Transposition and site-specific recombination: adapting DNA cut-and-paste mechanisms to a variety of genetic rearrangements. 1997

B Hallet, and D J Sherratt
Department of Biochemistry, University of Oxford, UK. Hallet@bioch.ox.ac.uk

In bacteria, two categories of specialised recombination promote a variety of DNA rearrangements. Transposition is the process by which genetic elements move between different locations of the genome, whereas site-specific recombination is a reaction in which DNA strands are broken and exchanged at precise positions of two target DNA loci to achieve determined biological function. Both types of recombination are represented by diverse genetic systems which generally encode their own recombination enzymes. These enzymes, generically called transposases and site-specific recombinases, can be grouped into several families on the basis of amino acid sequence similarities, which, in some cases, are limited to a signature of a few residues involved in catalysis. The well characterised site-specific recombinases are found to belong to two distinct groups whereas the transposases form a large super-family of enzymes encompassing recombinases from both prokaryotes and eukaryotes. In spite of important differences in the catalytic mechanisms used by these three classes of enzymes to cut and rejoin DNA molecules, similar strategies are used to coordinate the biochemical steps of the recombination reaction and to control its outcome. This review summarises our current understanding of transposition and site-specific recombination, attempting to illustrate how relatively conserved DNA cut-and-paste mechanisms can be used to bring about a variety of complex DNA rearrangements.

UI MeSH Term Description Entries
D008957 Models, Genetic Theoretical representations that simulate the behavior or activity of genetic processes or phenomena. They include the use of mathematical equations, computers, and other electronic equipment. Genetic Models,Genetic Model,Model, Genetic
D009698 Nucleoproteins Proteins conjugated with nucleic acids. Nucleoprotein
D011995 Recombination, Genetic Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses. Genetic Recombination,Recombination,Genetic Recombinations,Recombinations,Recombinations, Genetic
D004251 DNA Transposable Elements Discrete segments of DNA which can excise and reintegrate to another site in the genome. Most are inactive, i.e., have not been found to exist outside the integrated state. DNA transposable elements include bacterial IS (insertion sequence) elements, Tn elements, the maize controlling elements Ac and Ds, Drosophila P, gypsy, and pogo elements, the human Tigger elements and the Tc and mariner elements which are found throughout the animal kingdom. DNA Insertion Elements,DNA Transposons,IS Elements,Insertion Sequence Elements,Tn Elements,Transposable Elements,Elements, Insertion Sequence,Sequence Elements, Insertion,DNA Insertion Element,DNA Transposable Element,DNA Transposon,Element, DNA Insertion,Element, DNA Transposable,Element, IS,Element, Insertion Sequence,Element, Tn,Element, Transposable,Elements, DNA Insertion,Elements, DNA Transposable,Elements, IS,Elements, Tn,Elements, Transposable,IS Element,Insertion Element, DNA,Insertion Elements, DNA,Insertion Sequence Element,Sequence Element, Insertion,Tn Element,Transposable Element,Transposable Element, DNA,Transposable Elements, DNA,Transposon, DNA,Transposons, DNA
D004254 DNA Nucleotidyltransferases Enzymes that catalyze the incorporation of deoxyribonucleotides into a chain of DNA. EC 2.7.7.-. Nucleotidyltransferases, DNA
D004269 DNA, Bacterial Deoxyribonucleic acid that makes up the genetic material of bacteria. Bacterial DNA
D006026 Glycoside Hydrolases Any member of the class of enzymes that catalyze the cleavage of the glycosidic linkage of glycosides and the addition of water to the resulting molecules. Endoglycosidase,Exoglycosidase,Glycohydrolase,Glycosidase,Glycosidases,Glycoside Hydrolase,Endoglycosidases,Exoglycosidases,Glycohydrolases,Hydrolase, Glycoside,Hydrolases, Glycoside
D001419 Bacteria One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive. Eubacteria
D015321 Gene Rearrangement The ordered rearrangement of gene regions by DNA recombination such as that which occurs normally during development. DNA Rearrangement,DNA Rearrangements,Gene Rearrangements,Rearrangement, DNA,Rearrangement, Gene,Rearrangements, DNA,Rearrangements, Gene
D043324 beta-Fructofuranosidase A glycoside hydrolase found primarily in PLANTS and YEASTS. It has specificity for beta-D-fructofuranosides such as SUCROSE. beta-D-Fructofuranosidase,Acid Invertase,Invertase,Saccharase,Sacrosidase,Sucraid,Sucrose 6-Phosphate Hydrolase,beta-Fructosidase,6-Phosphate Hydrolase, Sucrose,Hydrolase, Sucrose 6-Phosphate,Invertase, Acid,Sucrose 6 Phosphate Hydrolase,beta D Fructofuranosidase,beta Fructofuranosidase,beta Fructosidase

Related Publications

B Hallet, and D J Sherratt
April 2008, The EMBO journal,
B Hallet, and D J Sherratt
April 1996, Science (New York, N.Y.),
B Hallet, and D J Sherratt
January 1984, Cold Spring Harbor symposia on quantitative biology,
B Hallet, and D J Sherratt
January 2006, Annual review of biochemistry,
B Hallet, and D J Sherratt
November 2019, Nature,
B Hallet, and D J Sherratt
November 2019, Nature,
B Hallet, and D J Sherratt
December 1992, World journal of microbiology & biotechnology,
B Hallet, and D J Sherratt
February 1995, Nucleic acids research,
B Hallet, and D J Sherratt
October 1979, Molecular & general genetics : MGG,
Copied contents to your clipboard!