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Article

Structure, subunit organization and behavior of the asymmetric Type IIT restriction endonuclease BbvCI.

Nucleic acids research - 10 Jan 2019

Shen Betty W, Doyle Lindsey, Bradley Phil, Heiter Daniel F, Lunnen Keith D, Wilson Geoffrey G, Stoddard Barry L

Abstract excerpt

BbvCI, a Type IIT restriction endonuclease, recognizes and cleaves the seven base pair sequence 5'-CCTCAGC-3', generating 3-base, 5'-overhangs. BbvCI is composed of two protein subunits, each containing one catalytic site. Either site can be inactivated by mutation resulting in enzyme variants that nick DNA in a strand-specific manner. Here we demonstrate that the holoenzyme is labile, with the R1 subunit...

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Identifiers

PMID: 30395313
DOI: 10.1093/nar/gky1059
PMCID: PMC6326814

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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