Results 181 to 190 of about 205,532 (202)
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Peptide inhibitors of DNA cleavage by tyrosine recombinases and topoisomerases
Journal of Molecular Biology, 2000The study of biochemical pathways requires the isolation and characterization of each and every intermediate in the pathway. For the site-specific recombination reactions catalyzed by the bacteriophage lambda tyrosine recombinase integrase (Int), this has been difficult because of the high level of efficiency of the reaction, the highly reversible ...
M, Klemm +4 more
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Archives of Microbiology, 2010
MrpA is the multimer resolution protein of the Streptomyces coelicolor A3(2) plasmid SCP2*. Previously, MrpA was found to significantly increase the stability of SCP2*-derived plasmids in Streptomyces lividans. The present report gives a functional characterization of MrpA.
Josef Altenbuchner, Lydia Warth
exaly +3 more sources
MrpA is the multimer resolution protein of the Streptomyces coelicolor A3(2) plasmid SCP2*. Previously, MrpA was found to significantly increase the stability of SCP2*-derived plasmids in Streptomyces lividans. The present report gives a functional characterization of MrpA.
Josef Altenbuchner, Lydia Warth
exaly +3 more sources
Mutational Analysis of the Archaeal Tyrosine Recombinase SSV1 Integrase Suggests a Mechanism of DNA Cleavage in trans* [PDF]
Journal of Biological Chemistry, 2004 The only tyrosine recombinase so far studied in archaea, the SSV1 integrase, harbors several changes in the canonical residues forming the catalytic pocket of this family of recombinases. This raised the possibility of a different mechanism for archaeal tyrosine recombinase.
Marie-Claude Serre
exaly +3 more sources
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]
Journal 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).
Makkuni Jayaram, Yuri Voziyanov
exaly +3 more sources
Cryptons: a group of tyrosine-recombinase-encoding DNA transposons from pathogenic fungi
Microbiology, 2003A new group of transposable elements, which the authors have named cryptons, was detected in several pathogenic fungi, including the basidiomyceteCryptococcus neoformans, and the ascomycetesCoccidioides posadasiiandHistoplasma capsulatum. These elements are unlike any previously described transposons. An archetypal member of the group, cryptonCn1, is 4
Timothy J D, Goodwin +2 more
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Molecular Diversity, 2011
Holliday junctions (HJs) are critical intermediates in many recombination-dependent DNA repair pathways. Our lab has previously identified several hexameric peptides that target HJ intermediates formed in DNA recombination reactions. One of the most potent peptides, WRWYCR, is active as a homodimer and has shown bactericidal activity partly because of ...
Marc C, Rideout +8 more
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Holliday junctions (HJs) are critical intermediates in many recombination-dependent DNA repair pathways. Our lab has previously identified several hexameric peptides that target HJ intermediates formed in DNA recombination reactions. One of the most potent peptides, WRWYCR, is active as a homodimer and has shown bactericidal activity partly because of ...
Marc C, Rideout +8 more
openaire +2 more sources
Involvement of Int Tn916 Type Tyrosine Recombinase in Nucleoid Structure in Deinococcus radiodurans
Journal of Basic MicrobiologyABSTRACT Tyrosine recombinases (YRs) are widespread among prokaryotes and archaea, catalyzing site‐specific DNA recombination reactions in a variety of cellular processes like chromosome dimer resolution, transfer of mobile genetic elements, and DNA insertion. Deinococcus radiodurans
Shruti Mishra +3 more
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2017
The site-specific recombinase Cre was previously reported to have in vitro activity. Here, we describe the method of purifying two new tyrosine site-specific recombinases VCre and Dre along with Cre by nickel affinity chromatography. We proved the in vitro function of the VCre and Dre on their respective conditional recombination sites.
Liu W, Tuck L, Marles-Wright J, Cai Y
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The site-specific recombinase Cre was previously reported to have in vitro activity. Here, we describe the method of purifying two new tyrosine site-specific recombinases VCre and Dre along with Cre by nickel affinity chromatography. We proved the in vitro function of the VCre and Dre on their respective conditional recombination sites.
Liu W, Tuck L, Marles-Wright J, Cai Y
openaire +4 more sources
2018
Site-specific recombinases are a family of DNA-modifying enzymes that can recognize short specific DNA sequences and drive recombination between them to rearrange DNA fragments which results in excision, integration or inversion. Here I describe in vivo application of the recombinases for chassis optimization for heterologous pathway expression in ...
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Site-specific recombinases are a family of DNA-modifying enzymes that can recognize short specific DNA sequences and drive recombination between them to rearrange DNA fragments which results in excision, integration or inversion. Here I describe in vivo application of the recombinases for chassis optimization for heterologous pathway expression in ...
openaire +1 more source