| Title: |
The Xer activation factor of TLCΦ expands the possibilities for Xer recombination |
| Authors: |
Miele, Solange; Provan, James, Iain; Vergne, Justine; Possoz, Christophe; Ochsenbein, Françoise; Barre, François-Xavier |
| Contributors: |
Institut de Biologie Intégrative de la Cellule (I2BC); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS); Département Biologie des Génomes (DBG); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS); Evolution et maintenance des chromosomes circulaires (EMC2); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC); Fondation pour la Recherche Medicale EQU202003010328; ANR-16-CE12-0030,PhenX,Base moléculaire de l'activation de la recombinaison Xer par les phages(2016); ANR-21-CE35-0013,InXS,Stabilisation de complexes de recombinaison Xer intégratifs(2021); ANR-18-CE12-0012,BaCh,Cohésion des Chromosomes Frères dans la Bactérie(2018); European Project: SFRH/BPD/28159/2006,FCT::Pós-Doutoramento,SFRH/2006,SFRH/BPD/28159/2006(2008) |
| Source: |
ISSN: 0305-1048. |
| Publisher Information: |
CCSD; Oxford University Press |
| Publication Year: |
2022 |
| Collection: |
HAL-CEA (Commissariat à l'énergie atomique et aux énergies alternatives) |
| Subject Terms: |
[SDV]Life Sciences [q-bio] |
| Description: |
International audience ; The chromosome dimer resolution machinery of bacteria is generally composed of two tyrosine recombinases, XerC and XerD. They resolve chromosome dimers by adding a crossover between sister copies of a specific site, dif. The reaction depends on a cell division protein, FtsK, which activates XerD by protein-protein interactions. The toxin-linked cryptic satellite phage (TLC) of Vibrio cholerae, which participates in the emergence of cholera epidemic strains, carries a dif-like attachment site (attP). TLC exploits the Xer machinery to integrate into the dif site of its host chromosomes. The TLC integration reaction escapes the control of FtsK because TLC encodes for its own XerD-activation factor, XafT. Additionally, TLC attP is a poor substrate for XerD binding, in apparent contradiction with the high integration efficiency of the phage. Here, we present a sequencing-based methodology to analyse the integration and excision efficiency of thousands of synthetic mini-TLC plasmids with differing attP sites in vivo. This methodology is applicable to the finegrained analyses of DNA transactions on a wider scale. In addition, we compared the efficiency with which XafT and the XerD-activation domain of FtsK drive recombination reactions in vitro. Our results suggest that XafT not only activates XerD-catalysis but also helps form and/or stabilize synaptic complexes between imperfect Xer recombination sites. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| Relation: |
info:eu-repo/grantAgreement/FCT//SFRH/BPD/28159/2006/EU/MOLECULAR MECHANISM OF HEALING, REPAIR AND REGENERATION IN VERTEBRATES/SFRH/BPD/28159/2006 |
| DOI: |
10.1093/nar/gkac429 |
| Availability: |
https://hal.science/hal-03872179; https://hal.science/hal-03872179v1/document; https://hal.science/hal-03872179v1/file/gkac429.pdf; https://doi.org/10.1093/nar/gkac429 |
| Rights: |
http://creativecommons.org/licenses/by/ ; info:eu-repo/semantics/OpenAccess |
| Accession Number: |
edsbas.4E1E97B9 |
| Database: |
BASE |