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Septins are guanine nucleotide-binding proteins that are conserved from fungito humans. Septins assemble into heterooligomeric complexes and higher-orderstructures with key roles in various cellular functions including cellmigration and division. The mechanisms by which septins assemble and interactwith other cytoskeletal elements like actin remain elusive. A powerful approachto address this question is by cell-free reconstitution of pu- rifiedcytoskeletal proteins combined with fluorescence microscopy. Here, we describeprocedures for the purification of recombinant Drosophila and human septinhexamers from Escherichia coli and reconstitution of actin-septin coassembly.These procedures can be used to compare assembly of Drosophila and humanseptins and their coassembly with the actin cytoskeleton by total internalreflection fluorescence microscopy.

Purification of recombinant human and Drosophila septin hexamers for TIRF assays of actin-septin filament assembly