Results 11 to 20 of about 362,571 (177)

Unveiling Hidden Catalytic Contributions of the Conserved His/Trp-III in Tyrosine Recombinases: Assembly of a Novel Active Site in Flp Recombinase Harboring Alanine at this Position [PDF]

open access: yesJournal of Molecular Biology, 2007
The catalytic pentad of tyrosine recombinases, that assists the tyrosine nucleophile, includes a conserved histidine/tryptophan (His/Trp-III). Flp and Cre harbor tryptophan at this position; most of their kin recombinases display histidine. Contrary to the conservation rule, Flp(W330F) is a much stronger recombinase than Flp(W330H).
Chien-Hui Ma, Makkuni Jayaram
exaly   +4 more sources

The XerC recombinase of Proteus mirabilis: characterization and interaction with other tyrosine recombinases. [PDF]

open access: yesFEMS Microbiology Letters, 2003
XerC and XerD are two site-specific recombinases, which act on different sites to maintain replicons in a monomeric state. This system, which was first discovered and studied in Escherichia coli, is present in several species including Proteus mirabilis, where the XerD recombinase was previously characterized by our laboratory. In this paper, we report
M. Villion, G. Szatmari
semanticscholar   +3 more sources

Mechanistic modelling of tyrosine recombination reveals key parameters determining the performance of a CAR T cell switching circuit

open access: yesEngineering Biology, 2020
Inducible genetic switches based on tyrosine recombinase-based DNA excision are a promising platform for the regulation and control of chimeric antigen receptor (CAR) T cell activity in cancer immunotherapy. These switches exploit the increased stability
Jack E. Bowyer   +3 more
doaj   +2 more sources

Minimal mutational requirements for conversion of a telomere resolvase into a Cre-like site-specific recombinase. [PDF]

open access: yesPLoS ONE
Hairpin telomere resolvases comprise a family of enzymes that produce the hairpin (hp) telomeres of bacteria and their phages that possess linear chromosomes and plasmids terminated by covalently closed hp telomeres.
Shu Hui Huang, Kerri Kobryn
doaj   +2 more sources

Nearest-neighbor amino acids of specificity-determining residues influence the activity of engineered Cre-type recombinases

open access: yesScientific Reports, 2020
The tyrosine-type site-specific DNA recombinase Cre recombines its target site, loxP, with high activity and specificity without cross-recombining the target sites of highly related recombinases. Understanding how Cre achieves this precision is key to be
Anjali Soni   +3 more
doaj   +2 more sources

Sequence analysis allows functional annotation of tyrosine recombinases in prokaryotic genomes [PDF]

open access: yesbioRxiv, 2019
Background Tyrosine recombinases perform site-specific genetic recombination in bacteria and archaea. They safeguard genome integrity by resolving chromosome multimers, as well as mobilize transposons, phages and integrons, driving dissemination of ...
Georgy Smyshlyaev   +2 more
semanticscholar   +2 more sources

Conversion of a telomere resolvase into a Cre-like site-specific recombinase. [PDF]

open access: yesPLoS ONE
Hairpin telomere resolvases are a unique family of enzymes involved in producing the hairpin (hp) telomeres of bacterial organisms and phages that possess linear DNA's terminated by hp telomeres.
Shu Hui Huang   +2 more
doaj   +2 more sources

Resolution of Mismatched Overlap Holliday Junction Intermediates by the Tyrosine Recombinase IntDOT [PDF]

open access: yesJournal of Bacteriology, 2017
ABSTRACT CTnDOT is an integrated conjugative element found in Bacteroides species. CTnDOT contains and transfers antibiotic resistance genes. The element integrates into and excises from the host chromosome via a Holliday junction (HJ) intermediate as part of a site-specific recombination mechanism.
Kenneth Ringwald   +2 more
semanticscholar   +3 more sources

Identification of the Integration/Excision Module and Regulatory Elements Involved in the Mobility of IME8, an Integrative and Mobilizable Element From Mosquitocidal Lysinibacillus sphaericus [PDF]

open access: yesMicrobial Biotechnology
Lysinibacillus sphaericus, a bacterium successfully used in the control of mosquitoes, bears its insecticidal traits in GI8, a recently identified mosquitocidal genomic island.
Yifeng Hu   +5 more
doaj   +2 more sources

Home - About - Disclaimer - Privacy