
When an invading bacterium or virus starts rummaging through the
contents of a cell nucleus, using proteins like tiny hands to rearrange
the host’s DNA strands, it can alter the host’s biological course. The
invading proteins use specific binding, firmly grabbing onto particular
sequences of DNA, to bend, kink and twist the DNA strands. The invaders
also use non-specific binding to grasp any part of a DNA strand, but
these seemingly random bonds are weak.
Emory University biophysicists have experimentally demonstrated, for the
fist time, how the nonspecific binding of a protein known as the lambda
repressor, or C1 protein, bends DNA and helps it close a loop that
switches off virulence. The researchers also captured the first
measurements of that compaction.
Their results, published in Physical Review E,
support the idea that nonspecific binding is not so random after all,...