Journal
NATURE MATERIALS
Volume 13, Issue 2, Pages 195-203Publisher
NATURE PORTFOLIO
DOI: 10.1038/nmat3858
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Funding
- DOE-BES [DE-FG02-06ER46314]
- NSF [DMR-1101900]
- NIH [R01-NS13560]
- US-Israel Binational Foundation [2009271]
- Israel Science Foundation [1372/13]
- Mexico-based science foundation CONACyT
- Mexico-based science foundation PIFI
- Mexico-based science foundation PROMEP
- Mexico-based science foundation UCMEXUS
- National Research Foundation of Korea [NRF 2011-355-C00037, NRF 2011-0031931, 2011-0030923, 2012R1A1A1011023, KAIST HRHRP N10110077]
- Ministry of Education, Science and Technology [R33-2008-000-10163-0]
- Stanford Synchrotron Radiation Laboratory (SSRL)
- DOE National Laboratory
- [NSF-DMR-1121053]
- National Research Foundation of Korea [2011-0031931, 2012R1A1A1011023] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1101900] Funding Source: National Science Foundation
- U.S. Department of Energy (DOE) [DE-FG02-06ER46314] Funding Source: U.S. Department of Energy (DOE)
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Bundles of taxol-stabilized microtubules (MTs)-hollow tubules comprised of assembled alpha beta-tubulin heterodimers-spontaneously assemble above a critical concentration of tetravalent spermine and are stable over long times at room temperature. Here we report that at concentrations of spermine several-fold higher the MT bundles (B-MT) quickly become unstable and undergo a shape transformation to bundles of inverted tubulin tubules (B-ITT), the outside surface of which corresponds to the inner surface of the B-MT tubules. Using transmission electron microscopy and synchrotron small-angle X-ray scattering, we quantitatively determined both the nature of the B-MT-to-B-ITT transformation pathway, which results from a spermine-triggered conformation switch from straight to curved in the constituent taxol-stabilized tubulin oligomers, and the structure of the B-ITT phase, which is formed of tubules of helical tubulin oligomers. Inverted tubulin tubules provide a platform for studies requiring exposure and availability of the inside, luminal surface of MTs to MT-targeted drugs and MT-associated proteins.
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