an appropriate biotic or abiotic surface. Irreversible attachment involves the loss of these flagella and the elaboration of adhesive organelles (e.g., curli or type 1 fimbriae); the type of organelle depends on the environment. Finally, production of the colanic acid capsule permits construction of the distinctive three-dimensional structure typical of mature biofilms (for a recent review of biofilm formation, see reference 149).For the surface organelles to appear in proper order, expression of these organelles must be coordin...

show abstract

“…Here we describe the cloning of the ydgR gene, which was identified by sequence analysis as the E. coli homologue of tppB from Salmonella typhimurium (14). Based on growth experiments with mutant bacterial strains, tppB was already identified in 1984 as a tripeptide permease (15,16).…”

mentioning

confidence: 99%

Functional and Structural Characterization of a Prokaryotic Peptide Transporter with Features Similar to Mammalian PEPT1

Weitz

Harder

Casagrande

et al. 2007

Journal of Biological Chemistry

View full text Add to dashboard Cite

The ydgR gene of Escherichia coli encodes a protein of the proton-dependent oligopeptide transporter (POT) family. We cloned YdgR and overexpressed the His-tagged fusion protein in E. coli BL21 cells. Bacterial growth inhibition in the presence of the toxic phosphonopeptide alafosfalin established YgdR functionality. Transport was abolished in the presence of the proton ionophore carbonyl cyanide p-chlorophenylhydrazone, suggesting a proton-coupled transport mechanism. YdgR transports selectively only di-and tripeptides and structurally related peptidomimetics (such as aminocephalosporins) with a substrate recognition pattern almost identical to the mammalian peptide transporter PEPT1. The YdgR protein was purified to homogeneity from E. coli membranes. Blue native-polyacrylamide gel electrophoresis and transmission electron microscopy of detergent-solubilized YdgR suggest that it exists in monomeric form. Transmission electron microscopy revealed a crown-like structure with a diameter of ϳ8 nm and a central density. These are the first structural data obtained from a proton-dependent peptide transporter, and the YgdR protein seems an excellent model for studies on substrate and inhibitor interactions as well as on the molecular architecture of cell membrane peptide transporters.

show abstract

The Escherichia coli tppB ( ydgR ) Gene Represents a New Class of OmpR-Regulated Genes

Cited by 31 publications

References 48 publications

Bacterial peptide transporters: Messengers of nutrition to virulence

Bacterial peptide transporters: Messengers of nutrition to virulence

A Complex Transcription Network Controls the Early Stages of Biofilm Development byEscherichia coli

Functional and Structural Characterization of a Prokaryotic Peptide Transporter with Features Similar to Mammalian PEPT1

Contact Info

Product

Resources

About