High-affinity binding of hemimethylated oriC by Escherichia coli membranes is mediated by a multiprotein system that includes SeqA and a newly identified factor, SeqB

AUTOR(ES)

Shakibai, Nader

FONTE

The National Academy of Sciences

RESUMO

The binding of hemimethylated oriC to Escherichia coli membranes has been implicated in the prevention of premature reinitiation at newly replicated chromosomal origins in a reaction that involves the SeqA protein. We describe the resolution of the membrane-associated oriC-binding activity into two fractions, both of which are required for the high-affinity binding of hemimethylated oriC. The active component in one fraction is identified as SeqA. The active component of the second fraction is a previously undescribed protein factor, SeqB. The reconstituted system reproduced the salient characteristics of the membrane-associated binding activity, suggesting that the membrane-associated oriC-binding machinery of E. coli is likely to be a multiprotein system that includes the SeqA and SeqB proteins.

Documentos Relacionados

• Excess SeqA prolongs sequestration of oriC and delays nucleoid segregation and cell division
• Structural and biochemical analyses of hemimethylated DNA binding by the SeqA protein
• Fructose Uptake in Sinorhizobium meliloti Is Mediated by a High-Affinity ATP-Binding Cassette Transport System
• Reconstitution of high-affinity opioid agonist binding in brain membranes.
• Maltose and Maltodextrin Transport in the Thermoacidophilic Gram-Positive Bacterium Alicyclobacillus acidocaldarius Is Mediated by a High-Affinity Transport System That Includes a Maltose Binding Protein Tolerant to Low pH