Results 151 to 160 of about 362,571 (177)
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Cre Recombinase and Other Tyrosine Recombinases

Chemical Reviews, 2016
Tyrosine-type site-specific recombinases (T-SSRs) have opened new avenues for the predictable modification of genomes as they enable precise genome editing in heterologous hosts. These enzymes are ubiquitous in eubacteria, prevalent in archaea and temperate phages, present in certain yeast strains, but barely found in higher eukaryotes.
Joachim Hauber   +2 more
exaly   +4 more sources

Dual Recombinase-Mediated Cassette Exchange by Tyrosine Site-Specific Recombinases

Methods in Molecular Biology, 2017
Recombinase-mediated cassette exchange, or RMCE, is a genome engineering tool that can be used to swap DNA fragments of interest between two DNA molecules. In a variation of RMCE, called dual RMCE, the exchange of DNA fragments is mediated by two recombinases in contrast to one recombinase in the classic RMCE reaction.
Eugenia Voziyanova   +2 more
exaly   +4 more sources

Strand Selection by the Tyrosine Recombinases

Progress in Molecular Biology and Translational Science, 2005
Publisher Summary This chapter focuses on four tyrosine recombinases for which there is a wealth of biochemical and structural data. This chapter reviews the biochemical and structural findings for each of these enzymes. This chapter also examines the factors that influence strand selection and consider the possible function of strand selection in ...
Paul D Sadowski
exaly   +4 more sources

Using Purified Tyrosine Site-Specific Recombinases In Vitro to Rapidly Construct and Diversify Metabolic Pathways

Methods in Molecular Biology, 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.
Yizhi Cai, Cai Yizhi
exaly   +6 more sources

Peptide inhibitors of DNA cleavage by tyrosine recombinases and topoisomerases.

Journal of Molecular Biology, 2000
The 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
semanticscholar   +3 more sources

Involvement of IntTn916 Type Tyrosine Recombinase in Nucleoid Structure in Deinococcus radiodurans

Journal of Basic Microbiology
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 ...
Shruti Mishra   +3 more
semanticscholar   +3 more sources

DIRS-1 and the other tyrosine recombinase retrotransposons

Cytogenetic and Genome Research, 2005
DIRS-1 is a retroelement from the slime mold <i>Dictyostelium discoideum</i>. Until recently only two related retrotransposons had been described: PAT from the nematode <i>Panagrellus redivivus</i> and <i>Prt1</i> from the zygomycete fungus <i>Phycomyces blakesleeanus</i>.
R T M, Poulter, T J D, Goodwin
openaire   +2 more sources

Transgenic expression of Cre recombinase from the tyrosine hydroxylase locus

genesis, 2004
AbstractCatecholaminergic neurons are affected in several neurological and psychiatric diseases. Tyrosine hydroxylase (TH) is the first, rate‐limiting enzyme in catecholamine synthesis. We report a knockin mouse expressing Cre‐recombinase from the 3′‐untranslated region of the endogenous Th gene by means of an internal ribosomal entry sequence (IRES ...
Jonas, Lindeberg   +6 more
openaire   +2 more sources

The VIPER elements of trypanosomes constitute a novel group of tyrosine recombinase-enconding retrotransposons

Molecular and Biochemical Parasitology, 2006
VIPER was initially characterized as a 2326bp LTR-like retroelement associated to SIRE, a short interspersed repetitive element specific of Trypanosoma cruzi. It carried a single ORF that coded for a putative reverse transcriptase-RNAse H protein, suggesting that it could be a truncated copy of a longer retroelement. Herein we report the identification
Hernan A, Lorenzi   +2 more
openaire   +2 more sources

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