A novel role for cAMP in the control of the activity of the E. coli chromosome replication initiator protein, DnaA.
DnaA protein interacts with cAMP with a KD of 1 microM. This interaction stimulates DnaA protein binding to the chromosome replication origin (oriC) and the mioC promoter region, protects DnaA protein from thermal inactivation, releases ADP but not ATP bound to DnaA protein, and restores normal DNA replication activity and ATPase activity in inactive ADP-DnaA protein preparations. A model is proposed in which cellular cAMP levels govern the replication activity of DnaA protein by promoting the recycling of the inactive ADP-DnaA protein form into the active ATP form.
Hughes
P
P
Institut Jacques Monod, Université Paris VII, France.
Landoulsi
A
A
Kohiyama
M
M
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000032:analysis; D001426:Bacterial Proteins / Q000502:physiology*; D000242:Cyclic AMP / Q000502:physiology*; D004261:DNA Replication; D004269:DNA, Bacterial / Q000096:biosynthesis; D004926:Escherichia coli / Q000235:genetics*; D006358:Hot Temperature; D011485:Protein Binding
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D000242:Cyclic AMP