1 research outputs found
Single Asparagine to Arginine Mutation Allows PerR to Switch from PerR Box to Fur Box
Fur family proteins, ubiquitous in
prokaryotes, play a pivotal role in microbial survival and virulence
in most pathogens. Metalloregulators, such as Fur and PerR, regulate
the transcription of genes connected to iron homeostasis and response
to oxidative stress, respectively. In <i>Bacillus subtilis</i>, Fur and PerR bind with high affinity to DNA sequences differing
at only two nucleotides. In addition to these differences in the PerR
and Fur boxes, we identify in this study a residue located on the
DNA binding motif of the Fur protein that is critical to discrimination
between the two close DNA sequences. Interestingly, when this residue
is introduced into PerR, it lowers the affinity of PerR for its own
DNA target but confers to the protein the ability to interact strongly
with the Fur DNA binding sequence. The present data show how two closely
related proteins have distinct biological properties just by changing
a single residue