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A flexible C ‐terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivo
Author(s) -
Buske P. J.,
Levin Petra Anne
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12272
Subject(s) - ftsz , linker , biology , cell division , cytoskeleton , cytoplasm , tubulin , conserved sequence , microbiology and biotechnology , cytokinesis , peptide sequence , biophysics , biochemistry , microtubule , cell , gene , computer science , operating system
Summary Assembly of the cytoskeletal protein FtsZ into a ring‐like structure is required for bacterial cell division. Structurally, FtsZ consists of four domains: the globular N ‐terminal core, a flexible linker, 8–9 conserved residues implicated in interactions with modulatory proteins, and a highly variable set of 4–10 residues at its very C terminus. Largely ignored and distinguished by lack of primary sequence conservation, the linker is presumed to be intrinsically disordered. Here we employ genetics, biochemistry and cytology to dissect the role of the linker in FtsZ function. Data from chimeric FtsZ s substituting the native linker with sequences from unrelated FtsZ s as well as a helical sequence from human beta‐catenin indicate that while variations in the primary sequence are well tolerated, an intrinsically disordered linker is essential for B acillus subtilis FtsZ assembly. Linker lengths ranging from 25 to 100 residues supported FtsZ assembly, but replacing the B . subtilis FtsZ linker with a 249‐residue linker from A grobacterium tumefaciens FtsZ interfered with cell division. Overall, our results support a model in which the linker acts as a flexible tether allowing FtsZ to associate with the membrane through a conserved C ‐terminal domain while simultaneously interacting with itself and modulatory proteins in the cytoplasm.