Structural highlights
Publication Abstract from PubMedMicrotubules, the dynamic, yet stiff hollow tubes built from alphabeta-tubulin protein heterodimers, are thought to be present only in eukaryotic cells. Here, we report a 3.6-A helical reconstruction electron cryomicroscopy structure of four-stranded mini microtubules formed by bacterial tubulin-like Prosthecobacter dejongeii BtubAB proteins. Despite their much smaller diameter, mini microtubules share many key structural features with eukaryotic microtubules, such as an M-loop, alternating subunits, and a seam that breaks overall helical symmetry. Using in vitro total internal reflection fluorescence microscopy, we show that bacterial mini microtubules treadmill and display dynamic instability, another hallmark of eukaryotic microtubules. The third protein in the btub gene cluster, BtubC, previously known as "bacterial kinesin light chain," binds along protofilaments every 8 nm, inhibits BtubAB mini microtubule catastrophe, and increases rescue. Our work reveals that some bacteria contain regulated and dynamic cytomotive microtubule systems that were once thought to be only useful in much larger and sophisticated eukaryotic cells. Four-stranded mini microtubules formed by Prosthecobacter BtubAB show dynamic instability.,Deng X, Fink G, Bharat TAM, He S, Kureisaite-Ciziene D, Lowe J Proc Natl Acad Sci U S A. 2017 Jul 18;114(29):E5950-E5958. doi:, 10.1073/pnas.1705062114. Epub 2017 Jul 3. PMID:28673988[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||
This page was last modified 16:10, 20 October 2017.