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Site-specific recombination, also known as conservative site-specific recombination, is a type of genetic recombination in which DNA strand exchange takes place between segments possessing only a limited degree of sequence homology. Site-specific recombinases (SSRs) perform rearrangements of DNA segments by recognizing and binding to short DNA sequences (sites), at which they cleave the DNA backbone, exchange the two DNA helices involved and rejoin the DNA strands. While in some site-specific recombination systems just a recombinase enzyme and the recombination sites is enough to perform all these reactions, in other systems a number of accessory proteins and/or accessory sites are also needed. Multiple genome modification strategies, among these recombinase-mediated cassette exchange (RMCE), an advanced approach for the targeted introduction of transcription units into predetermined genomic ''loci'', rely on the capacities of SSRs. Site-specific recombination systems are highly specific, fast and efficient, even when faced with complex eukaryotic genomes. They are employed in a variety of cellular processes, including bacterial genome replication, differentiation and pathogenesis, and movement of mobile genetic elements (Nash 1996). For the same reasons, they present a potential basis for the development of genetic engineering tools. Recombination sites are typically between 30 and 200 nucleotides in length and consist of two motifs with a partial inverted-repeat symmetry, to which the recombinase binds, and which flank a central crossover sequence at which the recombination takes place. The pairs of sites between which the recombination occurs are usually identical, but there are exceptions (e.g. attP and attB of λ integrase, see lambda phage). ==Classification: tyrosine- ''vs.'' serine- recombinases== Based on amino acid sequence homology and mechanistic relatedness most site-specific recombinases are grouped into one of two families: the tyrosine recombinase family or the serine recombinase family. The names stem from the conserved nucleophilic amino acid residue that they use to attack the DNA and which becomes covalently linked to it during strand exchange. Early members of the serine recombinase family were known as resolvase/invertases, while the founding member of the tyrosine recombinases, lambda- integrase, using attP/B recognition sites) differs from the now well known enzymes such as Cre (from the P1 phage) and FLP (from yeast ''S. cerevisiae'') while famous serine recombinases include enzymes such as: gamma-delta resolvase (from the Tn''1000'' transposon), Tn3 resolvase (from the Tn3 transposon) and ''φ''C31 integrase (from the ''φ''C31 phage).'' Although the individual members of the two recombinase families can perform reactions with same practical outcomes, the two families are unrelated to each other, having different protein structures and reaction mechanisms. Unlike tyrosine recombinases, serine recombinases are highly modular as was first hinted by biochemical studies, and later shown by crystallographic structures. Knowledge of these protein structures could prove useful when attempting to reengineer recombinase proteins as tools for genetic manipulation. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Site-specific recombination」の詳細全文を読む スポンサード リンク
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