Species specificity in the activation of Xer recombination at dif by FtsK.

In Escherichia coli, chromosome dimers are resolved to monomers by the addition of a single cross-over at a specific locus on the chromosome, dif. Recombination is performed by two tyrosine recombinases, XerC and XerD, and requires the action of an additional protein, FtsK. We show that Haemophilus...

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Main Authors: Yates, J, Aroyo, M, Sherratt, D, Barre, F
Format: Journal article
Language:English
Published: 2003
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author Yates, J
Aroyo, M
Sherratt, D
Barre, F
author_facet Yates, J
Aroyo, M
Sherratt, D
Barre, F
author_sort Yates, J
collection OXFORD
description In Escherichia coli, chromosome dimers are resolved to monomers by the addition of a single cross-over at a specific locus on the chromosome, dif. Recombination is performed by two tyrosine recombinases, XerC and XerD, and requires the action of an additional protein, FtsK. We show that Haemophilus influenzae FtsK activates recombination by H. influenzae XerCD at H. influenzae dif. However, it cannot activate recombination by E. coli XerCD. Reciprocally, E. coli FtsK cannot activate recombination by the H. influenzae recombinases at H. influenzae dif. We took advantage of this species specificity to gain further insight into the mechanism of activation of Xer recombination at dif by FtsK. We mapped the region of FtsK implicated in species specificity to the extreme 140-amino-acid C-terminal residues of the protein. Our results suggest that FtsK interacts directly with XerCD in order to activate recombination at dif.
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spelling oxford-uuid:37b2aa7e-5a4b-473d-9ec4-0826950348002022-03-26T13:45:35ZSpecies specificity in the activation of Xer recombination at dif by FtsK.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:37b2aa7e-5a4b-473d-9ec4-082695034800EnglishSymplectic Elements at Oxford2003Yates, JAroyo, MSherratt, DBarre, FIn Escherichia coli, chromosome dimers are resolved to monomers by the addition of a single cross-over at a specific locus on the chromosome, dif. Recombination is performed by two tyrosine recombinases, XerC and XerD, and requires the action of an additional protein, FtsK. We show that Haemophilus influenzae FtsK activates recombination by H. influenzae XerCD at H. influenzae dif. However, it cannot activate recombination by E. coli XerCD. Reciprocally, E. coli FtsK cannot activate recombination by the H. influenzae recombinases at H. influenzae dif. We took advantage of this species specificity to gain further insight into the mechanism of activation of Xer recombination at dif by FtsK. We mapped the region of FtsK implicated in species specificity to the extreme 140-amino-acid C-terminal residues of the protein. Our results suggest that FtsK interacts directly with XerCD in order to activate recombination at dif.
spellingShingle Yates, J
Aroyo, M
Sherratt, D
Barre, F
Species specificity in the activation of Xer recombination at dif by FtsK.
title Species specificity in the activation of Xer recombination at dif by FtsK.
title_full Species specificity in the activation of Xer recombination at dif by FtsK.
title_fullStr Species specificity in the activation of Xer recombination at dif by FtsK.
title_full_unstemmed Species specificity in the activation of Xer recombination at dif by FtsK.
title_short Species specificity in the activation of Xer recombination at dif by FtsK.
title_sort species specificity in the activation of xer recombination at dif by ftsk
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