Investigation of Diversity and Isotypes of the Beta-Tubulin cDNA in Several Small Strongyle (Cyathostominae) Species

2002 ◽  
Vol 88 (4) ◽  
pp. 673 ◽  
Author(s):  
Michaela Pape ◽  
Thomas Schnieder ◽  
Georg von Samson-Himmelstjerna
Keyword(s):  
Beta Tubulin ◽  
Small Strongyle

INVESTIGATION OF DIVERSITY AND ISOTYPES OF THE BETA-TUBULIN cDNA IN SEVERAL SMALL STRONGYLE (CYATHOSTOMINAE) SPECIES

2002 ◽  
Vol 88 (4) ◽  
pp. 673-677 ◽  
Author(s):  
Michaela Pape ◽  
Thomas Schnieder ◽  
Georg von Samson-Himmelstjerna
Keyword(s):  
Beta Tubulin ◽  
Small Strongyle

ALLELE-SPECIFIC PCR FOR THE BETA-TUBULIN CODON 200 TTC/TAC POLYMORPHISM USING SINGLE ADULT AND LARVAL SMALL STRONGYLE (CYATHOSTOMINAE) STAGES

2002 ◽  
Vol 88 (2) ◽  
pp. 254-257 ◽  
Author(s):  
G. von Samson-Himmelstjerna ◽  
M. Pape ◽  
C. von Witzendorff ◽  
T. Schnieder
Keyword(s):  
Beta Tubulin ◽  
Specific Pcr ◽  
Small Strongyle ◽  
Allele Specific ◽  
Allele Specific Pcr

Allele-Specific PCR for the Beta-Tubulin Codon 200 TTC/TAC Polymorphism Using Single Adult and Larval Small Strongyle (Cyathostominae) Stages

2002 ◽  
Vol 88 (2) ◽  
pp. 254 ◽  
Author(s):  
G. von Samson-Himmelstjerna ◽  
M. Pape ◽  
C. von Witzendorff ◽  
T. Schnieder
Keyword(s):  
Beta Tubulin ◽  
Specific Pcr ◽  
Small Strongyle ◽  
Allele Specific ◽  
Allele Specific Pcr

Novel small strongyle (Cyathostominae) beta-tubulin sequences

2001 ◽  
Vol 87 (2) ◽  
pp. 122-125 ◽  
Author(s):  
G. von Samson-Himmelstjerna ◽  
A. Harder ◽  
M. Pape ◽  
T. Schnieder
Keyword(s):  
Beta Tubulin ◽  
Small Strongyle

scholarly journals Immunological discrimination of β-tubulin isoforms in developing mouse brain. Post-translational modification of non-class-III β-tubulins

1992 ◽  
Vol 288 (3) ◽  
pp. 919-924 ◽  
Author(s):  
I Linhartová ◽  
P Dráber ◽  
E Dráberová ◽  
V Viklický
Keyword(s):  
Mouse Brain ◽  
Specific Class ◽  
Class Iii ◽  
Post Translational Modification ◽  
Beta Tubulin ◽  
Developmentally Regulated ◽  
Post Translational Modifications ◽  
Tubulin Isotypes ◽  
Tubulin Isoforms ◽  
Developing Mouse Brain

Individual beta-tubulin isoforms in developing mouse brain were characterized using immunoblotting, after preceding high-resolution isoelectric focusing, with monoclonal antibodies against different structural regions of beta-tubulin. Some of the antibodies reacted with a limited number of tubulin isoforms in all stages of brain development and in HeLa cells. The epitope for the TU-14 antibody was located in the isotype-defining domain and was present on the beta-tubulin isotypes of classes I, II and IV, but absent on the neuron-specific class-III isotype. The data suggest that non-class-III beta-tubulins in mouse brain are substrates for developmentally regulated post-translational modifications and that beta-tubulins of non-neuronal cells are also post-translationally modified.

scholarly journals Translation of beta-tubulin mRNA in vitro generates multiple molecular forms.

1988 ◽  
Vol 263 (31) ◽  
pp. 16023-16031
Author(s):  
M B Yaffe ◽  
G W Farr ◽  
H Sternlicht
Keyword(s):  
Molecular Forms ◽  
Beta Tubulin ◽  
Multiple Molecular Forms ◽  
Tubulin Mrna

scholarly journals Increased microtubule assembly in bovine brain tubulin lacking the type III isotype of beta-tubulin.

1990 ◽  
Vol 265 (3) ◽  
pp. 1794-1799
Author(s):  
A Banerjee ◽  
M C Roach ◽  
P Trcka ◽  
R F Ludueña
Keyword(s):  
Bovine Brain ◽  
Microtubule Assembly ◽  
Beta Tubulin ◽  
Type Iii ◽  
Brain Tubulin

scholarly journals Structural analysis of mutations in the Drosophila beta 2-tubulin isoform reveals regions in the beta-tubulin molecular required for general and for tissue-specific microtubule functions.

Genetics ◽  
1995 ◽  
Vol 139 (1) ◽  
pp. 267-286 ◽  
Author(s):  
J D Fackenthal ◽  
J A Hutchens ◽  
F R Turner ◽  
E C Raff
Keyword(s):  
Amino Acid ◽  
Three Dimensional ◽  
Variable Region ◽  
Internal Variable ◽  
Microtubule Assembly ◽  
Dimensional Structure ◽  
Wild Type ◽  
Beta Tubulin ◽  
Assembly Kinetics ◽  
Beta 2

Abstract We have determined the lesions in a number of mutant alleles of beta Tub85D, the gene that encodes the testis-specific beta 2-tubulin isoform in Drosophila melanogaster. Mutations responsible for different classes of functional phenotypes are distributed throughout the beta 2-tubulin molecule. There is a telling correlation between the degree of phylogenetic conservation of the altered residues and the number of different microtubule categories disrupted by the lesions. The majority of lesions occur at positions that are evolutionarily highly conserved in all beta-tubulins; these lesions disrupt general functions common to multiple classes of microtubules. However, a single allele B2t6 contains an amino acid substitution within an internal cluster of variable amino acids that has been identified as an isotype-defining domain in vertebrate beta-tubulins. Correspondingly, B2t6 disrupts only a subset of microtubule functions, resulting in misspecification of the morphology of the doublet microtubules of the sperm tail axoneme. We previously demonstrated that beta 3, a developmentally regulated Drosophila beta-tubulin isoform, confers the same restricted morphological phenotype in a dominant way when it is coexpressed in the testis with wild-type beta 2-tubulin. We show here by complementation analysis that beta 3 and the B2t6 product disrupt a common aspect of microtubule assembly. We therefore conclude that the amino acid sequence of the beta 2-tubulin internal variable region is required for generation of correct axoneme morphology but not for general microtubule functions. As we have previously reported, the beta 2-tubulin carboxy terminal isotype-defining domain is required for suprastructural organization of the axoneme. We demonstrate here that the beta 2 variant lacking the carboxy terminus and the B2t6 variant complement each other for mild-to-moderate meiotic defects but do not complement for proper axonemal morphology. Our results are consistent with the hypothesis drawn from comparisons of vertebrate beta-tubulins that the two isotype-defining domains interact in a three-dimensional structure in wild-type beta-tubulins. We propose that the integrity of this structure in the Drosophila testis beta 2-tubulin isoform is required for proper axoneme assembly but not necessarily for general microtubule functions. On the basis of our observations we present a model for regulation of axoneme microtubule morphology as a function of tubulin assembly kinetics.

scholarly journals Quantitative benzimidazole resistance and fitness effects of parasitic nematode beta-tubulin alleles

2020 ◽  
Vol 14 ◽  
pp. 28-36 ◽  
Author(s):  
Clayton M. Dilks ◽  
Steffen R. Hahnel ◽  
Qicong Sheng ◽  
Lijiang Long ◽  
Patrick T. McGrath ◽  
...  
Keyword(s):  
Parasitic Nematode ◽  
Beta Tubulin ◽  
Fitness Effects ◽  
Benzimidazole Resistance

Proteolytic analysis of polymerized maize tubulin: regulation of microtubule stability to low temperature and Ca2+ by the carboxyl terminus of beta-tubulin

1996 ◽  
Vol 19 (5) ◽  
pp. 539-548 ◽  
Author(s):  
C. L. BOKROS ◽  
J. D. HUGDAHL ◽  
S. S. D. BLUMENTHAL ◽  
L. C. MOREJOHN
Keyword(s):  
Low Temperature ◽  
Carboxyl Terminus ◽  
Beta Tubulin ◽  
Microtubule Stability
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