Journal
FEBS LETTERS
Volume 590, Issue 12, Pages 1816-1825Publisher
WILEY
DOI: 10.1002/1873-3468.12224
Keywords
arginine biosynthesis; carbamoylphosphate synthase; DNA topology; Protein-DNA interactions; pyrimidine biosynthesis; transcription regulation
Funding
- Research Foundation Flanders (FWO-Vlaanderen) [G.0429.06]
- Research Council of the Vrije Universiteit Brussel (OZR-VUB)
- Vlaamse Gemeenschapscommissie
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Escherichia coli aminopeptidase A (PepA) is a trigger enzyme endowed with catalytic activity and DNA-binding properties prominent in transcriptional regulation and site-specific DNA recombination. The current work demonstrates that PepA is a repressor in its own right, capable of specifically inhibiting transcription initiation at promoter P1 of the carAB operon, encoding carbamoylphosphate synthase. Furthermore, in vitro topology studies performed with DNA minicircles demonstrate that PepA binding constrains a single positive supercoil in the carP1 control region. Such a topological event is understood to constitute an impediment to transcription initiation and may serve as a mechanism to regulate gene expression.
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