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Results 1 - 7 of 7
EC Number
General Information
Commentary
Reference
malfunction
enhancement of tubulin polymerization by Cl--induced blockade of intrinsic GTPase
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
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
metabolism
the enzyme is involved in the mechanisms underlying regulation of cell division in response to DNA damage
physiological function
a part of stimulatory effects of Cl- on in vitro tubulin polymerization is mediated via an inhibitory effect on GTPase activity of tubulin, although Cl- also regulates in vitro tubulin polymerization by factors other than an inhibitory effect on GTPase activity
physiological function
FtsZDr, a tubulin homologue in radioresistant bacterium Deinococcus radiodurans, is characterized as a GTPase exhibiting polymerization/depolymerization dynamics in vitro and FtsZ ring formation in vivo
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
Results 1 - 7 of 7