Tubulin Dimer Reversible Dissociation
نویسندگان
چکیده
منابع مشابه
Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source.
The finding that exchange of tubulin subunits between tubulin dimers (alpha-beta + alpha'beta' <--> alpha'beta + alphabeta') does not occur in the absence of protein cofactors and GTP hydrolysis conflicts with the assumption that pure tubulin dimer and monomer are in rapid equilibrium. This assumption underlies the many physical chemical measurements of the K(d) for dimer dissociation. To resol...
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Tubulin proteostasis is regulated by a group of molecular chaperones termed tubulin cofactors (TBC). Whereas tubulin heterodimer formation is well-characterized biochemically, its dissociation pathway is not clearly understood. Here, we carried out biochemical assays to dissect the role of the human TBCE and TBCB chaperones in α-tubulin-β-tubulin dissociation. We used electron microscopy and im...
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An approximate value of the diamagnetic anisotropy of the tubulin dimer, Δχ dimer, has been determined assuming axial symmetry and that only the α -helices and β -sheets contribute to the anisotropy. Two approaches have been utilized: (a) using the value for the Δχ α for an α -helical peptide bond given by Pauling (1979) and (b) using the previously determined anisotropy of fibrinogen as a cali...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2016
ISSN: 0021-9258
DOI: 10.1074/jbc.m115.699728