Publications in Scientific Journals:

A. Muskotal, V. Szabó, B. Toth, M.D. Mihovilovic, F. Vonderviszt:
"Construction of a Xylanase A Variant Capable of Polymerization";
PLoS ONE, 6 (2011), 9 - 16.

English abstract:
The aim of our work is to furnish enzymes with polymerization ability by creating fusion constructs with the polymerizable
protein, flagellin, the main component of bacterial flagellar filaments. The D3 domain of flagellin, exposed on the surface of
flagellar filaments, is formed by the hypervariable central portion of the polypeptide chain. D3 is not essential for filament
formation. The concept in this project is to replace the D3 domain with suitable monomeric enzymes without adversely
affecting polymerization ability, and to assemble these chimeric flagellins into tubular nanostructures. To test the feasibility
of this approach, xylanase A (XynA) from B. subtilis was chosen as a model enzyme for insertion into the central part of
flagellin. With the help of genetic engineering, a fusion construct was created in which the D3 domain was replaced by
XynA. The flagellin-XynA chimera exhibited catalytic activity as well as polymerization ability. These results demonstrate that
polymerization ability can be introduced into various proteins, and building blocks for rationally designed assembly of
filamentous nanostructures can be created.

bioengineered flagella bacterial flagella filament formation terminal regions nanotubes display protein

"Official" electronic version of the publication (accessed through its Digital Object Identifier - DOI)

Electronic version of the publication:

Created from the Publication Database of the Vienna University of Technology.