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Vol. 12, No. 24, pp. 3889-3899, December 15, 1998
Section on DNA Replication, Repair, and Mutagenesis, National
Institute of Child Health and Human Development, National Institutes of
Health, Bethesda, Maryland 20892-2725 USA
Most SOS mutagenesis in Escherichia coli is dependent on the
UmuD and UmuC proteins. Perhaps as a consequence, the activity of these
proteins is exquisitely regulated. The intracellular level of UmuD and
UmuC is normally quite low but increases dramatically in
lon
strains, suggesting that both proteins are substrates
of the Lon protease. We report here that the highly purified UmuD
protein is specifically degraded in vitro by Lon in an ATP-dependent
manner. To identify the regions of UmuD necessary for Lon-mediated
proteolysis, we performed `alanine-stretch' mutagenesis on
umuD and followed the stability of the mutant protein in vivo.
Such an approach allowed us to localize the site(s) within UmuD
responsible for Lon-mediated proteolysis. The primary signal is located
between residues 15 and 18 (FPLF), with an auxiliary site between
residues 26 and 29 (FPSP), of the amino terminus of UmuD. Transfer of
the amino terminus of UmuD (residues 1-40) to an otherwise stable protein imparts Lon-mediated proteolysis, thereby indicating that the
amino terminus of UmuD is sufficient for Lon recognition and the
ensuing degradation of the protein.
[Key Words: UmuD'; ATP-dependent protease; SOS mutagenesis; degradation signal]
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