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The Bactofilin Cytoskeleton Protein BacM of Myxococcus xanthus Forms an Extended beta-Sheet Structure Likely Mediated by Hydrophobic Interactions

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Engelhardt,  Harald
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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journal.pone.0121074.pdf
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Zitation

Zuckerman, D. M., Boucher, L. E., Xie, K., Engelhardt, H., Bosch, J., & Hoiczyk, E. (2015). The Bactofilin Cytoskeleton Protein BacM of Myxococcus xanthus Forms an Extended beta-Sheet Structure Likely Mediated by Hydrophobic Interactions. PLOS ONE, 10(3): e0121074. doi:10.1371/journal.pone.0121074.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0027-A824-B
Zusammenfassung
Bactofilins are novel cytoskeleton proteins that are widespread in Gram-negative bacteria. Myxococcus xanthus, an important predatory soil bacterium, possesses four bactofilins of which one, BacM (Mxan_7475) plays an important role in cell shape maintenance. Electron and fluorescence light microscopy, as well as studies using over-expressed, purified BacM, indicate that this protein polymerizes in vivo and in vitro into similar to 3 nm wide filaments that further associate into higher ordered fibers of about 10 nm. Here we use a multipronged approach combining secondary structure determination, molecular modeling, biochemistry, and genetics to identify and characterize critical molecular elements that enable BacM to polymerize. Our results indicate that the bactofilin-determining domain DUF583 folds into an extended beta-sheet structure, and we hypothesize a left-handed beta-helix with polymerization into 3 nm filaments primarily via patches of hydrophobic amino acid residues. These patches form the interface allowing head-to-tail polymerization during filament formation. Biochemical analyses of these processes show that folding and polymerization occur across a wide variety of conditions and even in the presence of chaotropic agents such as one molar urea. Together, these data suggest that bactofilins are comprised of a structure unique to cytoskeleton proteins, which enables robust polymerization.