The phylogenetic distribution of tubulin:Tyrosine ligase

Preston, Susan F.; Deanin, Grace G.; Hanson, Rolf K.; Gordon, Malcolm W.

doi:10.1007/bf01739482

Cited by 46 publications

(23 citation statements)

References 25 publications

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“…However, tubulin tyrosine-ligase was not found at this time in Tetruhymena and yeast, and only a low level, at best, was observed in sea urchins [53]. Others reported the absence of tubulin tyrosine-ligase from invertebrate tissues [54] but it was eventually shown that if the enzyme is partially purified it can be detected easily in invertebrates, even though it still was not seen in Teti-ahymena [55]. Tubulin tyrosine-ligase is now known to enjoy a wide phylogenetic distribution.…”

Section: Tubulin Tyrosine-ligasementioning

confidence: 77%

Tubulin Post‐Translational Modifications

MacRae

1997

European Journal of Biochemistry

279

191

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This review describes the enzymes responsible for the post-translational modifications of tubulin, including detyrosinationltyrosination, acetylationldeacetylation, phosphorylation, polyglutamylation, polyglycylation and the generation of non-tyrosinatable a-tubulin. Tubulin tyrosine-ligase, which reattaches tyrosine to detyrosinated tubulin, has been extensively characterized and its gene sequenced. Enzymes such as tubulin-specific carboxypeptidase and a-tubulin acetyltransferase, required, respectively, for detyrosination and acetylation of tubulin, have yet to be purified to homogeneity and examined in defined systems. This has produced some conflicting results, especially for the carboxypeptidase. The phosphorylation of tubulin by several different types of kinases has been studied in detail but drawing conclusions is difficult because many of these enzymes modify proteins other than their actual substrates, an especially pertinent consideration for in vitro experiments. Tubulin phosphorylation in cultured neuronal cells has proven to be the best model for evaluation of kinase effects on tubulinlmicrotubule function. There is little information on the enzymes required for polyglutamylation, polyglycylation, and production of non-tyrosinatable tubulin, but the available data permit interesting speculation of a mechanistic nature. Clearly, to achieve a full appreciation of tubulin post-translational changes the responsible enzymes must be characterized. Knowing when the enzymes are active in cells, if soluble or polymerized tubulin is the preferred substrate and the amino acid residues modified by each enzyme are all important. Moreover, acquisition of purified enzymes will lead to cloning and sequencing of their genes. With this information, one can manipulate cell genomes in order to either modify key enzymes or change their relative amounts, and perhaps reveal the physiological significance of tubulin post-translational modifications.Keywords: tubulin; microtubule ; post-translational modification ; tyrosination ; detyrosination ; non-tyrosinatable ; acetylation; phosphorylation; polyglutamylation ; polyglycylation.Of the three major isotypes of tubulin in eukaryotic cells, atubulin and P-tubulin form heterodimeric complexes which associate head-to-tail into protofilaments and then laterally to make up the wall of the cylindrical microtubule [I-31. The third isotype, y-tubulin, appears in the cytosol and in microtubule-organizing centers as ring-shaped structures where it nucleates microtubules [4-61. Both a-tubulin and P-tubulin, and perhaps y-tubulin [7], exist within most eukaryotic cells as families of closely related isoforms. Isotubulin composition varies spatially and temporally, determined by differential transcription of a-tubulin and P-tubulin genes within small families [2,8,91 and by post-translational modifications of tubulin [I, 8, lo].

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Section: Tubulin Tyrosine-ligasementioning

confidence: 77%

Tubulin Post‐Translational Modifications

MacRae

1997

European Journal of Biochemistry

279

191

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“…The terminal tyrosine on a-tubulin can be both removed and replaced by enzymes originally found in rat brain (3,5,6) and since found in many other tissues and species (18,46,51). Although the presence or absence of the terminal tyrosine does not seem to alter the in vitro assembly properties of tubulin (2), the fraction of tyrosinated tubulin is different in assembled and unassembled pools (53).…”

Section: Discussionmentioning

confidence: 99%

Two functional alpha-tubulin genes of the yeast Saccharomyces cerevisiae encode divergent proteins.

Schatz¹,

Pillus²,

P³

et al. 1986

Mol. Cell. Biol.

172

112

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Two a-tubulin genes from the budding yeast Saccharomyces cerevisiae were identified and cloned by cross-species DNA homology. Nucleotide sequencing studies revealed that the two genes, named TUB) and TUB3, encoded gene products of 447 and 445 amino acids, respectively, that are highly homologous to oe-tubulins from other species. Comparison of the sequences of the two genes revealed a 19% divergence between the nucleotide sequences and a 10% divergence between the amino acid sequences. Each gene had a single intervening sequence, located at an identical position in codon 9. Cell fractionation studies showed that both gene products were present in yeast microtubules. These two genes, along with the TUB2 1-tubulin gene, probably encode the entire complement of tubulin in budding yeast cells.The process of cell division has been studied extensively in the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe. A particularly useful technique has been the isolation of conditional lethal mutants that arrest at specific morphological stages of the cell cycle (23,35,38,39,47,56,70). The normal function of the mutant gene product in such cell cycle mutants has, unfortunately, been discovered in relatively few instances. To define the role of these gene products in the mechanism of cell division, it will be essential to combine the genetic approach with biochemical and morphological analysis. Yeasts have become favorite organisms for such studies because of ease of growth and manipulation, because of the sophisticated recombinant DNA and classic genetic techniques that have been developed (11,61), and because of the successful application of such techniques as electron microscopy and immunofluorescence (1,13,26,27,34,42).One of the proteins whose function in the cell division cycle is best understood is the a,,-tubulin heterodimer, which polymerizes to form the microtubules found in most eucaryotic cells (63). By electron and light microscopy, microtubules in yeast have been observed to be elements of structures involved in chromosome and nuclear movement (1,13,26,27,34,42

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“…The resulting detyrosinated tubulin exposes a carboxy-terminal glutamic acid and is therefore referred to as Glu-tubulin. Tubulin tyrosination is known to occur in a great variety of species ranging from humans 32 to invertebrates such as trypanosomes. 33 However, although yeast cells encode a C-terminal tyrosine (Schizosaccharomyces pombe) or a phenylalanine (Saccharomyces cerevisiae), the tyrosination cycle itself does not exist in these species.…”

Section: The Tubulin Tyrosination Cyclementioning

confidence: 99%

Miniaturization and Validation of a Sensitive Multiparametric Cell-Based Assay for the Concomitant Detection of Microtubule-Destabilizing and Microtubule-Stabilizing Agents

Vassal¹,

Barette²,

Fonrose³

et al. 2006

SLAS Discovery

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The authors describe a cell-based assay for anti-microtubule compounds suitable for automation. This assay allows the identification, in a single screening campaign, of both microtubule-destabilizing and microtubule-stabilizing agents. Its rationale is based on the substrate properties of the tubulin-modifying enzymes involved in the tubulin tyrosination cycle. This cycle involves the removal of the C-terminal tyrosine of the tubulin α-subunit by an ill-defined tubulin carboxypeptidase and its readdition by tubulin tyrosine ligase. Because of the substrate properties of these enzymes, dynamic microtubules, sensitive to depolymerizing drugs, are composed of tyrosinated tubulin, whereas nondynamic, stabilized microtubules are composed of detyrosinated tubulin. Thus depolymerization or stabilization of the microtubule network can easily be detected with doubleimmunofluorescence staining using antibodies specific to tyrosinated and detyrosinated tubulin. The authors have scaled this assay to the 96-well plate format and adapted its process for an automated handling, including a readout using a microplate reader. They describe the different steps of this adaptation. This assay was validated using known compounds. This new cellbased assay represents an alternative to both global cytotoxicity assays and in vitro tubulin assembly assays commonly used for the detection of microtubule poisons. (Journal of Biomolecular Screening 2006:377-389)

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The phylogenetic distribution of tubulin:Tyrosine ligase

Cited by 46 publications

References 25 publications

Tubulin Post‐Translational Modifications

Tubulin Post‐Translational Modifications

Two functional alpha-tubulin genes of the yeast Saccharomyces cerevisiae encode divergent proteins.

Miniaturization and Validation of a Sensitive Multiparametric Cell-Based Assay for the Concomitant Detection of Microtubule-Destabilizing and Microtubule-Stabilizing Agents

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