New tubulins in protozoal parasites

Vaughan, Susan; Attwood, Teresa K.; Navarro, Miguel; Scott, Valerie; McKean, Paul G.; Gull, Keith

doi:10.1016/s0960-9822(00)00414-0

Cited by 48 publications

(34 citation statements)

References 12 publications

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“…1). This organization is similar to that seen for many eukaryotic ␣ and ␤ tubulins, whereby the genes are arranged within the genome as pairs or clusters (18). Interestingly, gene walking revealed a third ORF downstream of btubb (Fig.…”

Section: Resultssupporting

confidence: 72%

Genes for the cytoskeletal protein tubulin in the bacterial genus Prosthecobacter

Jenkins

Samudrala

Anderson

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

160

132

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Tubulins, the protein constituents of the microtubule cytoskeleton, are present in all known eukaryotes but have never been found in the Bacteria or Archaea. Here we report the presence of two tubulin-like genes [bacterial tubulin a (btuba) and bacterial tubulin b (btubb)] in bacteria of the genus Prosthecobacter (Division Verrucomicrobia). In this study, we investigated the organization and expression of these genes and conducted a comparative analysis of the bacterial and eukaryotic protein sequences, focusing on their phylogeny and 3D structures. The btuba and btubb genes are arranged as adjacent loci within the genome along with a kinesin light chain gene homolog. RT-PCR experiments indicate that these three genes are cotranscribed, and a probable promoter was identified upstream of btuba. On the basis of comparative modeling data, we predict that the Prosthecobacter tubulins are monomeric, unlike eukaryotic ␣ and ␤ tubulins, which form dimers and are therefore unlikely to form microtubule-like structures. Phylogenetic analyses indicate that the Prosthecobacter tubulins are quite divergent and do not support recent horizontal transfer of the genes from a eukaryote. The discovery of genes for tubulin in a bacterial genus may offer new insights into the evolution of the cytoskeleton.

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Section: Resultssupporting

confidence: 72%

Genes for the cytoskeletal protein tubulin in the bacterial genus Prosthecobacter

Jenkins

Samudrala

Anderson

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

160

132

View full text Add to dashboard Cite

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“…It is found in the genomes of other organisms with triplet microtubules (Chang and Stearns, 2000;Vaughan et al, 2000;Smrzka et al, 2000) but it is not present in the genomes of D. melanogaster (Adams et al, 2000;Celniker et al, 2002) or C. elegans (The C. elegans Sequencing Consortium, 1998). Cells with the δ-tubulin gene deleted (uni3-1) have flagellar, basal body and cell division defects.…”

Section: )mentioning

confidence: 99%

Mutations in α-tubulin promote basal body maturation and flagellar assembly in the absence of δ-tubulin

Fromherz

Giddings

Gomez‐Ospina

et al. 2004

Journal of Cell Science

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We have isolated suppressors of the deletion allele of δ-tubulin, uni3-1, in the biflagellate green alga Chlamydomonas reinhardtii. The deletion of δ-tubulin produces cells that assemble zero, one or two flagella and have basal bodies composed primarily of doublet rather than triplet microtubules. Flagellar number is completely restored in the suppressed strains. Most of the uni3-1 suppressors map to the TUA2 locus, which encodes α2-tubulin. Twelve independent tua2 mutations were sequenced. Amino acids D205 or A208, which are nearly invariant residues in α-tubulin, were altered. The tua2 mutations on their own have a second phenotype - they make the cells colchicine supersensitive. Colchicine supersensitivity itself is not needed for suppression and colchicine cannot phenocopy the suppression. The suppressors partially restore the assembly of triplet microtubules. These results suggest that the δ-tubulin plays two roles: it is needed for extension or stability of the triplet microtubule and also for early maturation of basal bodies. We suggest that the mutant α-tubulin promotes the early maturation of the basal body in the absence of δ-tubulin, perhaps through interactions with other partners, and this allows assembly of the flagella.

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“…In addition to the ubiquitous α and β-tubulin, MTs often require the presence of an additional tubulin protein,'γ-tubulin, for correct assembly as a templating protein (Erickson, 2000;Luduena, 1998). Two additional tubulins, designated δ and ε, have also been characterized and although their role in MT assembly remains uncertain (Vaughan, 2000), models of their function in MT assembly have been proposed (Inclan and Nogales, 2001).…”

Section: Introductionmentioning

confidence: 99%

The evolution of the structure of tubulin and its potential consequences for the role and function of microtubules in cells and embryos

et al. 2006

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This paper discusses the results of homology modeling and resulting calculation of key structural and physical properties for close to 300 tubulin sequences, including α α α α α, β β β β β, γ γ γ γ γ, δ δ δ δ δ and ε ε ε ε ε -tubulins. The basis for our calculations was the structure of the tubulin dimer In addition to the general structural trends between tubulin isoforms, we have observed that the carboxy-termini of α α α α α and β β β β β-tubulin exists in at least two stable configurations, either projecting away from the tubulin (or microtubule) surface, or collapsed onto the surface. In the latter case, the carboxy-termini form a lattice distinctly different from that of the well-known A and B lattices formed by the tubulin subunits. However, this C-terminal lattice is indistinguishable from the lattice formed when the microtubule-associated protein tau binds to the microtubule surface. Finally, we have discussed how tubulin sequence diversity arose in evolution giving rise to its particular phylogeny and how it may be used in cell-and tissue-specific expression including embryonal development.

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New tubulins in protozoal parasites

Cited by 48 publications

References 12 publications

Genes for the cytoskeletal protein tubulin in the bacterial genus Prosthecobacter

Genes for the cytoskeletal protein tubulin in the bacterial genus Prosthecobacter

Mutations in α-tubulin promote basal body maturation and flagellar assembly in the absence of δ-tubulin

The evolution of the structure of tubulin and its potential consequences for the role and function of microtubules in cells and embryos

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