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Article

Design and characterization of Escherichia coli mutants devoid of Ap4N-hydrolase activity.

Journal of molecular biology - 20 Mar 1990

Lévĕque F, Blanchin-Roland S, Fayat G, Plateau P, Blanquet S

Abstract excerpt

Escherichia coli strains with abnormally high concentrations of bis(5'-nucleosidyl)-tetraphosphates (Ap4N) were constructed by disrupting the apaH gene that encodes Ap4N-hydrolase. Variation deletions and insertions were also introduced in apaG and ksgA, two other cistrons of the ksgA apaGH operon. In all strains studied, a correlation was found between the residual Ap4N-hydrolase activity and the intracellular...

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Identifiers

PMID: 2157025
DOI: 10.1016/0022-2836(90)90127-8

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

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