Regulation of peptide transport in Escherichia coli: induction of the trp-linked operon encoding the oligopeptide permease.

AUTOR(ES)

Andrews, J C

RESUMO

Growth of Escherichia coli in medium containing leucine results in increased entry of exogenously supplied tripeptides into the bacterial cell. This leucine-mediated elevation of peptide transport required expression of the trp-linked opp operon and was accompanied by increased sensitivity to toxic tripeptides, by an enhanced capacity to utilize nutritional peptides, and by an increase in both the velocity and apparent steady-state level of L-[U-14C]alanyl-L-alanyl-L-alanine accumulation for E. coli grown in leucine-containing medium relative to these parameters of peptide transport measured with bacteria grown in media lacking leucine. Direct measurement of opp operon expression by pulse-labeling experiments demonstrated that growth of E. coli in the presence of leucine resulted in increased synthesis of the oppA-encoded periplasmic binding protein.

Documentos Relacionados

• opp-lac Operon fusions and transcriptional regulation of the Escherichia coli trp-linked oligopeptide permease.
• Phaseolotoxin transport in Escherichia coli and Salmonella typhimurium via the oligopeptide permease.
• Regulation of fatty acid transport in Escherichia coli: analysis by operon fusion.
• Illicit Transport: The Oligopeptide Permease
• Regulation of enterobactin iron transport in Escherichia coli: characterization of ent::Mu d(Apr lac) operon fusions.