scholarly journals Subpellicular and flagellar microtubules of Trypanosoma brucei brucei contain the same alpha-tubulin isoforms.

1987 ◽  
Vol 104 (3) ◽  
pp. 431-438 ◽  
Author(s):  
A Schneider ◽  
T Sherwin ◽  
R Sasse ◽  
D G Russell ◽  
K Gull ◽  
...  
Keyword(s):  
Trypanosoma Brucei ◽  
Close Contact ◽  
Electrophoretic Analysis ◽  
Translation Product ◽  
Trypanosoma Brucei Brucei ◽  
Alpha Tubulin ◽  
Predominant Species ◽  
Tubulin Isoforms ◽  
Small Pool ◽  
Flagellar Axoneme

The cytoskeleton of the parasitic hemoflagellate Trypanosoma brucei brucei essentially consists of two microtubule-based structures: a subpellicular layer of singlet microtubules, which are in close contact with the cell membrane, and the flagellar axoneme. In addition, the cells contain a small pool of soluble tubulin. Two-dimensional gel electrophoretic analysis of the tubulins present in these subcellular compartments revealed two distinct electrophoretic isoforms of alpha-tubulin, termed alpha 1 and alpha 3. alpha 1-Tubulin most likely represents the primary translation product, while alpha 3-tubulin is a posttranslationally acetylated derivative of alpha 1-tubulin. In the pool of soluble cytoplasmic tubulin, alpha 1 is the predominant species, while the very stable flagellar microtubules contain almost exclusively the alpha 3-tubulin isoform. The subpellicular microtubules contain both isoforms. Neither of the two alpha-tubulin isoforms is organelle specific, but the alpha 3 isoform is predominantly located in stable microtubules.

scholarly journals Distinct localization and cell cycle dependence of COOH terminally tyrosinolated alpha-tubulin in the microtubules of Trypanosoma brucei brucei.

1987 ◽  
Vol 104 (3) ◽  
pp. 439-446 ◽  
Author(s):  
T Sherwin ◽  
A Schneider ◽  
R Sasse ◽  
T Seebeck ◽  
K Gull
Keyword(s):  
Cell Cycle ◽  
Trypanosoma Brucei ◽  
Temporal Modulation ◽  
Trypanosoma Brucei Brucei ◽  
Alpha Tubulin ◽  
Tubulin Isoforms ◽  
A Cell ◽  
Cell Cycle Dependence ◽  
Microtubular Structures ◽  
Cycle Dependence

alpha-Tubulin can be posttranslationally modified in that its COOH-terminal amino acid residue, tyrosine, can be selectively removed and replaced again. This reaction cycle involves two enzymes, tubulin carboxypeptidase and tubulin tyrosine ligase. The functional significance of this unusual modification is unclear. The present study demonstrates that posttranslational tyrosinolation of alpha-tubulin does occur in the parasitic hemoflagellate Trypanosoma brucei brucei and that posttranslational tyrosinolation can be detected in both alpha-tubulin isoforms found in this organism. Trypanosomes contain a number of microtubular structures: the flagellar axoneme; the subpellicular layer of singlet microtubules which are closely associated with the cell membrane; the basal bodies; and a cytoplasmic pool of soluble tubulin. Tyrosinolated alpha-tubulin is present in all these populations. However, immunofluorescence studies demonstrate a distinct localization of tyrosinolated alpha-tubulin within individual microtubules and organelles. This localization is subject to a temporal modulation that correlates strongly with progress of a cell through the cell cycle. Our results indicate that the presence of tyrosinolated alpha-tubulin is a marker for newly formed microtubules.

scholarly journals Purification and assembly in vitro of tubulin from Trypanosoma brucei brucei

1990 ◽  
Vol 265 (1) ◽  
pp. 87-93 ◽  
Author(s):  
T H MacRae ◽  
K Gull
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Brucei ◽  
Purification Procedure ◽  
Polyacrylamide Gels ◽  
Trypanosoma Brucei Brucei ◽  
Alpha Tubulin ◽  
One Dimensional ◽  
Immunological Analysis ◽  
Selection Of

Trypanosome tubulin was purified to near homogeneity by chromatography on DEAE-Sephadex, Amicon filtration and assembly-disassembly in vitro. Polymerization of the tubulin in vitro yielded long, structurally normal, microtubules and some sheet structures on addition of GTP and incubation at 37 degrees C, in either the presence or the absence of Mg2+. Tubulin assembly was disrupted by glycerol and a selection of microtubule-reactive drugs. Immunological analysis of the purified tubulin revealed tyrosinated and acetylated alpha-tubulin, in addition to defining the migration characteristics of the alpha- and beta-tubulin on one-dimensional SDS/polyacrylamide gels. This is the first isolation of trypanosome tubulin with the ability to form structurally normal microtubules independent of the addition of taxol or nucleating microtubule fragments. The development of the purification procedure thus provides an important step for subsequent study of microtubule-associated protein-tubulin and plasma-membrane-microtubule cytoskeleton interactions of trypanosomes, and increases the potential for development of tubulin-based anti-trypanosome drugs.

Effects of n-hexane and ethylacetate fractions of Terminalia catappa leaf extract in experimental Trypanosoma brucei brucei infection in Wistar rats

2021 ◽  
Author(s):  
Folashade Sarah Ojeleye ◽  
Helen Ileigo Inabo ◽  
Clement Myah Zaman Whong ◽  
Bolanle Olufunke Priscilla Musa ◽  
Ochuko Orakpoghenor
Keyword(s):  
Trypanosoma Brucei ◽  
Wistar Rats ◽  
Leaf Extract ◽  
Trypanosoma Brucei Brucei ◽  
Terminalia Catappa

Modulation of Early Immune Responses and Suppression of Trypanosoma brucei brucei Infections by Surgical Denervation of the Spleen

2000 ◽  
Vol 8 (1) ◽  
pp. 31-38 ◽  
Author(s):  
Yajuan Liu ◽  
Manal Mustafa ◽  
Hu-Lun Li ◽  
Lauri Nuortio ◽  
Amged Mustafa ◽  
...  
Keyword(s):  
Immune Responses ◽  
Trypanosoma Brucei ◽  
Trypanosoma Brucei Brucei

Biochemical properties of histone-like proteins of procyclic Trypanosoma brucei brucei

Acta Tropica ◽  
1991 ◽  
Vol 50 (2) ◽  
pp. 169-183 ◽  
Author(s):  
Klaus Bender ◽  
Bruno Betschart ◽  
Johann Schaller ◽  
Urs Kämpfer ◽  
Hermann Hecker
Keyword(s):  
Trypanosoma Brucei ◽  
Biochemical Properties ◽  
Trypanosoma Brucei Brucei
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