Proteolytic inactivation of key regulatory proteins is essential in eu
karyotic cell-cycle control. We have identified a protease in the euba
cterium Caulobacter crescentus that is indispensable for viability and
cell-cycle progression, indicating that proteolysis is also involved
in controlling the bacterial cell cycle, Mutants of Caulobacter that l
ack the ATP-dependent serine protease ClpXP are arrested in the cell c
ycle before the initiation of chromosome replication and are blocked i
n the cell division process. ClpXP is composed of two types of polypep
tides, the ClpX ATPase and the ClpP peptidase, Site-directed mutagenes
is of the catalytically active serine residue of ClpP confirmed that t
he proteolytic activity of ClpXP is essential, Analysts of mutants lac
king ClpX or ClpP revealed that both proteins are required in vivo for
the cell-cycle-dependent degradation of the regulatory protein CtrA,
CtrA is a member of the response regulator family of two-component sig
nal transduction systems and controls multiple cell-cycle processes in
Caulobacter, In particular, CtrA negatively controls DNA replication
and our findings suggest that specific degradation of the CtrA protein
by the ClpXP protease contributes to G(1)-to-S transition in this org
anism.