The speed of FtsZ treadmilling is tightly regulated by membrane binding

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review


  • Daniela A. García-Soriano
  • Tamara Heermann, Max Planck Institute of Biochemistry
  • ,
  • Ana Raso, Max Planck Institute of Biochemistry, CSIC - Biological Research Center
  • ,
  • Germán Rivas, CSIC - Biological Research Center
  • ,
  • Petra Schwille, Max Planck Institute of Biochemistry

As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted protein can produce these dynamics. Here, we dissect the roles of membrane binding, GTPase activity, and the unstructured C-terminal linker on the treadmilling of a chimera FtsZ protein through in vitro reconstitution of different FtsZ-YFP-mts variants on supported membranes. In summary, our results suggest substantial robustness of dynamic vortex formation, where only significant mutations, resulting in abolished membrane binding or compromised lateral interactions, are detrimental for the generation of treadmilling rings. In addition to GTPase activity, which directly affects treadmilling dynamics, we found a striking correlation of membrane binding with treadmilling speed as a result of changing the MTS on our chimera proteins. This discovery leads to the hypothesis that the in vivo existence of two alternative tether proteins for FtsZ could be a mechanism for controlling FtsZ treadmilling.

TidsskriftScientific Reports
StatusUdgivet - jun. 2020

Se relationer på Aarhus Universitet Citationsformater

ID: 191591096