Literature DB >> 20298194

Catalysis of site-specific recombination by Tn3 resolvase.

Femi J Olorunniji1, W Marshall Stark.   

Abstract

The active-site interactions involved in the catalysis of DNA site-specific recombination by the serine recombinases are still incompletely understood. Recent crystal structures of synaptic gammadelta resolvase-DNA intermediates and biochemical analysis of Tn3 resolvase mutants have provided new insights into the structure of the resolvase active site, and how interactions of the catalytic residues with the DNA substrate might promote the phosphoryl transfer reactions.

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Year:  2010        PMID: 20298194     DOI: 10.1042/BST0380417

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  4 in total

Review 1.  Topoisomerases and site-specific recombinases: similarities in structure and mechanism.

Authors:  Wei Yang
Journal:  Crit Rev Biochem Mol Biol       Date:  2010-12       Impact factor: 8.250

2.  Vaccinia virus F16 protein, a predicted catalytically inactive member of the prokaryotic serine recombinase superfamily, is targeted to nucleoli.

Authors:  Tatiana G Senkevich; Eugene V Koonin; Bernard Moss
Journal:  Virology       Date:  2011-07-12       Impact factor: 3.616

3.  Stereospecific suppression of active site mutants by methylphosphonate substituted substrates reveals the stereochemical course of site-specific DNA recombination.

Authors:  Paul A Rowley; Aashiq H Kachroo; Chien-Hui Ma; Anna D Maciaszek; Piotr Guga; Makkuni Jayaram
Journal:  Nucleic Acids Res       Date:  2015-05-20       Impact factor: 16.971

4.  Nicked-site substrates for a serine recombinase reveal enzyme-DNA communications and an essential tethering role of covalent enzyme-DNA linkages.

Authors:  Femi J Olorunniji; Arlene L McPherson; Hania J Pavlou; Michael J McIlwraith; John A Brazier; Richard Cosstick; W Marshall Stark
Journal:  Nucleic Acids Res       Date:  2015-05-18       Impact factor: 16.971

  4 in total

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