Peptides and ATP binding cassette peptide transporters

Detmers, Frank; Lanfermeijer, Frank C.; Poolman, Bert

doi:10.1016/s0923-2508(01)01196-2

Cited by 97 publications

(84 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In addition to nutrition of the cell, in microorganisms the Opp system is also involved in various signaling processes including regulation of gene expression, chemotaxis, competence development, sporulation, DNA transfer by conjugation, and virulence development (reviewed in Ref. 5). In L. lactis (and other lactic acid bacteria), the Opp system is an essential part of the proteolytic system because it transports into the cell ␤-casein-derived peptides formed by the cell wall-associated protease PrtP, enabling the organism to grow in milk.…”

Section: Atp-binding Cassette (Abc)mentioning

confidence: 99%

The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter

Doeven

Abele

Tampé

et al. 2004

Journal of Biological Chemistry

Self Cite

123

View full text Add to dashboard Cite

The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein OppA, which interacts with the translocator OppBCDF with higher affinity than unliganded OppA. Transport screening with combinatorial peptide libraries revealed that (i) the Opp transporter is not selective with respect to amino acid side chains of the transported peptides; (ii) any peptide that can bind to OppA is transported via Opp, including very long peptides up to 35 residues long; and (iii) the binding specificity of OppA largely determines the overall transport selectivity.

show abstract

Section: Atp-binding Cassette (Abc)mentioning

confidence: 99%

The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter

Doeven

Abele

Tampé

et al. 2004

Journal of Biological Chemistry

Self Cite

123

View full text Add to dashboard Cite

show abstract

“…The ATP binding cassette (ABC) superfamily of transporters comprises at least seven families whose members transport diverse substrates across different types of cellular membranes (Ambudkar and Gottesman, 1998). The ABCB family members are best known for conferring multiple drug resistance, but members of some ABCB subfamilies are capable of transporting peptides that lack classical export signals (Detmers et al, 2001). Homologs of these subfamily members such as the TAP proteins, as well as other ABC transporters that transport peptides, have been found in microorganisms, plants and metazoans.…”

Section: Introductionmentioning

confidence: 99%

TagA, a putative serine protease/ABC transporter ofDictyosteliumthat is required for cell fate determination at the onset of development

et al. 2003

View full text Add to dashboard Cite

The tag genes of Dictyostelium are predicted to encode multi-domain proteins consisting of serine protease and ATP-binding cassette transporter domains. We have identified a novel tag gene, tagA, which is involved in cell type differentiation. The tagA mRNA accumulates during the first four hours of development,whereas TagA protein accumulates between two and ten hours of development and decreases thereafter. Wild-type cells express tagA in prespore cells and mature spores, defining tagA expression as prespore specific. However, tagA mutant cells that activate the tagA promoter do not sporulate, but instead form part of the outer basal disc and lower cup of the fruiting body. tagA mutant aggregates elaborate multiple prestalk cell regions during development and produce spores asynchronously and with low viability. tagA mutants produce about twice as many prestalk cells as the wild type as judged by a prestalk cell reporter construct. When mixed with wild-type cells, tagA- cells become overrepresented in the prestalk cell population, suggesting that this phenotype is cell-autonomous. These results suggest that TagA is required for the specification of an initial population of prespore cells in which tagA is expressed. Expression profiling uncovered a delay in the transcriptional program between 2 and 6 hours, coincident with TagA expression, revealing an early function for TagA. TagA also appears to play a general role in cell fate determination since tagA mutants express a spore coat protein gene (cotB) within vacuolated cells that form part of the stalk and they express a prestalk/stalk-specific gene (ecmB)within cells that become spores. The expression of TagA at two hours of development, the observed coincident delay in the transcriptional program and the subsequent mis-expression of cell-type specific genes provide evidence for cell fate determination beginning in some cells much earlier than previously believed.

show abstract

“…78 For example, the amino acid leucine is known to induce the expression of OppA peptide transporter in E. coli. 79 The exponential phase specific small RNA GcvB inhibits the binding of ribosome to the transcripts of ABC transporters OppA and DppA in S. Typhimurium.…”

mentioning

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

Peptides and ATP binding cassette peptide transporters

Cited by 97 publications

References 60 publications

The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter

The Binding Specificity of OppA Determines the Selectivity of the Oligopeptide ATP-binding Cassette Transporter

TagA, a putative serine protease/ABC transporter ofDictyosteliumthat is required for cell fate determination at the onset of development

Bacterial peptide transporters: Messengers of nutrition to virulence

Contact Info

Product

Resources

About