(Q28346667)

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Converting MlyI endonuclease into a nicking enzyme by changing its oligomerization state

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title

Converting MlyI endonuclease into a nicking enzyme by changing its oligomerization state (English)

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author name string

C E Besnier

series ordinal

1

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H Kong

series ordinal

2

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language of work or name

English

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publication date

September 2001

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published in

EMBO Reports

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volume

2

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page(s)

782-6

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issue

9

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cites work

FokI dimerization is required for DNA cleavage

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Structure of FokI has implications for DNA cleavage

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The nicking endonuclease N.BstNBI is closely related to type IIs restriction endonucleases MlyI and PleI

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Characterization of the specific DNA nicking activity of restriction endonuclease N.BstNBI.

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Preparation of DNA substrates for in vitro mismatch repair

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The monomeric homing endonuclease PI-SceI has two catalytic centres for cleavage of the two strands of its DNA substrate

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Simultaneous strand displacement amplification and fluorescence polarization detection of Chlamydia trachomatis DNA.

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Introduction of asymmetry in the naturally symmetric restriction endonuclease EcoRV to investigate intersubunit communication in the homodimeric protein

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Multiple DNA conformational changes induced by an initiator protein precede the nicking reaction in a rolling circle replication origin

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Methyl-directed DNA mismatch correction.

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Restriction and modification systems

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Sau3AI, a monomeric type II restriction endonuclease that dimerizes on the DNA and thereby induces DNA loops

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FokI requires two specific DNA sites for cleavage

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[N.BstSE--a site-specific nickase from Bacillus stearothermophilus SE-589]

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A PCR-based strategy for extensive mutagenesis of a target DNA sequence

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1093/EMBO-REPORTS/KVE175

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ResearchGate publication ID

11824642

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(Q28346667)

Converting MlyI endonuclease into a nicking enzyme by changing its oligomerization state

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