抄録
MazF is an mRNA interferase, which cleaves mRNAs in a sequence-specific manner, resulting in cellular growth arrest. During normal growth conditions, the MazF toxin is inactivated through binding to its cognate antitoxin, MazE. How MazF specifically recognizes its mRNA target and carries out cleavage and how the formation of the MazE-MazF complex inactivates MazF remain unclear. We determined crystal structures of MazF in complex with mRNA substrate and antitoxin MazE in Bacillus subtilis. In this review, I present the mechanism of the sequence-specific RNA recognition of MazF and the neutralization of MazF activity by MazE antitoxin.
