title: Role of the N-terminal domain of phiC31 integrase in attB-attP synapsis.
abstract: PhiC31 integrase is a serine recombinase containing an N-terminal domain (NTD) that provides catalytic activity and a large C-terminal domain that controls which pair of DNA substrates is able to synapse. We show here that substitutions in amino acid V129 in the NTD can lead to defects in synapsis and DNA cleavage, indicating that the NTD also has an important role in synapsis.
authors.affiliation: Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.
authors.forename: Paul A
authors.initials: PA
authors.lastname: Rowley
authors.forename: Margaret C M
authors.initials: MC
authors.lastname: Smith
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics; D001287:Attachment Sites, Microbiological; D001435:Bacteriophages / Q000502:physiology*; D004269:DNA, Bacterial / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism; D019426:Integrases / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011995:Recombination, Genetic; D016415:Sequence Alignment; D013302:Streptomyces / Q000821:virology*; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D004269:DNA, Bacterial; D004279:DNA, Viral; D014764:Viral Proteins; D019426:Integrases