The transmembrane domains of the bacterial cell division proteins FtsB and FtsL form a stable high-order oligomer.

ABSTRACT: FtsB and FtsL are two essential integral membrane proteins of the bacterial division complex or "divisome", both characterized by a single transmembrane helix and a juxtamembrane coiled coil domain. The two domains are important for the association of FtsB and FtsL, a key event for their recruitment to the divisome, which in turn allows the recruitment of the late divisomal components to the Z-ring and subsequent completion of the division process. Here we present a biophysical analysis performed in vitro that shows that the transmembrane domains of FtsB and FtsL associate strongly in isolation. Using Förster resonance energy transfer, we have measured the oligomerization of fluorophore-labeled transmembrane domains of FtsB and FtsL in both detergent and lipid. The data indicate that the t

SUBMITTER: Khadria AS 

PROVIDER: S-EPMC4133089 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature