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Literature summary for 6.3.2.61 extracted from

  • Wloga, D.; Rogowski, K.; Sharma, N.; Van Dijk, J.; Janke, C.; Edde, B.; Bre, M.H.; Levilliers, N.; Redeker, V.; Duan, J.; Gorovsky, M.A.; Jerka-Dziadosz, M.; Gaertig, J.
    Glutamylation on alpha-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila (2008), Eukaryot. Cell, 7, 1362-1372.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of GFP-tagged Ttll1p mainly in the basal bodies and of GFP-tagged Ttll9p mainly in the cilia of CU428 and B2086 cells Tetrahymena thermophila

Protein Variants

Protein Variants Comment Organism
additional information disruption of the TTLL1 and TTLL9 genes decrease the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies, in the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs, phenotype, overview Tetrahymena thermophila

Localization

Localization Comment Organism GeneOntology No. Textmining
cilium Ttll9p Tetrahymena thermophila 5929
-
flagellar basal body Ttll1p Tetrahymena thermophila
-
-
microtubule
-
Tetrahymena thermophila 5874
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Tetrahymena thermophila

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + alpha-tubulin + L-glutamate Tetrahymena thermophila glutamylation on alpha-tubulin is not essential but is required for efficiency of assembly and function of a subset of microtubule-based organelles, the spatial restriction of modifying enzymes appears to be a major mechanism that drives differential glutamylation at the subcellular level L-glutamyl-alpha-tubulin + ADP + phosphate
-
?
additional information Tetrahymena thermophila Ttll1p and Ttll9p are tubulin tyrosine ligase domain proteins, that act as alpha-tubulin-preferring glutamyl ligase enzymes, TTLL1- and TLLL9-type enzymes are highly conserved but are absent from higher plants and fungi, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Tetrahymena thermophila
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial purification of recombinant GFP-tagged Ttll1p and GFP-tagged Ttll9p Tetrahymena thermophila

Reaction

Reaction Comment Organism Reaction ID
ATP + [tubulin]-L-glutamate + L-glutamate = [tubulin]-(gamma-L-glutamyl)-L-glutamate + ADP + phosphate the enzymatic mechanism of microtubule glutamylation involves two distinct steps: initiation and elongation Tetrahymena thermophila

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + alpha-tubulin + L-glutamate glutamylation on alpha-tubulin is not essential but is required for efficiency of assembly and function of a subset of microtubule-based organelles, the spatial restriction of modifying enzymes appears to be a major mechanism that drives differential glutamylation at the subcellular level Tetrahymena thermophila L-glutamyl-alpha-tubulin + ADP + phosphate
-
?
ATP + alpha-tubulin + L-glutamate in an in vitro microtubule glutamylation assay, Ttll1p shows a chain-initiating activity while Ttll9p has primarily a chain-elongating activity. MALDI-TOF mass spectrometry analysis of glutamylated forms of ciliary alpha-tubulin Tetrahymena thermophila L-glutamyl-alpha-tubulin + ADP + phosphate
-
?
additional information Ttll1p and Ttll9p are tubulin tyrosine ligase domain proteins, that act as alpha-tubulin-preferring glutamyl ligase enzymes, TTLL1- and TLLL9-type enzymes are highly conserved but are absent from higher plants and fungi, overview Tetrahymena thermophila ?
-
?

Synonyms

Synonyms Comment Organism
alpha-tubulin-preferring glutamyl ligase
-
Tetrahymena thermophila
More tubulin glutamylases belong to the family of TTL domain-carrying proteins named TTLL proteins Tetrahymena thermophila
TTL domain protein
-
Tetrahymena thermophila
Ttll1p
-
Tetrahymena thermophila
Ttll9p
-
Tetrahymena thermophila
tubulin glutamylase
-
Tetrahymena thermophila
tubulin tyrosine ligase domain protein
-
Tetrahymena thermophila

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Tetrahymena thermophila

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Tetrahymena thermophila

Cofactor

Cofactor Comment Organism Structure
ATP
-
Tetrahymena thermophila