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Article

Mutagenesis of PepA suggests a new model for the Xer/cer synaptic complex.

Molecular microbiology - 1 Aug 2005

Reijns Martin, Lu Yangjie, Leach Stephen, Colloms Sean D

Abstract excerpt

PepA is an aminopeptidase and also functions as a DNA-binding protein in two unrelated systems in Escherichia coli: Xer site-specific recombination and transcriptional regulation of carAB. In these systems, PepA binds to and brings together distant segments of DNA to form interwrapped, nucleosome-like structures. Here we report the selection of PepA mutants that were unable to support efficient Xer recombination....

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Identifiers

PMID: 16091035
DOI: 10.1111/j.1365-2958.2005.04716.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Mutagenesis of PepA suggests a new model for the Xer/cer synaptic complex.PMID 16091035Read ↗

Mutational analysis of Escherichia coli PepA, a multifunctional DNA-binding aminopeptidase.Semantic proximity Read ↗

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X‐ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site‐specific recombinationSemantic proximity Read ↗

The ArcA/ArcB two-component regulatory system of Escherichia coli is essential for Xer site-specific recombination at psi.Semantic proximity Read ↗

carP, involved in pyrimidine regulation of the Escherichia coli carbamoylphosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColEI multimers.Semantic proximity Read ↗

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