Abstract：
BACKGROUND:The Gifsy-I phage integrates into the Salmonella Typhimurium chromosome via an integrase mediated, site-specific recombination mechanism. Excision of the Gifsy-I phage requires three proteins, the Gifsy-I integrase (Int), the Gifsy-I excisionase (Xis) protein, and host encoded Integration Host Factor (IHF). The Gifsy-I xis gene encodes the 94-residue Gifsy-I excisionase protein that has a molecular weight of 11.2 kDa and a pI of 10.2. Electrophoretic Mobility Shift Assays (EMSA) suggested at least one region of the protein is responsible for protein-DNA interactions with a tripartite DNA binding site composed of three direct imperfect repeats. RESULTS:Here we have undertaken experiments to dissect and model the structural motifs of Gifsy-I Xis necessary for its observed DNA binding activity. Diethyl sulfate mutagenesis (DES) and mutagenic PCR techniques were used to generate Gifsy-I xis mutants. Mutant Xis proteins that lacked activity in vivo were purified and tested by EMSA for binding to the Gifsy-I Xis attP attachment site. Results from mutagenesis experiments and EMSA were compared to results of structural predictions and sequence analyses. CONCLUSION:Sequence comparisons revealed evidence for three distinct structural motifs in the Gifsy-I Xis protein. Multiple sequence alignments revealed unexpected homologies between the Gifsy-I Xis protein and two distinct subsets of polynucleotide binding proteins. Our data may suggest a role for the Gifsy-I Xis in the regulation of the Gifsy-I phage excision beyond that of DNA binding and possible interactions with the Gifsy-I Int protein.
journal_name
BMC Microbioljournal_title
BMC microbiologyauthors
Flanigan A,Gardner Jdoi
10.1186/1471-2180-8-199subject
Has Abstractpub_date
2008-11-17 00:00:00pages
199issn
1471-2180pii
1471-2180-8-199journal_volume
8pub_type
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