Structural diversity and dynamics of microtubules and polymorphic tubulin assemblies

Unger, Eberhard; Böhm, Konrad J.; Vater, W

doi:10.1016/0892-0354(90)90007-f

Cited by 92 publications

(61 citation statements)

References 213 publications

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“…Each individual tubulin heterodimer is 8 nm in length and interacts laterally and longitudinally to form protofilaments and then MTs . In addition to microtubules, whose protofilament numbers vary betweens 8 and 17, under special experimental conditions tubulin can also give rise to polymorphic assemblies that include sheets, macrotubes, ribbons and several additional, exotic structures (Unger, 1990).…”

Section: Introductionmentioning

confidence: 99%

The evolution of the structure of tubulin and its potential consequences for the role and function of microtubules in cells and embryos

et al. 2006

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This paper discusses the results of homology modeling and resulting calculation of key structural and physical properties for close to 300 tubulin sequences, including α α α α α, β β β β β, γ γ γ γ γ, δ δ δ δ δ and ε ε ε ε ε -tubulins. The basis for our calculations was the structure of the tubulin dimer In addition to the general structural trends between tubulin isoforms, we have observed that the carboxy-termini of α α α α α and β β β β β-tubulin exists in at least two stable configurations, either projecting away from the tubulin (or microtubule) surface, or collapsed onto the surface. In the latter case, the carboxy-termini form a lattice distinctly different from that of the well-known A and B lattices formed by the tubulin subunits. However, this C-terminal lattice is indistinguishable from the lattice formed when the microtubule-associated protein tau binds to the microtubule surface. Finally, we have discussed how tubulin sequence diversity arose in evolution giving rise to its particular phylogeny and how it may be used in cell-and tissue-specific expression including embryonal development.

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Section: Introductionmentioning

confidence: 99%

The evolution of the structure of tubulin and its potential consequences for the role and function of microtubules in cells and embryos

et al. 2006

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“…Further symmetry breaking would lead to different 3D structures such as double-wall , ring-shaped, sheet-like, C-shaped and S-shaped ribbons, and hoop structures as seen during tubulin polymerization experiments [21][22][23].…”

Section: The Dynamical Equationsmentioning

confidence: 99%

“…This enables us to derive a nonlinear system particular, our model explains the continuum symmetry breaking of an isotropic pool of tubulin dimers that leads to formation of experimentally observed 3D structures such as ring-shaped or filaments [21][22][23]. We believe that this treatment is necessary to address the fundamental issues about the observed dynamical behavior of MTs.…”

Section: Introductionmentioning

confidence: 99%

A first principle (3+1)-dimensional model for microtubule polymerization

Rezania¹,

Tuszyński²

2008

Physics Letters A

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In this paper we propose a microscopic model to study the polymerization of microtubules (MTs). Starting from fundamental reactions during MT's assembly and disassembly processes, we systematically derive a nonlinear system of equations that determines the dynamics of microtubules in 3D. We found that the dynamics of a MT is mathematically expressed via a cubic-quintic nonlinear Schrödinger (NLS) equation. Interestingly, the generic 3D solution of the NLS equation exhibits linear growing and shortening in time as well as temporal fluctuations about a mean value which are qualitatively similar to the dynamic instability of MTs observed experimentally. By solving equations numerically, we have found spatio-temporal patterns consistent with experimental observations.

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“…Tubulin molecules exhibit chemically active surfaces with defined patterns of amino acid side chains, which provide a wide variety of active sites for derivatization, especially for nucleation, organization, and binding metal particles. Tubulin is able to self-assemble into a wide variety of polymorphs: tubules, sheets, ribbons, spirals, and rings, [14] all consisting of differently arranged protofilaments with a strict alternation of a-and b-tubulin monomers. In the presence of Ca 2+ ions, tubulin assembles in vitro into rings and spirals instead of MTs.…”

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confidence: 99%

“…1a), which consist of a protofilament with an inner side that corresponds to the outer side of protofilaments in MTs. [14] The heights of tubulin structures fixed by 1 % GA have been measured by scanning force microscopy (SFM) and predominantly range between 8-15 nm (the mean height is 10.9 ± 1.4 nm), which suggests that about two to four spirals may be packed on top of each other in the axial direction. Figure 1b displays an SFM image of several ring-like tubulin assemblies and a typical height profile.…”

mentioning

confidence: 99%

Assembly of Nanoparticle Ring Structures Based on Protein Templates

Behrens¹,

Habicht²,

Wagner³

et al. 2006

Advanced Materials

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Commercial requirements for miniaturized microelectronic devices provide strong motivation for exploring the synthesis of nanoscale systems using bottom-up techniques. The manipulation of charges at the single-electron level in regularly arranged nanoparticles can be utilized to create devices, such as switches, transistors, and digital electronic circuits.[1] An interesting feature of nanoscale ring systems is the AharonovBohm effect: interference phenomena of electron wave functions observed for electrons in ring systems. [2] Up to now, the bottom-up wet-chemical synthesis of inorganic materials has provided a tool for the fabrication of a range of nanostructures, from particles to one-dimensional (1D) structures, [3,4] but these chemical techniques offer little control over the deposition of metals or metal particles as nanometer-sized ring structures, even though interesting properties are expected for such structures. The growth of inorganic materials on biomolecular templates as well as biomolecule-directed assembly of inorganic building blocks are other promising strategies for fabricating complex functional nanostructures, such as wires and ring structures. [5][6][7][8][9] For example, wild-type and genetically engineered viruses have been used to template quasi-1D magnetic [10] and semiconducting nanowires [11] as well as ring structures of Au nanoparticles. [12] In this communication, we address the template-directed deposition of metals on ring-shaped tubulin assemblies for synthesizing metal ring nanostructures. The controlled deposition of metals on polymorphic tubulin structures, as already shown for microtubules (MTs), [13] have great potential for use in future electronic components, for example, AharonovBohm rings to be used in nanoscale circuits. Tubulin is a protein that forms a,b-heterodimers that are about 8 nm in length with diameters ranging from 4 to 5 nm. Tubulin molecules exhibit chemically active surfaces with defined patterns of amino acid side chains, which provide a wide variety of active sites for derivatization, especially for nucleation, organization, and binding metal particles. Tubulin is able to self-assemble into a wide variety of polymorphs: tubules, sheets, ribbons, spirals, and rings, [14] all consisting of differently arranged protofilaments with a strict alternation of a-and b-tubulin monomers. In the presence of Ca 2+ ions, tubulin assembles in vitro into rings and spirals instead of MTs. [15,16] Unlike tubulin rings, MTs have been used as templates to generate metal nanoparticles and nanowires, [13,[17][18][19] for the mineralization of iron oxide, [20] as well as for the kinesinbased transport of synthetic cargo [21][22][23] and CdSe quantum dots.[24]We have investigated ring and spiral formation by transmission electron microscopy (TEM, Fig. 1a). TEM images of tubulin rings fixed by 0.1 % glutaric dialdehyde (GA) and negatively stained by uranyl acetate reveal an outer and inner diameter of 56.4 ± 4.0 nm and 27.1 ± 3.8 nm, respectively, corresponding to a wall thickne...

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Structural diversity and dynamics of microtubules and polymorphic tubulin assemblies

Cited by 92 publications

References 213 publications

The evolution of the structure of tubulin and its potential consequences for the role and function of microtubules in cells and embryos

The evolution of the structure of tubulin and its potential consequences for the role and function of microtubules in cells and embryos

A first principle (3+1)-dimensional model for microtubule polymerization

Assembly of Nanoparticle Ring Structures Based on Protein Templates

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