Mutational analysis of the archaeal tyrosine recombinase SSV1 integrase suggests a mechanism of DNA cleavage in trans (Q42626370)

4 November 2017

title

Mutational analysis of the archaeal tyrosine recombinase SSV1 integrase suggests a mechanism of DNA cleavage in trans (English)

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4 November 2017

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Claire Letzelter

1

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4 November 2017

Michel Duguet

series ordinal

2

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4 November 2017

Marie-Claude Serre

series ordinal

3

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4 November 2017

language of work or name

English

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publication date

27 April 2004

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Journal of Biological Chemistry

4 November 2017

published in

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4 November 2017

volume

279

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4 November 2017

issue

28

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4 November 2017

page(s)

28936-28944

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The integrase family of tyrosine recombinases: evolution of a conserved active site domain

4 November 2017

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A newly identified, essential catalytic residue in a critical secondary structure element in the integrase family of site-specific recombinases is conserved in a similar element in eucaryotic type IB topoisomerases.

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A conformational switch controls the DNA cleavage activity of lambda integrase

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Flexibility in DNA recombination: structure of the lambda integrase catalytic core

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Wild-type Flp recombinase cleaves DNA in trans.

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Transfer RNA genes frequently serve as integration sites for prokaryotic genetic elements.

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Cleavage properties of an archaeal site-specific recombinase, the SSV1 integrase

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Autonomous DNA binding domains of lambda integrase recognize two different sequence families

21 January 2018

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The Cre recombinase cleaves the lox site in trans

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DNA cleavage in trans by the active site tyrosine during Flp recombination: Switching protein partners before exchanging strands

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Return to sobriety after the catalytic party

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M403971200

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4 November 2017

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