Crystal structure of tubulin folding cofactor A from <i>Arabidopsis thaliana</i> and its β‐tubulin binding characterization

Lu, Lu; Nan, Jie; Mi, Wei; Li, Lanfen; Wei, Chunhong; Li, Yang

doi:10.1016/j.febslet.2010.07.017

Cited by 7 publications

(12 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, ROS can act to oxidatively modify tubulin thus preventing post‐translational modifications that control the binding of microtubule‐associated proteins (Sedbrook 2004; Hammond, Cai & Verhey 2008; Cai 2010). Alternatively, ROS can damage tubulin monomers so that they cannot interact with cofactors involved in proper tubulin folding (Sedbrook 2004; Beghin, Galmarini & Dumontet 2007; Lu et al . 2010).…”

Section: Discussionmentioning

confidence: 99%

Ultra‐small TiO₂ nanoparticles disrupt microtubular networks in Arabidopsis thaliana

Wang

Kurepa

Smalle

2011

Plant Cell & Environment

115

View full text Add to dashboard Cite

In spite of the mounting concerns, current understanding of the extent and mechanisms of phytotoxicity of manufactured nanomaterials remains limited. Here we show that in Arabidopsis thaliana, ultra-small anatase TiO2 nanoparticles cause reorganization and elimination of microtubules followed by the accelerated and 26S proteasome-dependent degradation of tubulin monomers. Similar to other microtubule-disrupting agents, TiO2 nanoparticles induce isotropic growth of root cells. Because microtubules are essential for the normal function of all eukaryotic cells, these results reveal a potentially important consequence of environmental pollution by this widely used nanomaterial.

show abstract

Section: Discussionmentioning

confidence: 99%

Ultra‐small TiO₂ nanoparticles disrupt microtubular networks in Arabidopsis thaliana

Wang

Kurepa

Smalle

2011

Plant Cell & Environment

115

View full text Add to dashboard Cite

show abstract

“…Peptide mapping analysis and competition experiments with peptides showed that TBCA interacts with β-tubulin via the three α-helical regions, but not with the rod-end loops. The crystal structure of Arabidopsis TBCA combined with β-tubulin binding analysis confirmed the monomeric three-helix bundle structure and β-tubulin interaction with the α-helical regions [22]. The main interaction occurs with the middle kinked α2 helix, at the convex face of the rod.…”

Section: Tubulin-specific Folding Cofactorsmentioning

confidence: 85%

Faithful chaperones

Szołajska

Chroboczek

2011

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

This review describes the properties of some rare eukaryotic chaperones that each assist in the folding of only one target protein. In particular, we describe (1) the tubulin cofactors, (2) p47, which assists in the folding of collagen, (3) α-hemoglobin stabilizing protein (AHSP), (4) the adenovirus L4-100 K protein, which is a chaperone of the major structural viral protein, hexon, and (5) HYPK, the huntingtin-interacting protein. These various-sized proteins (102–1,190 amino acids long) are all involved in the folding of oligomeric polypeptides but are otherwise functionally unique, as they each assist only one particular client. This raises a question regarding the biosynthetic cost of the high-level production of such chaperones. As the clients of faithful chaperones are all abundant proteins that are essential cellular or viral components, it is conceivable that this necessary metabolic expenditure withstood evolutionary pressure to minimize biosynthetic costs. Nevertheless, the complexity of the folding pathways in which these chaperones are involved results in error-prone processes. Several human disorders associated with these chaperones are discussed.

show abstract

“…The crystal structure of the TBCA yeast homolog in S. cerevisiae , Rbl2p, shares a similar overall fold but crystallizes as an inverted dimer with the two long helices associated into a four-helix bundle [31]. On the other hand, the crystal structure of A. thaliana TBCA has recently been reported [32]. It forms a monomeric three-helix bundle where the α-helical residues are important for β-tubulin affinity as was previously shown for the human ortholog [30].…”

Section: Discussionmentioning

confidence: 99%

The Solution Structure of the N-Terminal Domain of Human Tubulin Binding Cofactor C Reveals a Platform for Tubulin Interaction

et al. 2011

View full text Add to dashboard Cite

Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of α- and β-tubulin monomers leading to the release of productive tubulin heterodimers ready to polymerize into microtubules. In this process it collaborates with other cofactors (TBC's A, B, D, and E) and forms a supercomplex with TBCD, β-tubulin, TBCE and α-tubulin. Here, we demonstrate that TBCC depletion results in multipolar spindles and mitotic failure. Accordingly, TBCC is found at the centrosome and is implicated in bipolar spindle formation. We also determine by NMR the structure of the N-terminal domain of TBCC. The TBCC N-terminal domain adopts a spectrin-like fold topology composed of a left-handed 3-stranded α-helix bundle. Remarkably, the 30-residue N-terminal segment of the TBCC N-terminal domain is flexible and disordered in solution. This unstructured region is involved in the interaction with tubulin. Our data lead us to propose a testable model for TBCC N-terminal domain/tubulin recognition in which the highly charged N-terminus as well as residues from the three helices and the loops interact with the acidic hypervariable regions of tubulin monomers.

show abstract

Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its β‐tubulin binding characterization

Cited by 7 publications

References 38 publications

Ultra‐small TiO₂ nanoparticles disrupt microtubular networks in Arabidopsis thaliana

Ultra‐small TiO₂ nanoparticles disrupt microtubular networks in Arabidopsis thaliana

Faithful chaperones

The Solution Structure of the N-Terminal Domain of Human Tubulin Binding Cofactor C Reveals a Platform for Tubulin Interaction

Contact Info

Product

Resources

About

Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its β‐tubulin binding characterization

Cited by 7 publications

References 38 publications

Ultra‐small TiO2 nanoparticles disrupt microtubular networks in Arabidopsis thaliana

Ultra‐small TiO2 nanoparticles disrupt microtubular networks in Arabidopsis thaliana

Faithful chaperones

The Solution Structure of the N-Terminal Domain of Human Tubulin Binding Cofactor C Reveals a Platform for Tubulin Interaction

Contact Info

Product

Resources

About

Ultra‐small TiO₂ nanoparticles disrupt microtubular networks in Arabidopsis thaliana

Ultra‐small TiO₂ nanoparticles disrupt microtubular networks in Arabidopsis thaliana