Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2202613 | Seminars in Cell & Developmental Biology | 2015 | 8 Pages |
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.
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Authors
P.J. Buske, Anuradha Mittal, Rohit V. Pappu, Petra Anne Levin,