The phage Mu transpososome core: DNA requirements for assembly and function.

作者: H. Savilahti , P. A. Rice , K. Mizuuchi

DOI: 10.1002/J.1460-2075.1995.TB00170.X

关键词:

摘要: The two chemical steps of phage Mu transpositional recombination, donor DNA cleavage and strand transfer, take place within higher order protein-DNA complexes called transpososomes. At the core these is a tetramer MuA (the transposase), bound to ends genome. While transpososome assembly normally requires number cofactors, under certain conditions only short fragment are required. requirements for this process, as well stability activity ensuing complexes, were established. divalent cation required stable complex could be omitted if substrate was prenicked, flanking very or strands non-complementary. presence single nucleotide beyond genome end on non-cut critical stability. Donor additionally at least nucleotides cleaved. double helix destabilized, implying distortion near active site. Although Mg2+, transfer took in Ca2+ well, suggesting conformational difference site steps.

参考文章(48)
P. O. Brown, Integration of Retroviral DNA Current Topics in Microbiology and Immunology. ,vol. 157, pp. 19- 48 ,(1990) , 10.1007/978-3-642-75218-6_2
Soon-Young Namgoong, Makkuni Jayaram, Keetae Kim, Rasika M. Harshey, DNA-protein cooperativity in the assembly and stabilization of mu strand transfer complex: Relevance of dna phasing and att site cleavage Journal of Molecular Biology. ,vol. 238, pp. 514- 527 ,(1994) , 10.1006/JMBI.1994.1311
G Chaconas, G Gloor, J L Miller, Amplification and purification of the bacteriophage Mu encoded B transposition protein. Journal of Biological Chemistry. ,vol. 260, pp. 2662- 2669 ,(1985) , 10.1016/S0021-9258(18)89412-1