An intrinsically disordered linker plays a critical role in bacterial cell division.

ABSTRACT: In bacteria, animals, fungi, and many single celled eukaryotes, division is initiated by the formation of a ring of cytoskeletal protein at the nascent division site. In bacteria, the tubulin-like GTPase FtsZ serves as the foundation for the cytokinetic ring. A conserved feature of FtsZ is an intrinsically disordered peptide known as the C-terminal linker. Chimeric experiments suggest the linker acts as a flexible boom allowing FtsZ to associate with the membrane through a conserved C-terminal domain and also modulates interactions both between FtsZ subunits and between FtsZ and modulatory proteins in the cytoplasm.

SUBMITTER: Buske PJ 

PROVIDER: S-EPMC4339304 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature