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Article

Substitutions of Conserved Residues in the C-terminal Region of DnaC Cause Thermolability in Helicase Loading.

The Journal of biological chemistry - 26 Feb 2016

Felczak Magdalena M, Sage Jay M, Hupert-Kocurek Katarzyna, Aykul Senem, Kaguni Jon M

Abstract excerpt

The DnaB-DnaC complex binds to the unwound DNA within the Escherichia coli replication origin in the helicase loading process, but the biochemical events that lead to its stable binding are uncertain. This study characterizes the function of specific C-terminal residues of DnaC. Genetic and biochemical characterization of proteins bearing F231S and W233L substitutions of DnaC reveals that their activity is...

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Identifiers

PMID: 26728455
DOI: 10.1074/jbc.M115.708586
PMCID: PMC4813501

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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.

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