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Updated: Jan 12, 2026
Author Spotlight: Purifying High-Quality Tubulin to Study Protein Dynamics and Therapeutic Applications
Published on: October 11, 2024
Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization
Marcin Grynberg1, Lukasz Jaroszewski, Adam Godzik
1Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 5A Pawinskiego St, 02-106 Warsaw, Poland. marcin@ljcrf.edu
Background:
The correct folding and dimerization of tubulins, before their addition to the microtubular structure, needs a group of conserved proteins called cofactors A to E. The biochemical analysis of cofactors gave an insight to their general functions, however not much is known about the domain structure and detailed, molecular function of these proteins.
Results:
Combining modelling and fold prediction tools, we present 3D models of all cofactors, including several previously unannotated domains of cofactors B-E. Apart from the new HEAT and Armadillo domains in cofactor D and an unusual spectrin-like domain in cofactor C, we have identified a new subfamily of ubiquitin-like domains in cofactors B and E. Together, these observations provide a reliable, molecular level model of cofactor complex.
Conclusion:
Distant homology searches allowed the identification of unknown regions of cofactors as self-reliant domains and allow us to present a detailed hypothesis of how a cofactor complex performs its function.
