DNA-protein interaction at the replication origins of plasmid chromosomes.
DNA-protein interaction at the replication origins of plasmid chromosomes.
复制标题
质粒染色体复制起点处的 DNA-蛋白质相互作用。
DOI:
10.1007/978-1-4613-2447-8_29
复制
发表时间:
1985
期刊:
影响因子:
--
通讯作者:
Gray,J
中科院分区:
文献类型:
--
作者:
Bastia,D;Vocke,C;Germino,J;Gray,J
Novel techniques have been developed to purify replication initiator proteins of the plasmids R6K and pSC101. The techniques consist of tagging the initiator cistrons at the C-terminus with β-galactosidase-encoding DNA ofEscherichiacoliin the correct translational phase. The hybrid proteins are then rapidly purified by adsorption to and elution from a β-galactosidase-specific affinity column. Two procedures have been devised to isolate the nonfused initiator proteins using the fused protein as a handle. The first procedure, called subunit association chromatography, exploits the association of a monomer of nontagged protein with that of β-galactosidase-tagged protein in isolating both types of proteins by β-galactosidase specific affinity column chromatography. The second procedure involves the fusion of the initiator protein to β-galactosidase via a specific linker DNA. The linker DNA encodes a protein which is readily and specifically hydrolyzed by a sequence specific protease, thus releasing the initiator protein from β-galactosidase. Using purified or partially purified initiator protein, we have demonstrated that the R6K encoded initiator protein (Pi protein) binds to a consensus 22 bp sequence at 2 regions of the plasmid chromosome. The pSC101-encoded initiator protein binds to sequences at or near the plasmid replication origin. At low concentrations the protein binds to a nucleation site and upon raising the concentrations of the protein binding is promoted at 4 adjacent sequences that have partial homologies with the nucleation sequence. Deletion of the binding site leads to a nonfunctional replication origin.