Coordinated control XerC and XerD catalytic during holliday junction resolution

Site-specific recombinases XerC and XerD function in the segregation of circular bacterial replicons. In a recombining nucleoprotein complex containing two molecules each of XerC and XerD, coordinated reciprocal switches in recombinase activity ensure that only XerC or XerD is active at any one time...

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Main Authors: Arciszewska, L, Baker, R, Hallet, B, Sherratt, D
Format: Journal article
Language:English
Published: 2000
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author Arciszewska, L
Baker, R
Hallet, B
Sherratt, D
author_facet Arciszewska, L
Baker, R
Hallet, B
Sherratt, D
author_sort Arciszewska, L
collection OXFORD
description Site-specific recombinases XerC and XerD function in the segregation of circular bacterial replicons. In a recombining nucleoprotein complex containing two molecules each of XerC and XerD, coordinated reciprocal switches in recombinase activity ensure that only XerC or XerD is active at any one time. Mutated recombinases that carry substitutions of a catalytic arginine residue stimulate cleavage and strand exchange mediated by the partner recombinase on DNA substrates that are normally recombined poorly by the partner. This is associated with a reciprocal impairment of the recombinase's own ability to initiate catalysis. The extent of this switch in catalysis is modulated by changes in recombination site sequence and is not a direct consequence of any catalytic defect. We propose that altered interactions between the mutated proteins and their wild-type partners lead to an increased level of an alternative Holliday junction intermediate that has a conformation appropriate for resolution by the partner recombinase. The results indicate how subtle changes in protein-DNA architecture at a Holliday junction can redirect recombination outcome. (C) 2000 Academic Press.
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spelling oxford-uuid:b7caa5bf-56ca-4f6b-886b-86ad3d8d35a72022-03-27T04:51:10ZCoordinated control XerC and XerD catalytic during holliday junction resolutionJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b7caa5bf-56ca-4f6b-886b-86ad3d8d35a7EnglishSymplectic Elements at Oxford2000Arciszewska, LBaker, RHallet, BSherratt, DSite-specific recombinases XerC and XerD function in the segregation of circular bacterial replicons. In a recombining nucleoprotein complex containing two molecules each of XerC and XerD, coordinated reciprocal switches in recombinase activity ensure that only XerC or XerD is active at any one time. Mutated recombinases that carry substitutions of a catalytic arginine residue stimulate cleavage and strand exchange mediated by the partner recombinase on DNA substrates that are normally recombined poorly by the partner. This is associated with a reciprocal impairment of the recombinase's own ability to initiate catalysis. The extent of this switch in catalysis is modulated by changes in recombination site sequence and is not a direct consequence of any catalytic defect. We propose that altered interactions between the mutated proteins and their wild-type partners lead to an increased level of an alternative Holliday junction intermediate that has a conformation appropriate for resolution by the partner recombinase. The results indicate how subtle changes in protein-DNA architecture at a Holliday junction can redirect recombination outcome. (C) 2000 Academic Press.
spellingShingle Arciszewska, L
Baker, R
Hallet, B
Sherratt, D
Coordinated control XerC and XerD catalytic during holliday junction resolution
title Coordinated control XerC and XerD catalytic during holliday junction resolution
title_full Coordinated control XerC and XerD catalytic during holliday junction resolution
title_fullStr Coordinated control XerC and XerD catalytic during holliday junction resolution
title_full_unstemmed Coordinated control XerC and XerD catalytic during holliday junction resolution
title_short Coordinated control XerC and XerD catalytic during holliday junction resolution
title_sort coordinated control xerc and xerd catalytic during holliday junction resolution
work_keys_str_mv AT arciszewskal coordinatedcontrolxercandxerdcatalyticduringhollidayjunctionresolution
AT bakerr coordinatedcontrolxercandxerdcatalyticduringhollidayjunctionresolution
AT halletb coordinatedcontrolxercandxerdcatalyticduringhollidayjunctionresolution
AT sherrattd coordinatedcontrolxercandxerdcatalyticduringhollidayjunctionresolution