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

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.

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Zuckerman, David M.1, Author
Boucher, Lauren E.1, Author
Xie, Kefang1, Author
Engelhardt, Harald2, Author              
Bosch, Jürgen1, Author
Hoiczyk, Egbert1, Author
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1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: 3D STRUCTURE PREDICTION; BACTERIAL CYTOSKELETON; CELL-SHAPE; MOLECULAR-DYNAMICS; CRYSTAL-STRUCTURE; I-TASSER; HELIX; INTERMEDIATE; FILAMENT; TUBULIN
 Abstract: 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.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published online
 Pages: 25
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 Table of Contents: -
 Rev. Type: Peer
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Title: PLOS ONE
Source Genre: Journal
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Publ. Info: 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA : PUBLIC LIBRARY SCIENCE
Pages: - Volume / Issue: 10 (3) Sequence Number: e0121074 Start / End Page: - Identifier: ISSN: 1932-6203