We have undertaken a site directed mutational analysis of two of the p
reserved regions in the amino acid sequence of Dam methylase in order
to characterize their role. Mutations in region IV (sequence DPPY) abo
lish catalytic activity and greatly affect AdoMet crosslinking. Mutant
s in region III display a lowered specific activity with an unchanged
AdoMet crosslinking capacity. We have also made a series of deletions
both at the N and C terminal parts of the protein, which have been fou
nd to provide inactive enzyme. We discuss the significance of these re
sults for the understanding of the functional properties of the enzyme
.