EC Number   |
General Information |
Reference |
|---|
   3.6.5.6 | 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 |
733253 |
| 3.6.5.6 | physiological function |
an important regulator of microtubule dynamics during cell division is the protein gamma-tubulin. gamma-Tubulin expression and its GTPase domain are necessary for the organization of mitochondria in tubular structures. In the cell, gamma-tubulin establishes a cellular network of threads named the gamma-string meshwork. gamma-Strings have the ability to connect the cytoplasm and the mitochondrial DNA together. gamma-Tubulin has a role in the maintenance of the mitochondrial network and functions. The endoplasmic reticulum is not affected by gamma-tubulin. gamma-Tubulin provides a cytoskeletal element that gives form to the mitochondrial network. gamma-Tubulin regulates the expression of mitochondrial genes, overview of upregulated mitochondria-related genes. It affects the replication of mitochondrial DNA |
756504 |
| 3.6.5.6 | more |
determination of Z-ring dynamics in live Escherichia coli strain BW25113 cells by using total internal reflection fluorescence (TIRF) microscopy to monitor the fluorescence of an FtsZ-GFP fusion protein. Mutants lacking one of the proteins that regulates the Z-ring (SlmA, SulA, MinC, ClpX, and ClpP) or stabilizes it (ZapA, ZapB, ZapC, ZapD, and MatP) also display wild-type Z-ring behavior. Thus, Z-ring dynamics are likely due to FtsZ's intrinsic polymerization properties, which are related to its GTPase activity. Z-ring dynamics were significantly reduced in mutants with lower GTPase activity |
-, 758464 |
| 3.6.5.6 | malfunction |
enhancement of tubulin polymerization by Cl--induced blockade of intrinsic GTPase |
733253 |
| 3.6.5.6 | 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 |
733983 |
| 3.6.5.6 | metabolism |
gamma-tubulin forms a cellular meshwork of gamma-strings and gamma-tubules. While gamma-tubules are polar cytosolic filaments within the gamma-string meshwork, gamma-strings are detected in both the cytoplasm and the nucleus and are formed of non-polar protein threads that cross the double membrane of the nuclear envelope. The gamma-string meshwork forms a boundary around chromatin, which coordinates cytosolic and nuclear events during mitosis by assuring that a nuclear envelope forms around daughter chromosomes. The gamma-tubulin meshwork may be a dynamic network that contributes to cellular homeostasis |
756504 |
| 3.6.5.6 | malfunction |
in FtsZ mutants with severely reduced treadmilling, the spatial distribution of septal synthesis and the molecular composition and ultrastructure of the septal cell wall are substantially altered. Z-ring dynamics are significantly reduced in mutants with lower GTPase activity. In addition, the subunit exchange rate constants (kex) of these mutants decreases with kcat in a manner consistent with coupling to GTP hydrolysis. FtsZ GTPase mutants change the spatial distribution pattern but not the rate of septal PG synthesis |
-, 758464 |
| 3.6.5.6 | 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 |
733717 |
| 3.6.5.6 | physiological function |
microtubules are amazing filaments made of GTPase enzymes that store energy used for their own selfdestruction to cause a stochastically driven dynamic called dynamic instability. Dynamic instability can be reproduced in vitro with purified tubulin, but the dynamics do not mimic that observed in cells. This is because stabilizers, e.g. paclitaxel, and destabilizers, e.g. Ca2+, act to alter microtubule dynamics. Another class of destabilizers consists of the microtubule-severing enzymes from the ATPases associated with various cellular activities (AAA+) family of ATP-enzymes. GTP-driven microtubule dynamics are coupled to ATP-driven destabilization by severing enzymes. The GTP enzyme that polymerizes into the microtubules is called tubulin, which comes as a heterodimer of alpha and beta forms. Tubulin controls microtubule dynamics, analysis of GTP hydrolysis on reconstructed microtubules, mechanism, overview |
756202 |
| 3.6.5.6 | malfunction |
reduced levels of gamma-tubulin or impairment of its GTPase domain disrupts the mitochondrial network and alters both their respiratory capacity and the expression of mitochondrial-related genes. By contrast, reduced mitochondrial number or increased protein levels of gamma-tubulin DNA-binding domain enhance the association of gamma-tubulin with mitochondria. Increased mitochondria protein transport and low cellular mitochondria content affect the gamma-tubulin meshwork. Sg-mediated knockdown of gamma-tubulin affects the activity of the mitochondria, but not the structure of the endoplasmic reticulum |
756504 |
