Literature summary for 3.6.5.6 extracted from

Geyer, E.A.; Burns, A.; Lalonde, B.A.; Ye, X.; Piedra, F.A.; Huffaker, T.C.; Rice, L.M.
A mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics (2015), eLife, 4, e10113.

Search for more literature for 3.6.5.6

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of His-tagged beta-tubulin mutant T238A in Saccharomyces cerevisiae, the transformed cells shows no mutant and wild-type microtubule dynamics	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
C354A	site-directed mutagenesis of beta-tubulin, the mutation dramatically reduces the rate of microtubule shrinking and the frequency of catastrophe	Saccharomyces cerevisiae
C354S	site-directed mutagenesis of beta-tubulin, the mutation dramatically reduces the rate of microtubule shrinking and the frequency of catastrophe	Saccharomyces cerevisiae
T238A	naturally occuring mutation, the buried mutation T238A in alphabeta-tubulin yields microtubules with dramatically reduced shrinking rate and catastrophe frequency, the mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics. The mutation causes these effects by suppressing a conformational change that normally occurs in response to GTP hydrolysis in the lattice, without detectably changing the conformation of unpolymerized alphabetab-tubulin. The mutation predominantly affects post-GTPase conformational and dynamic properties of microtubules. The buried T238A mutation in beta-tubulin hyperstablizes microtubules in vivo and in vitro. Mutant-induced changes in polymerization dynamics do not result from defective GTPase activity. The T238A alphabeta-tubulin undergoes spontaneous nucleation more readily than wild-type, even in the presence of a nonhydrolyzable GTP analog, GTPgammaS, phenotype, overview	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
microtubule	-	Saccharomyces cerevisiae	5874	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
GTP + H2O	Saccharomyces cerevisiae	-	GDP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged beta-tubulin mutant T238A from Saccharomyces cerevisiae by nickel affinity chromatography	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + H2O	-	Saccharomyces cerevisiae	GDP + phosphate	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.9	-	assay at	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
malfunction	the buried mutation T238A in alphabeta-tubulin yields microtubules with dramatically reduced shrinking rate and catastrophe frequency, the mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics. The mutation causes these effects by suppressing a conformational change that normally occurs in response to GTP hydrolysis in the lattice, without detectably changing the conformation of unpolymerized alphabetab-tubulin. The mutation predominantly affects post-GTPase conformational and dynamic properties of microtubules, phenotype, overview	Saccharomyces cerevisiae
metabolism	microtubule dynamic instability depends on the GTPase activity of the polymerizing alphabeta-tubulin subunits, which cycle through at least three distinct conformations as they move into and out of microtubules. This conformational cycle contributes to microtubule growing, shrinking, and switching	Saccharomyces cerevisiae
physiological function	the enzyme activity is esentially coupled to the alphabeta-tubulin conformational cycle that contributes to microtubule dynamics, overview. alphabeta-Tubulin conformational changes occur as a consequence of GTP hydrolysis deeper in the microtubule lattice	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)