Flagellin has the ability to polymerize into long filaments under appropriate conditions. Our work aims at the construction of flagellin-based fusion proteins which possess polymerization ability and preserve the functional properties of the fusion partner as well. The hypervariable D3 domain of Salmonella flagellin, containing residues 190– 283, is a good target for genetic engineering studies since it can be extensively modified or removed without disturbing the self-assembling ability. In this work a fusion construct of flagellin and the superfolder mutant of the green fluorescent protein were created by replacing D3 with superfolder green fluorescent protein (GFP). The obtained GFP variant was capable of forming stable, highly fluorescent filamentous assemblies. Our results imply that other proteins (enzymes, binding proteins, etc.) can also be furnished by polymerization ability in a similar way. This approach paves the way for the construction of multifunctional tubular nanostructures.