A codon change in beta-tubulin which drastically affects microtubule structure in Drosophila melanogaster fails to produce a significant phenotype in Saccharomyces cerevisiae

1991 ◽  
Vol 11 (9) ◽  
pp. 4726-4731
Author(s):  
V Praitis ◽  
W S Katz ◽  
F Solomon
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Eukaryotic Cells ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Cell Biol ◽  
Codon Change ◽  
Almost All ◽  
Beta Tubulin Gene ◽  
Microtubule Structure

The relative uniformity of microtubule ultrastructure in almost all eukaryotic cells is thought to be a consequence of the conserved elements of tubulin sequence. In support of this idea, a mutation in a beta-tubulin gene of Drosophila melanogaster, occurring at a highly conserved position, produces U-shaped microtubules, suggesting a defect in either nucleation or packing during assembly (M. T. Fuller, J. H. Caulton, J. A. Hutchens, T. C. Kaufman, and E. C. Raff, J. Cell Biol. 104:385-394, 1987, and J. E. Rudolph, M. Kimble, H. D. Hoyle, M. A. Subler, and E. C. Raff, Mol. Cell. Biol. 7:2231-2242, 1987). Surprisingly, we find that introducing the same mutation into the sole beta-tubulin gene of Saccharomyces cerevisiae has virtually no consequences for microtubule structure or function in that organism.

scholarly journals A codon change in beta-tubulin which drastically affects microtubule structure in Drosophila melanogaster fails to produce a significant phenotype in Saccharomyces cerevisiae.

1991 ◽  
Vol 11 (9) ◽  
pp. 4726-4731 ◽  
Author(s):  
V Praitis ◽  
W S Katz ◽  
F Solomon
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Eukaryotic Cells ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Cell Biol ◽  
Codon Change ◽  
Almost All ◽  
Beta Tubulin Gene ◽  
Microtubule Structure

The relative uniformity of microtubule ultrastructure in almost all eukaryotic cells is thought to be a consequence of the conserved elements of tubulin sequence. In support of this idea, a mutation in a beta-tubulin gene of Drosophila melanogaster, occurring at a highly conserved position, produces U-shaped microtubules, suggesting a defect in either nucleation or packing during assembly (M. T. Fuller, J. H. Caulton, J. A. Hutchens, T. C. Kaufman, and E. C. Raff, J. Cell Biol. 104:385-394, 1987, and J. E. Rudolph, M. Kimble, H. D. Hoyle, M. A. Subler, and E. C. Raff, Mol. Cell. Biol. 7:2231-2242, 1987). Surprisingly, we find that introducing the same mutation into the sole beta-tubulin gene of Saccharomyces cerevisiae has virtually no consequences for microtubule structure or function in that organism.

scholarly journals Diversity among beta-tubulins: a carboxy-terminal domain of yeast beta-tubulin is not essential in vivo.

1988 ◽  
Vol 8 (7) ◽  
pp. 2730-2736 ◽  
Author(s):  
W S Katz ◽  
F Solomon
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Meiotic Division ◽  
Functional Significance ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal ◽  
Beta Tubulin Gene

Sequences of genes for beta-tubulins from many different organisms demonstrate that they encode highly conserved proteins but that these proteins diverge considerably at their carboxyl termini. The patterns of interspecies conservation of this diversity suggest that it may have functional significance. We have taken advantage of the properties of Saccharomyces cerevisiae to test this hypothesis in vivo. The sole beta-tubulin gene of this species is one of the most divergent of all beta-tubulins and encodes 12 amino acids which extend past the end of most other beta-tubulin molecules. We have constructed strains in which the only beta-tubulin gene is an allele lacking these 12 codons. We show here that this carboxy-terminal extension is not essential. The absence of these 12 amino acids had no effect on a number of microtubule-dependent functions, such as mitotic and meiotic division and mating. It did confer dominant supersensitivity to a microtubule-depolymerizing drug.

Diversity among beta-tubulins: a carboxy-terminal domain of yeast beta-tubulin is not essential in vivo

1988 ◽  
Vol 8 (7) ◽  
pp. 2730-2736
Author(s):  
W S Katz ◽  
F Solomon
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Meiotic Division ◽  
Functional Significance ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal ◽  
Beta Tubulin Gene

Sequences of genes for beta-tubulins from many different organisms demonstrate that they encode highly conserved proteins but that these proteins diverge considerably at their carboxyl termini. The patterns of interspecies conservation of this diversity suggest that it may have functional significance. We have taken advantage of the properties of Saccharomyces cerevisiae to test this hypothesis in vivo. The sole beta-tubulin gene of this species is one of the most divergent of all beta-tubulins and encodes 12 amino acids which extend past the end of most other beta-tubulin molecules. We have constructed strains in which the only beta-tubulin gene is an allele lacking these 12 codons. We show here that this carboxy-terminal extension is not essential. The absence of these 12 amino acids had no effect on a number of microtubule-dependent functions, such as mitotic and meiotic division and mating. It did confer dominant supersensitivity to a microtubule-depolymerizing drug.

scholarly journals Nucleotide sequence analysis of beta tubulin gene in a wide range of dermatophytes

2014 ◽  
Vol 52 (7) ◽  
pp. 674-688 ◽  
Author(s):  
Ali Rezaei-Matehkolaei ◽  
Hossein Mirhendi ◽  
Koichi Makimura ◽  
G. Sybren de Hoog ◽  
Kazuo Satoh ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Nucleotide Sequence ◽  
Nucleotide Sequence Analysis ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Wide Range ◽  
Beta Tubulin Gene

scholarly journals Interacting proteins identified by genetic interactions: a missense mutation in alpha-tubulin fails to complement alleles of the testis-specific beta-tubulin gene of Drosophila melanogaster.

1989 ◽  
Vol 9 (3) ◽  
pp. 875-884 ◽  
Author(s):  
T S Hays ◽  
R Deuring ◽  
B Robertson ◽  
M Prout ◽  
M T Fuller
Keyword(s):  
Drosophila Melanogaster ◽  
Missense Mutation ◽  
Null Allele ◽  
Genetic Interaction ◽  
Structural Proteins ◽  
Interacting Proteins ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Gene Encoding ◽  
Alpha Tubulin

In this paper we demonstrate that failure to complement between mutations at separate loci can be used to identify genes that encode interacting structural proteins. A mutation (nc33) identified because it failed to complement mutant alleles of the gene encoding the testis-specific beta 2-tubulin of Drosophila melanogaster (B2t) did not map to the B2t locus. We show that this second-site noncomplementing mutation is a missense mutation in alpha-tubulin that results in substitution of methionine in place of valine at amino acid 177. Because alpha- and beta-tubulin form a heterodimer, our results suggest that the genetic interaction, failure to complement, is based on the structural interaction between the protein products of the two genes. Although the nc33 mutation failed to complement a null allele of B2t (B2tn), a deletion of the alpha-tubulin gene to which nc33 mapped complemented B2tn. Thus, the failure to complement appears to require the presence of the altered alpha-tubulin encoded by the nc33 allele, which may act as a structural poison when incorporated into either the tubulin heterodimer or microtubules.

The beta tubulin gene of Eimeria tenella

1996 ◽  
Vol 76 (1-2) ◽  
pp. 315-319 ◽  
Author(s):  
Guan Zhu ◽  
Janet S. Keithly
Keyword(s):  
Eimeria Tenella ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Beta Tubulin Gene

Mutational analysis of the class i beta-tubulin gene in renal cell carcinoma (RCC)

2003 ◽  
Vol 2 (6) ◽  
pp. 66
Author(s):  
Roisean E Ferguson ◽  
Claire F Taylor ◽  
Anthea J Stanley ◽  
Roger M Phillips ◽  
Adrian D Joyce ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Cell Carcinoma ◽  
Renal Cell ◽  
Mutational Analysis ◽  
Class I ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Beta Tubulin Gene

Analysis of beta-tubulin Gene Fragments from Benzimidazole-sensitive and -tolerant Cercospora beticola

2006 ◽  
Vol 154 (6) ◽  
pp. 321-328 ◽  
Author(s):  
R. M. Davidson ◽  
L. E. Hanson ◽  
G. D. Franc ◽  
L. Panella
Keyword(s):  
Cercospora Beticola ◽  
Tubulin Gene ◽  
Beta Tubulin ◽  
Beta Tubulin Gene

Phenotypic consequences of tubulin overproduction in Saccharomyces cerevisiae: differences between alpha-tubulin and beta-tubulin

1990 ◽  
Vol 10 (10) ◽  
pp. 5295-5304
Author(s):  
B Weinstein ◽  
F Solomon
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Division ◽  
Microtubule Assembly ◽  
Beta Tubulin ◽  
Alpha Tubulin ◽  
Tubulin Genes ◽  
Data Support ◽  
Cell Biol

Overexpression of alpha- and beta-tubulin genes in Saccharomyces cerevisiae, separately or together, leads to accumulation of large excesses of each of the polypeptides and arrest of cell division. However, other consequences of overexpression of these genes differ in several ways. As shown previously (D. Burke, P. Gasdaska, and L. Hartwell, Mol. Cell. Biol. 9:1049-1059, 1989), overexpression of beta-tubulin leads, at early times, to loss of microtubule structures and loss of viability. Eventually, the excess beta-tubulin forms abnormal structures. We show here that, in contrast, overexpression of alpha-tubulin led to none of these phenotypes and in fact could suppress each of the phenotypes associated with beta-tubulin accumulation. Truncated forms of beta-tubulin that were not competent to carry out microtubule functions also failed to elicit the beta-tubulin-specific phenotypes when overexpressed. The data support the hypothesis that beta-tubulin in excess over alpha-tubulin is uniquely toxic, perhaps because it interferes with normal microtubule assembly.

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