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Article

The C-terminal domain is sufficient for endonuclease activity of Neisseria gonorrhoeae MutL.

The Biochemical journal - 25 Sept 2009

Duppatla Viswanadham, Bodda Chiranjeevi, Urbanke Claus, Friedhoff Peter, Rao Desirazu N

Abstract excerpt

The mutL gene of Neisseria gonorrhoeae has been cloned and the gene product purified. We have found that the homodimeric N. gonorrhoeae MutL (NgoL) protein displays an endonuclease activity that incises covalently closed circular DNA in the presence of Mn(2+), Mg(2+) or Ca(2+) ions, unlike human MutLalpha which shows endonuclease activity only in the presence of Mn(2+). We report in the present paper that the...

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Source

Identifiers

PMID: 19656086
DOI: 10.1042/BJ20090626

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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The C-terminal domain is sufficient for endonuclease activity of Neisseria gonorrhoeae MutL.PMID 19656086Read ↗

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