Tyrosine Recombinase

Tyrosine recombinases are site-specific DNA rearrangement enzymes that alter genetic information by exchanging strands at defined recognition sites. They bind two target DNA sequences, bring them together, and use an active-site tyrosine to cleave one DNA strand and form a temporary covalent DNA-enzyme intermediate; strand exchange and re-ligation then produce recombination without requiring extensive sequence homology. Depending on site orientation, this reaction can integrate, excise, invert, or resolve DNA segments. In biology, tyrosine recombinases regulate microbial genomes and bacteriophage life cycles, while engineered systems such as Cre-lox support conditional gene deletion, lineage tracing, transgenesis, and controlled genome engineering.

Tyrosine Recombinase - Related Videos

Research

JoVE Journal - Biology

Molecular Evolution of the Tre Recombinase

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Cited by 4 •

2008

Here we report the generation of Tre recombinase through directed, molecular evolution. Tre recombinase recognizes a pre-defined target sequence within the LTR sequences of the HIV-1 provirus, resulting in the excision and eradication of the provirus from infected human cells. While still in its infancy, directed molecular evolution will allow the creation of custom enzymes that will serve as tools of molecular surgery and molecular medicine.

Principles of Site-Specific Recombinase (SSR) Technology

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Cited by 14 •

2008

The advent of site-specific recombinase (SSR) technology and the Cre/lox system has led to numerous advances in molecular biology, and has proven itself as a valuable tool for assessing gene function in transgenic animals. This interview discusses the mechanism of site specific recombination by Cyclization recombinase (Cre) and how the use of this enzyme has led to the development of conditional mutagenesis, which has significant advantages over traditional knock out strategies.

Education

JoVE Core - Cell Biology

Receptor Tyrosine Kinases

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2025

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...

Interview: HIV-1 Proviral DNA Excision Using an Evolved Recombinase

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Cited by 2 •

2008

Current HIV-1 strategies act to suppress the viral life cycle but do not effectively eradicate infection. Here, we demonstrate that an engineered recombinase can efficiently excise integrated HIV-1 proviral DNA from the genome of infected cells.

Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia

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Cited by 6 •

2013

Receptor tyrosine kinases are ectopically expressed in many cancers and have been identified as therapeutic targets in acute leukemia. This manuscript describes an efficient strategy for pre-clinical evaluation of tyrosine kinase inhibitors for the treatment of acute leukemia.

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