Document Detail


Phage integrases: biology and applications.
MedLine Citation:
PMID:  14687564     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Phage integrases are enzymes that mediate unidirectional site-specific recombination between two DNA recognition sequences, the phage attachment site, attP, and the bacterial attachment site, attB. Integrases may be grouped into two major families, the tyrosine recombinases and the serine recombinases, based on their mode of catalysis. Tyrosine family integrases, such as lambda integrase, utilize a catalytic tyrosine to mediate strand cleavage, tend to recognize longer attP sequences, and require other proteins encoded by the phage or the host bacteria. Phage integrases from the serine family are larger, use a catalytic serine for strand cleavage, recognize shorter attP sequences, and do not require host cofactors. Phage integrases mediate efficient site-specific recombination between two different sequences that are relatively short, yet long enough to be specific on a genomic scale. These properties give phage integrases growing importance for the genetic manipulation of living eukaryotic cells, especially those with large genomes such as mammals and most plants, for which there are few tools for precise manipulation of the genome. Integrases of the serine family have been shown to work efficiently in mammalian cells, mediating efficient integration at introduced att sites or native sequences that have partial identity to att sites. This reaction has applications in areas such as gene therapy, construction of transgenic organisms, and manipulation of cell lines. Directed evolution can be used to increase further the affinity of an integrase for a particular native sequence, opening up additional applications for genomic modification.
Authors:
Amy C Groth; Michele P Calos
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Journal of molecular biology     Volume:  335     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2004 Jan 
Date Detail:
Created Date:  2003-12-22     Completed Date:  2004-02-03     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  667-78     Citation Subset:  IM    
Affiliation:
Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305-5120, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Bacteriophages / enzymology*
Binding Sites
Genetic Engineering*
Humans
Integrases / chemistry,  classification,  genetics*
Protein Conformation
Substrate Specificity
Grant Support
ID/Acronym/Agency:
DK58187/DK/NIDDK NIH HHS; HL68112/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
EC 2.7.7.-/Integrases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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