Disease relevance of Mup53

• The sequences around the recombination sites of Gin and Pin are also largely homologous; a consensus sequence is derived for the recombination sites of Gin and Pin, and of Hin in Salmonella typhimurium [1].
• The Gin DNA invertase of bacteriophage Mu carries out processive recombination in which multiple rounds of exchange follow synaptic complex formation [2].
• Inversion of the G segment in the DNA of Escherichia coli phage Mu depends on the Mu Gin protein and alters the host range of the phage [3].

High impact information on Mup53

• The extensive knotting by Gin has implications for the energetics of recombination and shows that the enhancer for recombination is required only at an early stage, and thus may normally operate in a hit-and-run fashion [2].
• However, the linking number changes also reveal that unlike wild-type Gin, mutant Gin can recombine through more than one synaptic complex and can relax DNA in the absence of synapsis [4].
• This expanded repertoire allows mutant Gin to mediate DNA rearrangements not performed by wild-type Gin [4].
• The Gin recombination system of phage Mu mediates inversion of the DNA sequence between two sites (gix) [4].
• We conclude that serine at position 9 is part of the catalytic domain of Gin [5].

Biological context of Mup53

• We have analyzed recombinant plasmids carrying one or both ends of Mu DNA for the expression of the Gin and Mom functions [6].
• The predicted amino acid sequences of PinD and three ORFs showed high homology to those of Gin and its flanking gene products [7].
• Each inverted repeat (IR) contains two binding sites for Gin which have to be arranged in a specific configuration to constitute a recombinogenic site [8].
• In addition to the sites within the IR, Gin binds with lower affinity to AT-rich sequences adjacent to the IR [8].
• In addition, we show that processive recombination by wild-type Gin is not restricted by the number of base-pairs separating the gix sites from each other and from the enhancer [9].

Anatomical context of Mup53

• The Gin recombinase of phage Mu can catalyse site-specific recombination in plant protoplasts [10].

Associations of Mup53 with chemical compounds

• The covalent complex is formed through linkage of Gin to the 5' DNA phosphate at the site of the break via a phosphoserine [5].
• In the protein-DNA complex, however, oxidation of cysteine residues still seems to be possible, indicating that the N-terminal parts of two Gin subunits are also in close proximity when bound to DNA [11].

Other interactions of Mup53

• The Gin protein and the presumptive Mom protein are not always detected in minicells, even though the plasmids being tested have the gin- and mom-containing segment of Mu DNA [6].

Analytical, diagnostic and therapeutic context of Mup53

• We investigated the recombination mechanism of a mutant Gin protein by analyzing the knotted products of processive recombination by electron microscopy and gel electrophoresis [9].

References