An Arg/Ala-Rich Helix in the N-Terminal Region of M. tuberculosis FtsQ Anchors FtsZ to Membranes

Mycobacteria tuberculosis ( Mtb ) inflicts a quarter of the worldwide population. Most drugs for treating tuberculosis target cell growth and division. With rising drug resistance, it becomes ever more urgent to better understand Mtb cell division. This process begins with the formation of the Z-ring via polymerization of FtsZ and anchoring of the Z-ring to the inner membrane. Here we show that the transmembrane protein FtsQ is a membrane anchor of the Mtb Z-ring. More specifically, FtsQ uses an Arg/Ala-rich helix in its otherwise disordered N-terminal cytoplasmic region to bind with the GTPase domain of FtsZ. Binding of FtsQ to the GTPase domain of FtsZ also has enormous implications for drug binding and Z-ring formation including its curvature. ### Competing Interest Statement The authors have declared no competing interest.