Title: Stepwise assembly of a relaxosome at the F plasmid origin of transfer. | Journal: The Journal of biological chemistry. 1995 Nov;270(47):28381-6 | Authors: Howard MT, Nelson WC, Matson SW. | Abstract: A central step in the transfer of genetic information during bacterial conjugation of the Escherichia coli F plasmid involves the formation of a protein-DNA complex, called the relaxosome, at the origin of transfer. During conjugation, the relaxosome introduces a site- and strand-specific nick from which the physical transfer of a single strand of DNA is initiated. At least two F-encoded proteins, TraIp (traI gene product) and TraYp (traY gene product), and one host-encoded protein, integration host factor, are involved in this process. In this report, we use DNase I protection and electron microscopic techniques to investigate the mechanism of relaxosome formation. Our results show that TraYp and integration host factor form a protein-DNA complex that facilitates the binding of TraIp to assemble a relaxosome capable of introducing a site- and strand-specific nick at the origin of transfer. This nick is identical to that observed during conjugation. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/7499340 |
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