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Figure 3.
Conserved mutation of Val-148 in RseA allowed retention of
Site-2 cleavage. (A) Mutation of Val-148 to conserved, but not
dissimilar or charged, amino acids in RseA allowed retention of
Site-2 cleavage. DegS and OMP peptide were added together to the
reactions where DegS is indicated. (B) Classification of three
categories of amino acids at position 148 of RseA based on their
impact on Site-1 and Site-2 cleavages. Mutation of Val-148 to
any of the five amino acids—Glu, Asp, Gly, Pro, and
Phe—crippled Site-1 cleavage of RseA by DegS. Among the
mutations that allow Site-1 cleavage, six (mutation of Val-148
to Lys, His, Arg, Ser, Gln, and Tyr) do not allow Site-2
cleavage.
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