Structural highlights
Function
GIN_BPMU Performs inversion of a viral 3 kp segment (G-segment) that encodes two alternate pairs of tail fiber proteins thereby modifying the host specificity of the virus. Binds as a dimer to the viral gix sites which are 34-bp palindromic sequences that flank the invertible G-segment. Catalyzes site-specific recombination in the presence of the host factor Fis. Gin dimers bound to each of the gix sites and host factor Fis bound to the enhancer come together to form the synaptic complex. Each Gin monomer introduces a nick and becomes covalently attached to the 5'-phosphate of the DNA, resulting in double-stranded staggered breaks at both recombination sites. A 180 degrees rotation of one of the two Gin dimers followed by religation of the DNA leads to the inversion of the G-segment (G+ or G- orientation).[1] [2] [3] [4]
See Also
References
- ↑ Ritacco CJ, Kamtekar S, Wang J, Steitz TA. Crystal structure of an intermediate of rotating dimers within the synaptic tetramer of the G-segment invertase. Nucleic Acids Res. 2013 Feb 1;41(4):2673-82. doi: 10.1093/nar/gks1303. Epub 2012 , Dec 28. PMID:23275567 doi:10.1093/nar/gks1303
- ↑ Klippel A, Cloppenborg K, Kahmann R. Isolation and characterization of unusual gin mutants. EMBO J. 1988 Dec 1;7(12):3983-9. doi: 10.1002/j.1460-2075.1988.tb03286.x. PMID:2974801 doi:https://dx.doi.org/10.1002/j.1460-2075.1988.tb03286.x
- ↑ Kahmann R, Rudt F, Koch C, Mertens G. G inversion in bacteriophage Mu DNA is stimulated by a site within the invertase gene and a host factor. Cell. 1985 Jul;41(3):771-80. doi: 10.1016/s0092-8674(85)80058-1. PMID:3159478 doi:https://dx.doi.org/10.1016/s0092-8674(85)80058-1
- ↑ Plasterk RH, Kanaar R, van de Putte P. A genetic switch in vitro: DNA inversion by Gin protein of phage Mu. Proc Natl Acad Sci U S A. 1984 May;81(9):2689-92. doi: 10.1073/pnas.81.9.2689. PMID:6232613 doi:https://dx.doi.org/10.1073/pnas.81.9.2689
