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Literature summary for 2.3.1.108 extracted from

  • Akella, J.S.; Wloga, D.; Kim, J.; Starostina, N.G.; Lyons-Abbott, S.; Morrissette, N.S.; Dougan, S.T.; Kipreos, E.T.; Gaertig, J.
    MEC-17 is an alpha-tubulin acetyltransferase (2010), Nature, 467, 218-222.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of GST-tagged Mec-17 in Escherichia coli strain BL21 Mus musculus
MEC-17 sequences are absent from Chlamydomonas reinhardtii, an organism that has alphaTAT activity Chlamydomonas reinhardtii

Localization

Localization Comment Organism GeneOntology No. Textmining
flagellum
-
Chlamydomonas reinhardtii
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + [alpha-tubulin]-L-lysine Chlamydomonas reinhardtii acetylation of the epsilon-amino group of Lys40 CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine Mus musculus acetylation of the epsilon-amino group of Lys40 CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine Caenorhabditis elegans acetylation of the epsilon-amino group of Lys40 CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine Danio rerio acetylation of the epsilon-amino group of Lys40 CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine Tetrahymena thermophila acetylation of the epsilon-amino group of Lys40, in Tetrahymena, alpha-tubulin is the major if not the only substrate of MEC-17-dependent K acetylation CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
additional information Caenorhabditis elegans wild-type adults have a strong signal for acetylated alpha-tubulin in the six touch receptor neurons ?
-
?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-
Chlamydomonas reinhardtii
-
-
-
Danio rerio
-
-
-
Mus musculus
-
-
-
Tetrahymena thermophila
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged Mec-17 from Escherichia coli strain BL21 by glutathione affinity chromatography Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Danio rerio
-
neuron peripheral, acetyl-K40 alpha-tubulin is enriched in cilia and axons of neurons Danio rerio
-
optic nerve
-
Danio rerio
-
spinal cord
-
Danio rerio
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + [alpha-tubulin]-L-lysine acetylation of the epsilon-amino group of Lys40 Chlamydomonas reinhardtii CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine acetylation of the epsilon-amino group of Lys40 Mus musculus CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine acetylation of the epsilon-amino group of Lys40 Caenorhabditis elegans CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine acetylation of the epsilon-amino group of Lys40 Tetrahymena thermophila CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine acetylation of the epsilon-amino group of Lys40 Danio rerio CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine acetylation of the epsilon-amino group of Lys40, in Tetrahymena, alpha-tubulin is the major if not the only substrate of MEC-17-dependent K acetylation Tetrahymena thermophila CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
?
additional information wild-type adults have a strong signal for acetylated alpha-tubulin in the six touch receptor neurons Caenorhabditis elegans ?
-
?
additional information in vitro, MEC-17 exclusively acetylates Lys40 of alpha-tubulin Caenorhabditis elegans ?
-
?
additional information recombinant GST-MEC-17 directly acetylates purified tubulin from the MEC17-KO strain in vitro Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
alpha-TAT
-
Chlamydomonas reinhardtii
alpha-TAT
-
Mus musculus
alpha-TAT
-
Caenorhabditis elegans
alpha-TAT
-
Tetrahymena thermophila
alpha-TAT
-
Danio rerio
alpha-tubulin acetyltransferase
-
Chlamydomonas reinhardtii
alpha-tubulin acetyltransferase
-
Mus musculus
alpha-tubulin acetyltransferase
-
Caenorhabditis elegans
alpha-tubulin acetyltransferase
-
Tetrahymena thermophila
alpha-tubulin acetyltransferase
-
Danio rerio
Mec-17
-
Mus musculus
Mec-17
-
Caenorhabditis elegans
Mec-17
-
Tetrahymena thermophila
Mec-17
-
Danio rerio

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Chlamydomonas reinhardtii
8
-
assay at Mus musculus
8
-
assay at Caenorhabditis elegans
8
-
assay at Tetrahymena thermophila
8
-
assay at Danio rerio

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Chlamydomonas reinhardtii
acetyl-CoA
-
Mus musculus
acetyl-CoA
-
Caenorhabditis elegans
acetyl-CoA
-
Tetrahymena thermophila
acetyl-CoA
-
Danio rerio

Expression

Organism Comment Expression
Tetrahymena thermophila construction of a Mec-17 disruption mutant. The MEC-17-KO Tetrahymena cells have a normal growth rate, but theMEC-17-KOcells grow more slowly than wild type on medium with the microtubule depolymerizing compound oryzalin. Conversely, the MEC-17 KO cells grew faster than wild-type cells in medium with paclitaxel, a microtubule-stabilizing drug. This drug phenotype is consistent with an increase in dynamics of microtubules in MEC17-KO cells additional information

General Information

General Information Comment Organism
evolution MEC-17 is related to the Gcn5 histone acetyltransferases Mus musculus
evolution MEC-17 is related to the Gcn5 histone acetyltransferases Caenorhabditis elegans
evolution MEC-17 is related to the Gcn5 histone acetyltransferases Tetrahymena thermophila
evolution MEC-17 is related to the Gcn5 histone acetyltransferases Danio rerio
malfunction disruption of the Tetrahymena MEC-17 gene, resulting in a marked loss of acetyl-K40 in Tetrahymena cells, phenocopies the K40R alpha-tubulin mutation and makes microtubules more labile. Overexpression of GFP-Mec17p in Tetrahymena greatly increases acetylation of microtubules Tetrahymena thermophila
malfunction MEC-12 is the only alpha-tubulin with K40, and mec-12(e1607) probable null allele worms have greatly reduced touch responses. Intergration of single transgenes encoding MEC-12 with either wild-type K40 or K40R or K40Q substitutions into the mec-12(e1607)mutant using Mos1 transposon excision repair restores the levels of touch response to 80% of wild type level,whereas animals with either MEC-12-K40R or MEC-12-K40Q show reduced touch response, overview Caenorhabditis elegans
malfunction zebrafish embryos depleted in MEC-17 show a dramatic loss of acetyl-K40 in neurons but not in cilia. Depletion of MEC-17 in zebrafish, by injection with random sequence morpholinos or 5-bp mismatched morpholinos, produces phenotypes consistent with neuromuscular defects Danio rerio
additional information MEC-17 sequences are absent from Chlamydomonas reinhardtii, an organism that has alphaTAT activity Chlamydomonas reinhardtii
physiological function MEC-17 is required for the function of touch receptor neurons in Caenorhabditis elegans and acts as a K40-specific acetyltransferase for alpha-tubulin. W06B11.1 os also required for acetylation of K40 and contribute to touch sensation Caenorhabditis elegans
physiological function the K40 residue of alpha-tubulin is important in vertebrates, acetyl-K40-carrying microtubules are abundant in the nervous system, including the brain, optical nerves, spinal cord, and axons of peripheral nerves. MEC-17 is required for K40 acetylation in zebrafish and normal embryonic development Danio rerio
physiological function the K40 residue of alpha-tubulin is important in vertebrates, MEC-17 controls the levels of microtubule acetylation in mammalian cells Mus musculus
physiological function the K40 residue of alpha-tubulin is not required for survival in protists, such as Chlamydomonas Chlamydomonas reinhardtii
physiological function the K40 residue of alpha-tubulin is not required for survival in protists, such as Tetrahymena Tetrahymena thermophila