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-Structure paper
Title | Four-stranded mini microtubules formed by BtubAB show dynamic instability. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 114, Issue 29, Page E5950-E5958, Year 2017 |
Publish date | Jul 18, 2017 |
Authors | Xian Deng / Gero Fink / Tanmay A M Bharat / Shaoda He / Danguole Kureisaite-Ciziene / Jan Löwe / |
PubMed Abstract | Microtubules, the dynamic, yet stiff hollow tubes built from αβ-tubulin protein heterodimers, are thought to be present only in eukaryotic cells. Here, we report a 3.6-Å helical reconstruction ...Microtubules, the dynamic, yet stiff hollow tubes built from αβ-tubulin protein heterodimers, are thought to be present only in eukaryotic cells. Here, we report a 3.6-Å helical reconstruction electron cryomicroscopy structure of four-stranded mini microtubules formed by bacterial tubulin-like 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 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. |
External links | Proc Natl Acad Sci U S A / PubMed:28673988 / PubMed Central |
Methods | EM (helical sym.) / X-ray diffraction |
Resolution | 2.5 - 3.6 Å |
Structure data | PDB-5o01: |
Chemicals | ChemComp-HOH: ChemComp-GDP: |
Source |
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Keywords | MOTOR PROTEIN / bacterial cytoskeleton / mini microtubules / STRUCTURAL PROTEIN / microtubules |