Mfd functions in transcription-coupled repair to remove a stalled RNA polymerase that has encountered DNA damage and is unable to continue translocating.
Structural studies of E. coli Mfd by X-ray crystallography have revealed that this molecule is autoinhibited for UvrA-binding in its apo form due to a "clamp" interaction between the N-terminal UvrB-homology module and the C-terminal domain.
[6] In 2015, Merrikh Lab at University of Washington discovered that Mfd quickens the bacterial mutation process.
[2] This work researches ways to slow the rate of bacterial mutations and to block their evolution, in order to fight against antibiotic resistance.
[8] Animal immune systems try to kill bacteria in a number of ways, one being the release of nitrogen monoxide (NO).