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ATP + H2O
ADP + phosphate
-
hydrolyzed at a rate about half as fast like GTP
-
-
?
GTP + H2O
GDP + phosphate
ITP + H2O
IDP + phosphate
-
hydrolyzed at equivalent rates like GTP
-
-
?
XTP + H2O
XDP + phosphate
-
hydrolyzed at a rate about half as fast like GTP
-
-
?
additional information
?
-
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
644199, 644200, 644202, 644203, 644204, 644205, 644206, 644209, 644210, 644211, 667729 -
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
inverse isotope effect, reaction rate in D2O is twice the rate in H2O
-
-
?
GTP + H2O
GDP + phosphate
-
GTP-binding proteins from the tubulin family, including alpha,beta-tubulin are key components of the cytoskeleton and play central roles in chromosome segregation and cell division. The nucleotide switch of alpha,beta-tubulin is triggered by GTP hydrolysis and regulates microtubule assembly dynamics. Unassembled tubulin-GTP is in the inactive, curved conformation as in tubulin-GDP rings, and is driven into the straight microtubule conformation by the assembly contacts. Binding of the GTP gamma-phosphate only lowers the free energy difference between the curved and straight forms
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
recombinant tubulin homologue FtsZDr binds to GTP and shows GTPase activity, equirement of both Mg2+ and GTP for the polymerization of FtsZDr in higher ordered structure. The critical concentrationof FtsZDr required for GTPase activity is 0.0001 mM
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
GTP-binding proteins from the tubulin family, including alpha,beta-tubulin are key components of the cytoskeleton and play central roles in chromosome segregation and cell division. The nucleotide switch of alpha,beta-tubulin is triggered by GTP hydrolysis and regulates microtubule assembly dynamics. Unassembled tubulin-GTP is in the inactive, curved conformation as in tubulin-GDP rings, and is driven into the straight microtubule conformation by the assembly contacts. Binding of the GTP gamma-phosphate only lowers the free energy difference between the curved and straight forms
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
additional information
?
-
-
ATP, UTP and CTP are no substrates
-
-
?
additional information
?
-
enzyme FtsZDr acts as a GTPase exhibiting polymerization/depolymerization dynamics in vitro and FtsZ ring formation in vivo
-
-
?
additional information
?
-
-
enzyme FtsZDr acts as a GTPase exhibiting polymerization/depolymerization dynamics in vitro and FtsZ ring formation in vivo
-
-
?
additional information
?
-
the enzyme produces bundles of protofilaments in the presence of either GTP or Mg2+ions. But the formation of the higher size ordered structures required both GTP and Mg2+in vitro. It shows polymerization/depolymerization dynamics as a function of GTP and Mg2+. Nucleotide binding studies with GTP and ATP, overview
-
-
?
additional information
?
-
-
the enzyme produces bundles of protofilaments in the presence of either GTP or Mg2+ions. But the formation of the higher size ordered structures required both GTP and Mg2+in vitro. It shows polymerization/depolymerization dynamics as a function of GTP and Mg2+. Nucleotide binding studies with GTP and ATP, overview
-
-
?
additional information
?
-
the guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ
-
-
-
additional information
?
-
the guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ
-
-
-
additional information
?
-
-
GTP hydrolysis occurs at a single exchangeable GTP-binding site which is at the interface between head-to-tail arranged heterodimer enzyme
-
-
?
additional information
?
-
gamma-tubulin binds to mitochondrial DNA
-
-
-
additional information
?
-
GTP binding to the alpha occurs in the dimerization region between the alpha and beta monomers and remains unhydrolyzed. This is called the non-exchangeable site or N-site. GTP binding to beta-tubulin sits at the interface between two dimers within the protofilament, the longitudinal lattice of tubulin dimers running parallel to the microtubule filament long axis. Tubulin controls microtubule dynamics, analysis of GTP hydrolysis on reconstructed microtubules, mechanism, overview. GTP binding to the beta tubulin is hydrolyzable and this site is called the exchangeable site or E-site. Hydrolysis of GTP at the E-site is required for microtubule dynamic instability. GTP hydrolysis leads to the compaction of the lattice around the interdimer longitudinal interface sandwiching the E-site nucleotide. This compaction in turn results in a conformational rearrangement in all alpha-tubulin monomers corresponding to a small rotation of the intermediate domain and C-terminal H11-H12 helices with respect to the N-terminal domain in alpha-tubulin. Additionally, helix H8 from alpha-tubulin is also distorted in the GDP-state. The hydrolysis is immediate, but the probability of hydrolysis within a certain time is increased when the next dimer binds. Such catalysis leads to a situation where dimers at the end of the filament typically have GTP, and are in a non-compacted, straight conformation. This is called the GTP cap. Dimers within the body of the filament are typically in the GDP-state and prefer to be in the compacted, bent conformation. Due to binding to neighbors, the GDP dimers cannot compact and are held straight. Thus, GDP dimers in the body are in a high potential energy state, spring-loaded to compact whenever constraints are relaxed. The purpose of the GTPase is to force dimers within the body into this spring-loaded state. When the dimers at the top are lost or hydrolyzed stochastically, the end cap loses coherence and the entire microtubule bends back to relax the dimers to their lowest energy state. The longitudinal binding is less affected by the hydrolysis and protofilaments peel back into rings unraveling the microtubule
-
-
-
additional information
?
-
-
efficiency of in vitro tubulin polymerization in solutions containing a non-hydrolyzable analogue of GTP, GpCpp, instead of GTP is much higher than that in the presence of GTP
-
-
?
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evolution
tubulin comes as a heterodimer of alpha and beta forms While there is only 45% amino-acid sequence similarity between alpha and beta tubulin isoforms, the three-dimensional structures of the monomers are very similar, each consisting of three domains of similar length and secondary structure composition: the N-terminal, the middle, and the C-terminal domain. Both alpha and beta bind GTP
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
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
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
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
-
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
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
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
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
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
physiological function
the tubulin homologue FtsZ is the central component of the cell division machinery in nearly all walled bacterial species. During division, FtsZ polymerizes on the cytoplasmic face of the inner membrane to form a ring-like structure, the Z-ring, and recruits more than 30 proteins to the division site. Many of these proteins are involved in septal synthesis of the peptidoglycan (PG) cell wall. The guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ. Exceptionally, in Escherichia coli the GTPase activity of FtsZ appears nonessential for cell division and does not dictate the cell constriction rate. In Escherichia coli cells, FtsZ exhibits dynamic treadmilling predominantly determined by its guanosine triphosphatase activity. The treadmilling dynamics direct the processive movement of the septal cell wall synthesis machinery but do not limit the rate of septal synthesis. FtsZ treadmilling provides a mechanism for achieving uniform septal cell wall synthesis to enable correct polar morphology
physiological function
-
the tubulin homologue FtsZ is the central component of the cell division machinery in nearly all walled bacterial species. During division, FtsZ polymerizes on the cytoplasmic face of the inner membrane to form a ring-like structure, the Z-ring, and recruits more than 30 proteins to the division site. Many of these proteins are involved in septal synthesis of the peptidoglycan (PG) cell wall. The guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ. Exceptionally, in Escherichia coli the GTPase activity of FtsZ appears nonessential for cell division and does not dictate the cell constriction rate. In Escherichia coli cells, FtsZ exhibits dynamic treadmilling predominantly determined by its guanosine triphosphatase activity. The treadmilling dynamics direct the processive movement of the septal cell wall synthesis machinery but do not limit the rate of septal synthesis. FtsZ treadmilling provides a mechanism for achieving uniform septal cell wall synthesis to enable correct polar morphology
-
additional information
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
additional information
-
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
-
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D158A
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
D212G
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
D269A
site-directed mutagenesis
E238A
site-directed mutagenesis
E250A
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
G105S
site-directed mutagenesis
D158A
-
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
-
D269A
-
site-directed mutagenesis
-
E238A
-
site-directed mutagenesis
-
E250A
-
site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells
-
C13A
site-directed mutagenesis, mutation of Cyst13 to Ala (GFP-A13gamma-tubulinresist) impairs GTP binding to the GTPase domain, stable co-expresses of the mutated recombinant protein in gamma-tubulin sh-U2-OS cells
R399A/K400A/R409A
site-directed mutagenesis
C354A
-
site-directed mutagenesis of beta-tubulin, the mutation dramatically reduces the rate of microtubule shrinking and the frequency of catastrophe
C354S
-
site-directed mutagenesis of beta-tubulin, the mutation dramatically reduces the rate of microtubule shrinking and the frequency of catastrophe
T143G
-
mutation in tubulin signature motif of beta-tubulin, both GTP-binding affinity and microtubule-dependent GTPase activity are reduced at least 15 fold, mutant cells have a delay in mitosis
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
additional information
comparison of threadmilling speed and catalytic activity of wild-type and mutant cells and FtsZ polymers, overview. FtsZ GTPase mutants change the spatial distribution pattern but not the rate of septal PG synthesis
additional information
-
comparison of threadmilling speed and catalytic activity of wild-type and mutant cells and FtsZ polymers, overview. FtsZ GTPase mutants change the spatial distribution pattern but not the rate of septal PG synthesis
-
additional information
generation of stably or transient transfected gamma-tubulin shRNA, pEGFP-gamma-tubulinresist, pEGFP-A13-gamma-tubulinresist, gamma-tubulinsgrest, gamma-tubulinR399A-K400A-R409A sgrest, and gamma-tubulin336-451 U2OS, and MCF10A cells. Stable co-expression of gamma-tubulin sgRNA depleting the endogenous gamma-tubulin pool. Fixed U2OS cells transiently expressing gamma-tubulin sgRNA (Cas9-crispGFP) are immunofluorescence stained with an anti-MTCO2 antibody and a gamma-tubulin antibody originated in mouse. Sg-mediated knockdown of gamma-tubulin affects the activity of the mitochondria, but not the structure of the endoplasmic reticulum
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Monasterio, O.; Timasheff, S.N.
Inhibition of tubulin self-assembly and tubulin-colchicine GTPase activity by guanosine 5'-(gamma-fluorotriphosphate)
Biochemistry
26
6091-6099
1987
Bos taurus
brenda
Caplow, M.; Shanks, J.
Mechanism of the microtubule GTPase reaction
J. Biol. Chem.
265
8935-8941
1990
Bos taurus, Sus scrofa
brenda
Burns, R.G.
Kinetics of GTP hydrolysis during the assembly of chick brain MAP-tubulin microtubule protein
Biochem. J.
277
239-243
1991
Gallus gallus
brenda
Roychowdhury, S.; Rasenick, M.M.
Tubulin-G protein association stabilizes GTP binding and activates GTPase: Cytoskeletal participation in neuronal signal transduction
Biochemistry
33
9800-9805
1994
Bos taurus, Gallus gallus
brenda
Perez-Ramirez, B.; Shearwin, K.E.; Timasheff, S.N.
The colchicine-induced GTPase activity of tubulin: State of the product. Activation by microtubule-promoting cosolvents
Biochemistry
33
6253-6261
1994
Bos taurus
brenda
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Cosolvent modulation of the tubulin-colchicine GTPase-activating conformational change: Strength of the enzymatic activity
Biochemistry
33
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1994
Bos taurus
brenda
Sage, C.R.; Dougherty, C.A.; Davis, A.S.; Burns, R.G.; Wilson, L.; Farrell, K.W.
Site directed mutagenesis of putative GTP-binding sites of yeast beta-tubulin: Evidence that alpha-, beta-, and gamma-tubulins are atypical GTPases
Biochemistry
34
7409-7419
1995
Bos taurus, Saccharomyces cerevisiae, Gallus gallus
brenda
Mejillano, M.R.; Shivanna, B.D.; Himes, R.H.
Studies on the nocodazole-induced GTPase activity of tubulin
Arch. Biochem. Biophys.
336
130-138
1996
Bos taurus
brenda
Soto, C.; Rodriguez, P.H.; Monasterio, O.
Calcium and gadolinium ions stimulate the GTPase activity of purified chicken brain tubulin through a conformational change
Biochemistry
35
6337-6344
1996
Gallus gallus
brenda
Best, A.; Ahmed, S.; Kozma, R.; Lim, L.
The ras-related GTPase Rac1 binds tubulin
J. Biol. Chem.
271
3756-3762
1996
Rattus norvegicus
brenda
Banerjee, A.
Differential effects of colchicine and its B-ring modified analog MTPT on the assembly-independent GTPase activity of purified beta-tubulin isoforms from bovine brain
Biochem. Biophys. Res. Commun.
231
698-700
1997
Bos taurus
brenda
Tian, G.; Bhamidipati, A.; Cowan, N.J.; Lewis, S.A.
Tubulin folding cofactors as GTPase-activating proteins
J. Biol. Chem.
274
24054-24058
1999
Bos taurus, Gallus gallus, Mus musculus
brenda
Roychowdhury, S.; Panda, D.; Wilson, L.; Rasenick, M.M.
G Protein alpha subunits activate tubulin GTPase and modulate microtubule polymerization dynamics
J. Biol. Chem.
274
13485-13490
1999
Bos taurus, Ovis aries
brenda
Dougherty, C.A.; Sage, C.R.; Davis, A.; Farrell, K.W.
Mutation in the beta-tubulin signature motif suppresses microtubule GTPase activity and dynamics, and slows mitosis
Biochemistry
40
15725-15732
2001
Saccharomyces cerevisiae
brenda
Gupta, K.; Panda, D.
Perturbation of microtubule polymerization by quercetin through tubulin binding: a novel mechanism of its antiproliferative activity
Biochemistry
41
13029-13038
2002
Capra hircus
brenda
Brannstrom, K.; Segerman, B.; Gullberg, M.
Molecular dissection of GTP exchange and hydrolysis within the ternary complex of tubulin heterodimers and Op18/stathmin family members
J. Biol. Chem.
278
16651-16657
2003
Homo sapiens
brenda
Anders, K.R.; Botstein, D.
Dominant-lethal alpha-tubulin mutants defective in microtubule depolymerization in yeast
Mol. Biol. Cell
12
3973-3986
2001
Saccharomyces cerevisiae
brenda
Buey, R.M.; Diaz, J.F.; Andreu, J.M.
The nucleotide switch of tubulin and microtubule assembly: a polymerization-driven structural change
Biochemistry
45
5933-5938
2006
Bos taurus, Rattus norvegicus
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Nogales, E.; Wang, H.W.
Structural mechanisms underlying nucleotide-dependent self-assembly of tubulin and its relatives
Curr. Opin. Struct. Biol.
16
221-229
2006
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In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB
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169
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2005
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Banerjee, M.; Poddar, A.; Mitra, G.; Surolia, A.; Owa, T.; Bhattacharyya, B.
Sulfonamide drugs binding to the colchicine site of tubulin: thermodynamic analysis of the drug-tubulin interactions by isothermal titration calorimetry
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48
547-555
2005
Capra hircus
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Wang, C.; Cormier, A.; Gigant, B.; Knossow, M.
Insight into the GTPase activity of tubulin from complexes with stathmin-like domains
Biochemistry
46
10595-10602
2007
Bos taurus
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Layden, B.T.; Saengsawang, W.; Donati, R.J.; Yang, S.; Mulhearn, D.C.; Johnson, M.E.; Rasenick, M.M.
Structural model of a complex between the heterotrimeric G protein, Gsalpha, and tubulin
Biochim. Biophys. Acta
1783
964-973
2008
Ovis aries
brenda
Xi, J.H.; Bai, F.; McGaha, R.; Andley, U.P.
Alpha-crystallin expression affects microtubule assembly and prevents their aggregation
FASEB J.
20
846-857
2006
Bos taurus, Mus musculus
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Gupta, K.K.; Bharne, S.S.; Rathinasamy, K.; Naik, N.R.; Panda, D.
Dietary antioxidant curcumin inhibits microtubule assembly through tubulin binding
FEBS J.
273
5320-5332
2006
Capra hircus
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Srivastava, P.; Panda, D.
Rotenone inhibits mammalian cell proliferation by inhibiting microtubule assembly through tubulin binding
FEBS J.
274
4788-4801
2007
Capra hircus
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Tang, M.; Bideshi, D.K.; Park, H.W.; Federici, B.A.
Iteron-binding ORF157 and FtsZ-like ORF156 proteins encoded by pBtoxis play a role in its replication in Bacillus thuringiensis subsp. israelensis
J. Bacteriol.
189
8053-8058
2007
Bacillus thuringiensis
brenda
Thakur, M.; Chakraborti, P.K.
GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA
J. Biol. Chem.
281
40107-40113
2006
Escherichia coli, Mycobacterium tuberculosis
brenda
Inoue, I.; Ino, R.; Nishimura, A.
New model for assembly dynamics of bacterial tubulin in relation to the stages of DNA replication
Genes Cells
14
435-444
2009
Escherichia coli
brenda
Cormier, A.; Clement, M.J.; Knossow, M.; Lachkar, S.; Savarin, P.; Toma, F.; Sobel, A.; Gigant, B.; Curmi, P.A.
The PN2-3 domain of centrosomal P4.1-associated protein implements a novel mechanism for tubulin sequestration
J. Biol. Chem.
284
6909-6917
2009
Ovis aries
brenda
Mendieta, J.; Rico, A.I.; Lopez-Vinas, E.; Vicente, M.; Mingorance, J.; Gomez-Puertas, P.
Structural and functional model for ionic (K(+)/Na(+)) and pH dependence of GTPase activity and polymerization of FtsZ, the prokaryotic ortholog of tubulin
J. Mol. Biol.
390
17-25
2009
Methanocaldococcus jannaschii (Q57816), Methanocaldococcus jannaschii
brenda
Nakajima, K.; Niisato, N.; Marunaka, Y.
Enhancement of tubulin polymerization by Cl--induced blockade of intrinsic GTPase
Biochem. Biophys. Res. Commun.
425
225-229
2012
Sus scrofa
brenda
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
eLife
4
e10113
2015
Saccharomyces cerevisiae
brenda
Modi, K.M.; Tewari, R.; Misra, H.S.
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
Int. J. Biochem. Cell Biol.
50
38-46
2014
Deinococcus radiodurans (Q9RWN5), Deinococcus radiodurans
brenda
Bailey, M.E.; Jiang, N.; Dima, R.I.; Ross, J.L.
Microtubule severing enzymes couple ATPase activity with tubulin GTPase spring loading
Biopolymers
105
547-556
2016
Homo sapiens (P23258)
brenda
Lindstroem, L.; Li, T.; Malycheva, D.; Kancharla, A.; Nilsson, H.; Vishnu, N.; Mulder, H.; Johansson, M.; Rossello, C.A.; Alvarado-Kristensson, M.
The GTPase domain of gamma-tubulin is required for normal mitochondrial function and spatial organization
Commun. Biol.
1
37
2018
Homo sapiens (P23258)
brenda
Yang, X.; Lyu, Z.; Miguel, A.; McQuillen, R.; Huang, K.C.; Xiao, J.
GTPase activity-coupled treadmilling of the bacterial tubulin FtsZ organizes septal cell wall synthesis
Science
355
744-747
2017
Escherichia coli (P0A9A6), Escherichia coli BW25113 (P0A9A6)
brenda