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Mycobacteriophage D29 integrase-mediated recombination: Specificity of mycobacteriophage integration

Peña, CEA and Stoner, J and Hatfull, GF (1998) Mycobacteriophage D29 integrase-mediated recombination: Specificity of mycobacteriophage integration. Gene, 225 (1-2). 143 - 151. ISSN 0378-1119

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Mycobacteriophage D29 is a lytic phage that infects both fast- and slow- growing species of the mycobacteria. D29 forms clear plaques on lawns of Mycobacterium smegmatis and Mycobacterium bovis bacille Calmette-Guerin (BCG) in which a very high proportion of infected cells are killed. However, genomic analysis of D29 demonstrates that it is a close relative of the temperate mycobacteriophage L5, and is presumably a non-temperate derivative of a temperate parent. The D29 genome encodes a putative integrase protein with a primary amino acid sequence similar to that of the L5 integrase; the corresponding int genes fall in colinear positions within the D29 and L5 genomes, immediately flanking and transcribed away from their associated attP sites. We show here that the D29 integrase is functional and catalyzes integrative recombination between the D29 attP site and the M. smegmatis attB site in vitro in an mIHF-dependent manner. D29 integrase also mediates recombination between the L5 attP site and attB DNA and, reciprocally, L5 integrase catalyzes recombination with D29 attP DNA. However, in both in- vitro and in-vivo assays, the D29-encoded integrase recombines the D29 attP more efficiently than the L5 attP, and vice versa, suggesting that each integration system has evolved a degree of specificity of attP recognition. We also present the sequences of the putative attP site and integrase protein of the cryptic prophage-like element φRv2, and compare them to those of mycobacteriophages L5 and D29.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Peña, CEA
Stoner, J
Hatfull, GFgfh@pitt.eduGFH
Date: 28 December 1998
Date Type: Publication
Journal or Publication Title: Gene
Volume: 225
Number: 1-2
Page Range: 143 - 151
DOI or Unique Handle: 10.1016/s0378-1119(98)00490-9
Schools and Programs: Dietrich School of Arts and Sciences > Biological Sciences
Refereed: Yes
ISSN: 0378-1119
MeSH Headings: Amino Acid Sequence; Base Sequence; Binding Sites; Cloning, Molecular; DNA, Viral--genetics; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Viral; Integrases--genetics; Integrases--isolation & purification; Integrases--metabolism; Molecular Sequence Data; Mycobacteriophages--enzymology; Mycobacteriophages--genetics; Mycobacterium--enzymology; Mycobacterium--genetics; Recombinant Fusion Proteins--genetics; Recombinant Fusion Proteins--isolation & purification; Recombinant Fusion Proteins--metabolism; Recombination, Genetic; Sequence Alignment; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Substrate Specificity; Virus Integration--genetics
PubMed ID: 9931474
Date Deposited: 12 Mar 2013 19:09
Last Modified: 14 Oct 2017 03:55


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