Information on EC 3.6.4.2 - dynein ATPase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.4.2
-
RECOMMENDED NAME
GeneOntology No.
dynein ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphonic ester bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (tubulin-translocating)
A multisubunit protein complex associated with microtubules. Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome towards the microtubule's minus end. It also functions in the movement of eukaryotic flagella and cilia. It consists of two heavy chains (about 500 kDa), three-four intermediate chains (about 70 kDa) and four light chains (about 50 kDa).
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aequipecten sp.
gill
-
-
Manually annotated by BRENDA team
starfish
-
-
Manually annotated by BRENDA team
Chlamydomonas sp.
Ciona sp.
-
-
-
Manually annotated by BRENDA team
Colobocentrotus sp.
sea urchin
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
organism contains two dynein-2 isoforms
-
-
Manually annotated by BRENDA team
cytoplasmic dynein, heavy chain 1; organism contains two dynein-2 isoforms
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
blue mussel
-
-
Manually annotated by BRENDA team
surf clam
-
-
Manually annotated by BRENDA team
sea urchin
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
sea urchin
-
-
Manually annotated by BRENDA team
organism contains two dynein-2 isoforms
-
-
Manually annotated by BRENDA team
Unio sp.
gill
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-dATP + H2O
2'-dADP + phosphate
show the reaction diagram
-
-
-
-
?
2'-deoxy-ATP + H2O
2'-deoxy-ADP + phosphate
show the reaction diagram
-
-
-
?
3'-dATP + H2O
3'-dADP + phosphate
show the reaction diagram
-
-
-
-
?
3'-deoxy-ATP + H2O
3'-deoxy-ADP + phosphate
show the reaction diagram
-
-
-
?
8-bromo-ATP + H2O
8-bromo-ADP + phosphate
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
BODIPY-FL-ATP + H2O
BODIPY-FL-ADP + phosphate
show the reaction diagram
-
fluorescent ATP analogue, hydrolysis at 78% of the rate with ATP, without induction of microtubule translocation or sliding disintegration of elastase-treated axonemes. After preincubation with nonhydrolysable adenosine 5'-(beta:gamma-imido)triphosphate, BODIPY-FL-ATP induces sliding disintegration in about 10% of the axonemes
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
dideoxy-ATP + H2O
monomethyl-ADP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
ITP + H2O
IDP + phosphate
show the reaction diagram
-
-
-
?
TTP + H2O
TDP + phosphate
show the reaction diagram
UTP + H2O
UDP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(7-chloro-4-oxo-3,4-dihydroquinazolin-2(1H)-ylidene)-3-(2,4-dichlorophenyl)-3-oxopropanenitrile
3-(2,4-dichlorophenyl)-3-oxo-2-(4-oxo-3,4-dihydroquinazolin-2(1H)-ylidene)propanenitrile
Adenylyl imidodiphosphate
-
competitive inhibition
AlCl3
-
1 mM, complete inhibition
antibody 70.1
-
antibody raised against the intermediate chain of dynein, exerts a functional inhibitory effect upon dynein function by preventing its association with the accessory complex dynactin. Treatment with 70.1 prevents formation of the prominent endoplasmic reticulum ring characteristic of metaphase I oocytes
-
antibody 74.1
-
monoclonal antibody directed against the dynein intermediate chain. Antibody prevents binding of the dynein intermediate chain to the p150Glued subunit of dynactin and disrupts the dynein-dynactin complex without having an effect on the dynactin structure. Inhibition induces rapid loss of radial microtubule organization, while the levels of key centrososmal proteins or the rates of microtubule nucleation do not change significantly
-
EGTA
-
inhibits demembranated sperm motility at 30°C, reversible by Ca2+, is less effective at 40°C
erythro-9-[3-(2-hydroxynonyl)]adenine
fragment CC1
-
fragment of p150Glued subunit of the dynactin complex that corresponds to the coiled coil 1. Fragment prevents binding of the dynein intermediate chain to the p150Glued subunit of dynactin and disrupts the dynein–dynactin complex without having an effect on the dynactin structure. Inhibition induces rapid loss of radial microtubule organization, while the levels of key centrososmal proteins or the rates of microtubule nucleation do not change significantly
-
Li+
-
6 mM, 72% inhibition
lissencephaly protein Lis1
-
the lissencephaly protein Lis1 regulates the mechanical behavior of cytoplasmic dynein, the primary minus-end-directed microtubule motor, regulatory mechanism. Rather than binding to the main ATPase site within dynein's AAA+ ring or its microtubule-binding stalk directly, dimeric Lis1 engages the interface between these elements. Lis1 causes individual dynein motors to remain attached to microtubules for extended periods, even during cycles of ATP hydrolysis that canonically induces detachment. Lis1 operates like a clutch that prevents dynein's ATPase domain from transmitting a detachment signal to its track-binding domain. The Lis1 beta propeller domain contains regulatory elements that act on dynein's motor and Lis1 alters allosteric communication between dynein's ATPase and microtubule-binding domains
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myristoyl-CoA
-
0.040 mM, activates at 0.010 mM
palmitoyl-CoA
-
noncompetitive inhibition of 14S dynein ATPase at 0.040 mM, bovine serum albumin (1mg/ml) and spermine (0.1 and 1 mM) reverse inhibition
vanadate
VO43-
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
-
2fold activation, maximum between 0.5 and 0.7 M
axonemes
-
salt-extracted axonemes cause a 7 to 8fold activation of 21S dynein, maximum activation with axoneme/dynein weight ratio 14/1, low ionic strength, pH 7.9-8.3
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Calmodulin
Cl-
-
more than 15fold activation between 0 and 1.0 M
Lactate
-
2fold activation, maximum between 0.5 and 0.7 M
Lis1
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stimulates the average in vitro enzymatic activity of dynein by 40%. A subpopulation of brain dynein binds Lis1. ATPase activity is substantially higher for dynein motors that interact with Lis1. It is proposed that modulation of the Lis1-dynein-interaction serves as a control point in motor regulation
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Lys-Phe-Gly-Val-Gly-Phe-Lys
-
-
-
microtubule
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microtubules
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myristoyl-CoA
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activats at 0.01 mM, inhibits at 0.04 mM
NH4Cl
-
concentrations of 0.2 to 0.4 M stimulate enzyme activity 1.4 to 1.6fold
palmitoyl-CoA
-
activates dynein between 2 and 0.01 mM, inhibites at 0.04 mM
phosphatidylcholine
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mixture of 0.2 mg/ml phosphatidylserine and phosphatidylcholine leads to an 2.4fold increase in dynein activity
phosphatidylserine
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mixture of 0.2 mg/ml phosphatidylserine and phosphatidylcholine leads to an 2.4fold increase in dynein activity
sea urchin egg
-
3-to 8fold
-
succinate
-
2fold activation, maximum between 0.5 and 0.7 M
Triton X-100
tubulin
-
from porcine brain, 3fold increase of 30S dynein activity at pH 10, maximum at a tubulin/30S dynein molar ratio of 10
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Val-Ala-Ile-Thr-Val-Leu-Val-Lys
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 400
ATP
0.00003 - 0.00059
microtubule
-
additional information
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 121.1
ATP
5
Formycin triphosphate
Tetrahymena thermophila
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-
additional information
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.007
-
asthenozoospermic samples
0.01
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activity in crude dynein extract of fowl spermatozoa at 40°C
0.013
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asthenozoospermic samples, addition of 2 mM adenosine; asthenozoospermic samples, addition of 2 mM adenosine and 50 microM dipyridamol
0.014
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asthenozoospermic samples, addition of 2 mM 2-deoxyadenosine; normozoospermic samples
0.018
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normozoospermic samples, addition of 0.001 mM 5'-(N-ethylcarboxyamido)-adenosine; normozoospermic samples, addition of 2 mM adenosine; normozoospermic samples, addition of 2 mM adenosine and 0.05 mM dipyridamol
0.019
-
normozoospermic samples, addition of 2 mM 2-deoxyadenosine
0.026
-
containing 2 mM MgCl2, pH 8.0. 37°C
0.03
-
19S sucrose gradient dynein particle, substrate GTP
0.05
-
21S sucrose gradient fraction, 4 mM MgSO4, 0.5 mM EDTA, 1 mM ATP, pH 8
0.07
-
low salt extract
0.08
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21S sucrose gradient fraction, 4 mM MgSO4, 0.5 mM EDTA, 1 mM ATP, pH 8, in the absence of KCL
0.09
-
19S sucrose gradient dynein particle, substrate ITP
0.11
-
19S sucrose gradient dynein particle, substrate UTP
0.14
-
sperm flagellar axonemes
0.18
-
without activation
0.26
-
latent activity of 21S dynein 1, increasing activity after exposure to 40°C, Triton X-100 or -SH reagents
0.33
-
in the presence of 0.1 mg/ml phosphatidylserine and phosphatidylcholine, only ATPase activity is activated
0.36
-
30S dynein, substrate 3'-deoxy-ATP
0.43
-
30S dynein, substrate 8-bromo-ATP
0.48
-
in the presence of 0.6 mg/ml microtubules
0.62
-
salt extract with detergent
0.72
-
salt extract
0.93
-
30S dynein
0.96
-
30S dynein, substrate 2'-deoxy-ATP
1.2
-
19S sucrose gradient dynein particle
2.23
-
14S dynein ATPase
2.3
-
reassembled subunits of 18S dynein
2.5
-
30S dynein, in the presence of tubulin
2.8
Colobocentrotus sp.
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
12S dynein 2
7.9
-
assay at
10.5
-
21S dynein 1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10.5
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gradual increase from pH 6 to pH 9, sharp peak at pH 10.5
6.5 - 9.5
-
linear increase from pH 6 to pH 9, sharp peak at pH 9.5
7
-
activity is about 3.5fold less than at pH 7.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
higher activity at compared to 30°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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only intact but also demembranated cytosol-free sperm are motile at 30°C, but inactive at 40°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cytoplasmic dynein is the sole motor for microtubule-based ER motility throughout the early stages of development
Manually annotated by BRENDA team
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hippocampal neuron. Tctex-1 is enriched in growing axons of cultured hippocampal neurons. The cytoplasmic dynein light chain Tctex-1 plays a key role in multiple steps of hippocampal neuron development, including initial neurite sprouting, axon specification, and later dendritic elaboration. The neuritogenic effects elicited by Tctex-1 are independent from its cargo adaptor role for dynein motor transport. The selective high level of Tctex-1 at the growth cone of growing axons drives fast neurite extension by modulating actin dynamics and also Rac1 activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
dendritic spines
Manually annotated by BRENDA team
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redistribution of endoplasmic reticulum during oocyte maturation is dynein-driven and cell cycle-dependent
Manually annotated by BRENDA team
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epidermal growth factor relocates to the cell centre in a dynein-dependent fashion, comcomitant with the sorting away of transferrin receptor, but still remains in GTPase Rab5-positive early endosome. disrupion of dynein function results in retarded recycling of transferrin from epidermal growth factor-containing endosomes, retarded loss of GTPase Rab5, and reduced endosome enlargement
Manually annotated by BRENDA team
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dynactin and cytoplasmic dynein require each other for microtubule plus-end accumulation
Manually annotated by BRENDA team
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cytoplasmic dynein localizes to phagosomes in vivo
-
Manually annotated by BRENDA team
additional information
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both dynein heavy and intermediate chains are enriched in the postsynaptic density fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
alpha1,alpha2,IC2,IC3,LC2,LC3,LC4, 1 * 450000 + 1 * 430000 + 1 * 96000 + 1 * 82000 + 1* 18000 + 1 * 16500 + 1 * 14000, dynein polypeptides from flagella, heavy chains, intermediate chains (IC) and light chains (LC), SDS-PAGE
14500
-
alpha1,alpha2,IC1,IC2,IC3,LC2,LC3,LC4, 1 * 450000 + 1 * 430000 + 1 * 130000 + 1 * 96000 + 1 * 82500 + 1* 19000 + 1 * 16500 + 1 * 14500, dynein polypeptides from flagella, heavy chains, intermediate chains (IC) and light chains (LC), SDS-PAGE
16000
-
alpha,LC1, 1 * 440000 + 1 * 16000, 18S dynein, alpha subunit
18000
-
alpha,LC1,LC2, 1 * 400000 + 1 * 22000 + 1 * 18000, 12S dynein
21000
-
alpha1,alpha2,IC2,IC3,LC1,LC2,LC3, 1 * 450000 + 1 * 430000 + 1 * 94000 + 1 * 80000 + 1* 27000 + 1 * 21000 + 1 * 17000, dynein polypeptides from cilia, heavy chains, intermediate chains (IC) and light chains (LC), SDS-PAGE
22000
-
alpha,LC1,LC2, 1 * 400000 + 1 * 22000 + 1 * 18000, 12S dynein
69000
-
alpha, IC1,IC2,LC1-7, 1 * 420000 + 1 * 78000 + 1 * 69000 + 7 * 8000-20000, 18S dynein, beta subunit
76000
-
alpha1,alpha2,IC1,IC2,IC3,LC1-LC4, 1 * 333000 + 1 * 320000 + 1 * 122000 + 1 * 90000 + 1 * 76000 + 1 * 76000 + 4 * 24000-14000, 21S dynein 1, SDS-PAGE
80000
-
alpha1,alpha2,IC2,IC3,LC1,LC2,LC3, 1 * 450000 + 1 * 430000 + 1 * 94000 + 1 * 80000 + 1* 27000 + 1 * 21000 + 1 * 17000, dynein polypeptides from cilia, heavy chains, intermediate chains (IC) and light chains (LC), SDS-PAGE
82000
-
alpha1,alpha2,IC2,IC3,LC2,LC3,LC4, 1 * 450000 + 1 * 430000 + 1 * 96000 + 1 * 82000 + 1* 18000 + 1 * 16500 + 1 * 14000, dynein polypeptides from flagella, heavy chains, intermediate chains (IC) and light chains (LC), SDS-PAGE
82500
-
alpha1,alpha2,IC1,IC2,IC3,LC2,LC3,LC4, 1 * 450000 + 1 * 430000 + 1 * 130000 + 1 * 96000 + 1 * 82500 + 1* 19000 + 1 * 16500 + 1 * 14500, dynein polypeptides from flagella, heavy chains, intermediate chains (IC) and light chains (LC), SDS-PAGE
91000
-
alpha,beta, IC1,IC2, 1 * 420000 + 1 * 360000 + 1 * 140000 + 1 * 91000, unidentified lower weight peptides
94000
-
alpha1,alpha2,IC2,IC3,LC1,LC2,LC3, 1 * 450000 + 1 * 430000 + 1 * 94000 + 1 * 80000 + 1* 27000 + 1 * 21000 + 1 * 17000, dynein polypeptides from cilia, heavy chains, intermediate chains (IC) and light chains (LC), SDS-PAGE
122000
-
alpha1,alpha2,IC1,IC2,IC3,LC1-LC4, 1 * 333000 + 1 * 320000 + 1 * 122000 + 1 * 90000 + 1 * 76000 + 1 * 76000 + 4 * 24000-14000, 21S dynein 1, SDS-PAGE
130000
-
alpha1,alpha2,IC1,IC2,IC3,LC2,LC3,LC4, 1 * 450000 + 1 * 430000 + 1 * 130000 + 1 * 96000 + 1 * 82500 + 1* 19000 + 1 * 16500 + 1 * 14500, dynein polypeptides from flagella, heavy chains, intermediate chains (IC) and light chains (LC), SDS-PAGE
140000
-
alpha,beta, IC1,IC2, 1 * 420000 + 1 * 360000 + 1 * 140000 + 1 * 91000, unidentified lower weight peptides
320000
333000
-
alpha1,alpha2,IC1,IC2,IC3,LC1-LC4, 1 * 333000 + 1 * 320000 + 1 * 122000 + 1 * 90000 + 1 * 76000 + 1 * 76000 + 4 * 24000-14000, 21S dynein 1, SDS-PAGE
360000
380000
-
cytoplasmic dynein motor domain
385000
390000
-
alpha, 1 * 390000, 12S dynein, no clear intermediate peptides, unidentified lower weight peptides
400000
-
alpha,LC1,LC2, 1 * 400000 + 1 * 22000 + 1 * 18000, 12S dynein
420000
430000
440000
-
alpha,LC1, 1 * 440000 + 1 * 16000, 18S dynein, alpha subunit
450000
500000
-
12S dynein, scanning transmission electron microscopy
550000
-
12S sucrose density gradient fraction, calculated from sedimentation constant (12.3 S) and Stokes radius (10.2 nm)
720000
-
12S dynein 2, analytical gel electrophoreses
1250000
1500000
-
gel filtration
2000000
-
30S dynein, scanning transmission electron microscopy
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
side-chain modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
-
all dyneins share a conserved motor domain. The core of the dynein motor domain consists of six tandem AAA+ ATPase domains. The first AAA+ domain (AAA1) is the primary site of ATP hydrolysis, whereas the other five domains (AAA2-6) have regulatory or structural functions. The dynein linker domain acts as a relatively rigid lever that amplifies small conformational changes in the AAA+ domains upon ATP hydrolysis
-
crystal structure analysis
-
the active sites for microtubule binding and ATP hydrolysis communicate via conformational changes transduced through a ca. 10 nm length antiparallel coilded-coil stalk, which connects the binding domain to the roughly 300 kDa motor core. A balancing of opposing conformations in the stalk and microtubule binding domain (MTBD) enables modest ling-range interactions arising from ATP-binding in the motor core to induce a relaxation of the MTBD into the stable low affinity state
-
hanging-drop method, 1.7 A resolution, dynein light chain TcTex-1
-
hanging-drop vapor diffusion method, dynein light chain Dnlc2A
-
microtubule-binding domain
-
resolution of 6 A of a functional dimer of two ca. 300 kDa motor domains of yeast cytoplasmic dynein, which are dimerized by glutathione S-transferase GST. The structure reveals an unusual asymmetric arrangement of ATPase domains and an unexpected interaction between two coiled coils the create a base for the microtubule binding domain
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
stable up to
additional information
-
thermal denaturation of Tctex-1 is irreversible due to protein aggregation at high temperatures
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unfolding in guanidine-HCl and urea
-
VO43- and Fe(III)-ATP mediate photolysis of dynein heavy chains at specific sites
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, buffered solution with protease inhibitors, 5 days, 20%, -80°C, liqid nitrogen, 6 months, 20%
0°C, several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sephacel, Calmodulin-affinity column, 5-20% sucrose gradient centrifugation
ammonium sulfate precipitation, Sepharose 4B, hydroxyapatite column, 5-20% sucrose density gradient
-
and separation of subunits, i.e. intermediate chains
-
dynein motor domains in which mutations are introduced to block nucleotide binding at each of the fourATPase associated modules
-
extraction of axonemes with high salt, 0.6 M KCl, 5-20% sucrose gradient centrifugation, hydroxylapatite
-
high salt extraction, 0.6 M KCl, DEAE-Sephacel, 5-25% sucrose gradient centrifugation
-
high-salt extraction
high-salt extraction, 0.6 M NaCl, sucrose density gradient
Ciona sp.
-
high-salt extraction, sucrose gradient
low salt extraction, 0.1% Triton X-100, 0.1 mM PMSF, 200 mM sucrose 25 mM potassium glutamate, 1 mM dithiothreitol and 35 mM Tris-HCl, pH 7.9, 5-25% sucrose gradient
-
native native dynein-c from flagella
-
recombinant dynein light chain Dnlc2A
-
S-tag affinity purification
-
sucrose density gradient fractionation, gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dynein light chain Dnlc2A expressed in Escherichia coli
-
dynein motor domain
-
dynein motor domains in which mutations are introduced to block nucleotide binding at each of the fourATPase associated modules
-
expression in HC11 mammary epithelial cells
-
expression of C-terminal 380-kDa motor domain of cytoplasmic dynein heavy chain fused with His6-FLAG-GFP at its N-terminus and BFP at the interior of the AAA2 module, and fused with a His6-FLAG-biotinylation sequence at its N terminus
-
expression of full-length heavy chain and of 380 kDa truncated heavy chain with N-terminal His-FLAG-biotin tandem tags in Dictyostelium discoideum
-
expression of full-length or 380 kDa fragment of dynein heavy chain with His-FLAG-green fluorescent protein tandem tags or with His-FLAG-biotin tandem tags
-
expression of green fluorescent protein/dynein intermediate chain isoforms fusion proteins in PC12 cells
-
recombinant protein
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAkinA
-
kinesin-1 mutant, has normal ATPase activity despite the absence of dynein plus-end accumulation
L1098F
-
mutation in the stem region of dynein heavy chain, suppression of the phenotype of nudF/lis1 loss
R3086C
-
mutation in the end of AAA4 domain of dynein heavy chain, suppression of the phenotype of nudF/lis1 loss. Mutation causes a decrease in the basal level of dynein ATPase activity and an increase in dynein distribution along microtubules
E2022Q
-
mutation in the Walker B motif of the AAA1 module. In the presence of ATP, the mutant is trapped in a single state, D*-ATP. It binds to microtubules with high affintiy, similar to wild-type
K1975T
-
Walker A mutation in the AAA1 module. Mutant tightly binds to microtubules in the presence and absence of ATP. The inhibition of ATP binding to the AAA1 ATPase site by the mutation completely blocks the ATP-induced dissociation of the complex with the microtubules
K2675T
-
Walker A mutation in the AAA1 module. Mutant tightly binds to microtubules in the presence and absence of ATP. Inhibition of ATP binding to the AAA3 ATPase site by the K2675T mutationdoes not block the ATP-induced dissociation of the complex with the microtubules
L3339C/I3517C
-
380-kDa motor domain mutant to introduce disulfide cross-linking
L3339C/Q3510C
-
380-kDa motor domain mutant to introduce disulfide cross-linking
Q3340C/I3513C
-
380-kDa motor domain mutant to introduce disulfide cross-linking
S88A
-
phosphorylation-inactive mutant of dynein light chain 1. Overexpression causes apoptosis and accelerated mammary gland involution, with increased levels of Bcl-2 interacting mediator of cell death
S88E
-
phosphorylation mimicking active mutant, inhibits its interaction with the endogenous dynein light chain 1 as well as with Bcl-2 interacting mediator of cell death
T89A
-
intermediate chain, phosphorylation site
T89D
-
intermediate chain, phosphorylation site
T98E
-
intermediate chain, phosphorylation site
E2488Q
-
mutation in nucleotide-binding domain AAA3
E2819Q
-
mutation in nucleotide-binding domain AAA4
R2209A
-
mutation in AAA1 module, reduced ATPase activity
R2911A
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mutation in AAA3 module, reduced ATPase activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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the straightforward dynein-ATPase assay can be used to obtain data of functional interest in clinical or experimental settings, to test the effect of new drugs that could inhibit dynein-ATPase actitivty and therefor sperm motility
medicine
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redistribution of endoplasmic reticulum during oocyte maturation is dynein-driven and cell cycle-dependent. Role for dynein in the cytoplasmic changes that prepare the oocyte for fertilization