Characterization of bacterial cell membrane attachment sites of plasmid R6K.
In vitro binding studies revealed that plasmid R6K could attach to both inner and outer membrane fractions of its host cell, Escherichia coli. Derivatives of R6K carrying one or two of its three origins of replication could not bind stably to the same membrane fractions in the presence of salt. However, the derivative, pRK35, carrying the intact three origins of replication could bind stably to membrane fractions from its host in the presence or absence of salt. These observations suggest that the three origins of DNA replication must be contiguous for stable binding of the plasmid to the cell membrane. The results of binding experiments showed that plasmid R6K bound competitively with pRK35 as well as the heterologous plasmid, pl524.
Jemilohun
P F
PF
Department of Biology, Jackson State University, Mississippi 39217, USA.
Clark
C W
CW
Archibold
E R
ER
D001667:Binding, Competitive; D002462:Cell Membrane / Q000378:metabolism; D004274:DNA, Recombinant / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D010957:Plasmids; D018741:Replication Origin; D012486:Salmonella typhimurium / Q000378:metabolism
D004274:DNA, Recombinant