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Information on EC 5.6.1.1 - microtubule-severing ATPase and Organism(s) Caenorhabditis elegans and UniProt Accession P34808
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5.6.1.1 microtubule-severing ATPaseIUBMB Comments
A member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
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Word Map
- 5.6.1.1
- spastic
- hereditary
- kinesins
- paraplegia
-
mitotic
- cortical
- cytoskeleton
-
disassembly
- centrosome
- gelsolin
-
corticospinal
- atpases
- cytokine
- paraparesis
-
atlastin
-
microtubule-based
-
actin-binding
-
microtubule-binding
-
escrt-iii
-
antimitotic
-
axonopathy
-
minus-ends
- gamma-tubulin
-
kinesin-related
-
plus-ends
-
mt-associated
-
microtubule-dependent
-
phragmoplasts
- midbody
- medicine
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
n
+
n
+
a microtubule
=
n
+
n
+
(n+1)
alpha/beta tubulin heterodimers
Synonyms
spastin, katanin, scinderin, kinesin spindle protein, mei-1, adseverin, katanin p60, microtubule-severing protein, microtubule-stimulated atpase, p60-katanin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
katanin
SPAS-1
spastin
katanin
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (tubulin-dimerizing)
A member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
assembly of female meiotic spindles requires MEI-1 and MEI-2, which constitute the microtubule-severing AAA+ ATPase Katanin
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
additional information
?
-
-
direct role of microtubule severing in translocation of the meiotic spindle to the cortex
-
-
?
additional information
?
-
-
the enzyme has multiple effects on microtubules in vitro. Purified MEI-1/MEI-2 complexes preferentially sever at intersections between two microtubules and directly bundle microtubules in vitro. These activities promote parallel/antiparallel microtubule organization in meiotic spindles, MEI-1/MEI-2 complexes bundle microtubules and preferentially sever at intersections between two microtubules in vitro
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
assembly of female meiotic spindles requires MEI-1 and MEI-2, which constitute the microtubule-severing AAA+ ATPase Katanin
-
-
?
additional information
?
-
-
direct role of microtubule severing in translocation of the meiotic spindle to the cortex
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sb26
-
mutation in the tbb-2 beta-tubulin gene that partially inhibits MEI-1/MEI-2 activity
-
additional information
in solution, wild-type katanin is in an autoinhibited state in the presence or absence of nucleotide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
microtubules
-
SPAS-1's ATPase activity increases with increasing concentrations of microtubules up to 0.00025 mM and then declines at higher microtubule concentrations. In the presence of 0.00025 mM microtubules, ATPase activity is 7times higher than in the absence of microtubules
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
variants show disorganized microtubules that lack focused spindle poles reminiscent of the Katanin loss-of-function phenotype, demonstrating that the microtubule-severing activity is essential for meiotic spindle assembly in Caenorhabditis elegans
physiological function
assembly of female meiotic spindles requires MEI-1 and MEI-2, which constitute the microtubule-severing AAA+ ATPase Katanin
malfunction
-
rapid inactivation of katanin results in complete loss of ASPM-1 positive spindle poles. Strong loss-of-function mutants assemble apolar intersecting microtubule arrays, whereas weaker mutants assemble bipolar meiotic spindles that are longer than wild-type. Microtubule disassembly in enzyme point mutants, overview. Progressive loss of katanin leads to a progressive loss in the organization of pole-to-pole microtubule bundles, phenotypes
physiological function
physiological function
-
SPAS-1 shows microtubule-severing activity when expresses in cultured cells. When alpha/beta tubulin dimer is incubated with SPAS-1, tubulin is pulled down with SPAS-1, suggesting the Caenorhabditis elegans SPAS-1 binds to tubulin
physiological function
-
katanin maintains meiotic metaphase chromosome alignment and spindle structure in vivo. Assembly of Caenorhabditis elegans female meiotic spindles requires both MEI-1 and MEI-2 subunits of the microtubule-severing ATPase katanin. A linear relationship between in vitro microtubule disassembly rates and in vivo spindle length exists
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KTNA1_CAEEL
472
0
51739
Swiss-Prot
other Location (Reliability: 2), other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
SPAS-1S, consists of eight exons, determined by SDS-PAGE and Western blotting
52000
-
1 * 52000, SDS-PAGE, when low concentrations of SPAS-1 (below 0.55 mg/ml) are analyzed, stable hexamers are not formed, rather it shows a broad elution profile over monomer to hexamer, even in the presence of ATP
57000
-
SPAS-1L, consists of nine exons, determined by SDS-PAGE and Western blotting
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
heterotetramer of KATNAL1/B1 (an ATPase associated with diverse cellular activities) and the regulatory subunit con80. It does not assemble beyond a dimer of heterodimers (heterotetramer), even at concentrations up to 0.05 mM
hexamer
MEI-2 subunit stabilizes the MEI-1 hexamer for optimal ATP-dependent microtubule severing
dimer
heterodimer
hexamer
-
SPAS-1 forms a stable hexamer in a concentration-dependent manner. The microtubule binding domain MTBD of SPAS-1 plays a critical role in enrichment of SPAS-1 to microtubules, where SPAS-1 is concentrated above 5 mg/ml and able to form a stable hexamer. Hexamer formation takes place in an ATP-independent manner
monomer
-
1 * 52000, SDS-PAGE, when low concentrations of SPAS-1 (below 0.55 mg/ml) are analyzed, stable hexamers are not formed, rather it shows a broad elution profile over monomer to hexamer, even in the presence of ATP
heterodimer
-
catalytic and non-catalytic domain together form hexameric rings
heterodimer
-
MEI-1 and MEI-2 are the Caenorhabditis elegans homologs of the p60 (catalytic) and the p80 (localization) subunits
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method at 20°C, crystal structure of MEI-1 AAA ATPase in the ADP-bound state reveals a pseudo-hexameric left-handed spiral assembly
secondary structure analyzed by circular dichroism (CD) spectrum. SPAS-1 retains a high degree of alpha-helical structure
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K437P/K441P
predicted not to form the C-terminal alpha-helix, microtuble network remains in mutant protein expressing HEK293 cells
additional information
additional information
-
homozygotic gene disruption mutants, meiotic spindles move to the cortex, but association with cortex is unstable
additional information
-
mei-1(null): mutant lacking katanin activity, mei-1(gf): gain-of-function mutant
additional information
-
mutational analysis reveals that the conserved exposed, basic amino acid residues in the pore region of stastin as well as the aromatic residue are important for the recognition and severing of microtubules. The conformational change of W251 is detected upon ATP binding by measuring the fluorescence emission spectra of tryptophan. Given that K257 is located close to the corresponding aromatic residue W251, it seems possible that K257 is also involved in a mechanochemical process from conformational change of W251 in microtubule severing
additional information
C-terminal deletion mutants: 1-432, 1-435, 1-447, C-terminal alpha-helix is essential for microtuble severing
additional information
-
C-terminal deletion mutants: 1-432, 1-435, 1-447, C-terminal alpha-helix is essential for microtuble severing
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47
-
the melting temperature Tm is estimated from the denaturation curve
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant untagged short isoform of MEI-1 subunit and MBP-TEV-tagged MEI-2 subunit from Escherichia coli by amylose affinity chromatography, eluted with TEV protease
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the selenomethionine-substituted (Se-MEI-1/MEI-2) katanin complex in Escherichia coli BL21
expressed in Escherichia coli BL21(DE3), FLAG tagged versions expressed in HEK293 cells
recombinant expression of untagged short isoform of MEI-1 subunit, coexpression with MBP-TEV-tagged MEI-2 subunit, in Escherichia coli
-
SPAS-1 protein (451 amino acid reisdues) is produced as an N-terminally His6-tagged recombinant protein, expressed in Escherichia coli BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hartman, J.J.; Mahr, J.; McNally, K.; Okawa, K.; Iwamatsu, A.; Thomas, S.; Cheesman, S.; Heuser, J.; Vale, R.D.; McNally, F.J.
Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit
Cell
93
277-287
1998
Saccharomyces cerevisiae, Caenorhabditis elegans, Dictyostelium sp., Drosophila sp. (in: flies), Homo sapiens, Strongylocentrotus purpuratus, Xenopus laevis
McNally, F.J.; Thomas, S.
Katanin is responsible for the M-phase microtubule-severing activity in Xenopus eggs
Mol. Biol.
9
1847-1861
1998
Caenorhabditis elegans, Gallus gallus, Chlamydomonas reinhardtii, Mus musculus, Strongylocentrotus purpuratus, Xenopus laevis, Homo sapiens (O75449), Homo sapiens
Quarmby, L.
Cellular Samurai: katanin and the severing of microtubules
J. Cell Sci.
113
2821-2827
2000
Arabidopsis sp., Caenorhabditis elegans, Chlamydomonas reinhardtii, Drosophila sp. (in: flies), Homo sapiens, no activity in Saccharomyces cerevisiae, Xenopus laevis
Yang, H.Y.; McNally, K.; McNally, F.J.
MEI-1/katanin is required for translocation of the meiosis I spindle to the oocyte cortex in C. elegans
Dev. Biol.
260
245-259
2003
Caenorhabditis elegans
Srayko, M.; Otoole, E.T.; Hyman, A.A.; Mueller-Reichert, T.
Katanin disrupts the microtubule lattice and increases polymer number in C. elegans meiosis
Curr. Biol.
16
1944-1949
2006
Caenorhabditis elegans
Ribbeck, K.; Mitchison, T.J.
Meiotic spindle: sculpted by severing
Curr. Biol.
16
R923-R925
2006
Caenorhabditis elegans
Lu, C.; Srayko, M.; Mains, P.E.
The Caenorhabditis elegans microtubule-severing complex MEI-1/MEI-2 katanin interacts differently with two superficially redundant beta-tubulin isotypes
Mol. Biol. Cell
15
142-150
2004
Caenorhabditis elegans
Matsushita-Ishiodori, Y.; Yamanaka, K.; Ogura, T.
The C. elegans homologue of the spastic paraplegia protein, spastin, disassembles microtubules
Biochem. Biophys. Res. Commun.
359
157-162
2007
Caenorhabditis elegans
Matsushita-Ishiodori, Y.; Yamanaka, K.; Hashimoto, H.; Esaki, M.; Ogura, T.
Conserved aromatic and basic amino acid residues in the pore region of Caenorhabditis elegans spastin play critical roles in microtubule severing
Genes Cells
14
925-940
2009
Caenorhabditis elegans
Onitake, A.; Matsushita-Ishiodori, Y.; Johjima, A.; Esaki, M.; Ogura, T.; Yamanaka, K.
The C-terminal alpha-helix of SPAS-1, a Caenorhabditis elegans spastin homologue, is crucial for microtubule severing
J. Struct. Biol.
179
138-142
2012
Caenorhabditis elegans (Q8MNV0), Caenorhabditis elegans
McNally, K.; Berg, E.; Cortes, D.B.; Hernandez, V.; Mains, P.E.; McNally, F.J.
Katanin maintains meiotic metaphase chromosome alignment and spindle structure in vivo and has multiple effects on microtubules in vitro
Mol. Biol. Cell
25
1037-1049
2014
Caenorhabditis elegans
Joly, N.; Martino, L.; Gigant, E.; Dumont, J.; Pintard, L.
Microtubule-severing activity of the AAA+ ATPase Katanin is essential for female meiotic spindle assembly
Development
143
3604-3614
2016
Caenorhabditis elegans (P34808), Caenorhabditis elegans
EXTERNAL LINKS (specific for EC-Number 5.6.1.1)
Transporter Classification Database (TCDB): 1.R.1.1.1
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