Association of the folded chromosome with the cell envelope of E. coli: characterization of the proteins at the DNA-membrane attachment site.
Gentle lysis of E. coli cells in the presence of a DNA counterion (either 1.0 M NaCl or 5 mM spermidine) permits the isolation of the folded intact bacterial chromosome associated with membrane fragments. Most of the proteins in these chromosomes are also found in purified membrane preparations, and they can be identified as belonging to either the inner or the outer bacterial membrane. Ultraviolet irradiation of the membrane-attached chromosomes causes the formation of a stable complex between two inner membrane proteins (molecular weight 80,000 and 56,000 daltons) and 5-bromodeoxyuridine (BrdU)-substituted DNA. The photochemical attachment of BrdU-substituted DNA to specific membrane proteins suggests that these proteins may be bound to the DNA in vivo. Such DNA-membrane-binding proteins may have a role in the attachment of the folded chromosome to the bacterial envelope.
D001426:Bacterial Proteins / Q000032:analysis* / Q000378:metabolism; D001665:Binding Sites; D002462:Cell Membrane / Q000032:analysis / Q000378:metabolism; D002876:Chromosomes, Bacterial / Q000378:metabolism* / Q000528:radiation effects; D004269:DNA, Bacterial / Q000378:metabolism*; D004586:Electrophoresis; D004926:Escherichia coli / Q000032:analysis / Q000648:ultrastructure*; D008970:Molecular Weight; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D004269:DNA, Bacterial