Mechanism of action of vinblastine. Binding of [acetyl-3H]-vinblastine to embryonic chick brain tubulin and tubulin from sea urchin sperm tail outer doublet microtubules

Biochemistry ◽  
1975 ◽  
Vol 14 (26) ◽  
pp. 5586-5592 ◽  
Author(s):  
Leslie Wilson ◽  
Karen M. Creswell ◽  
Daniel Chin
Keyword(s):  
Sea Urchin ◽  
Mechanism Of Action ◽  
Embryonic Chick ◽  
Chick Brain ◽  
Sperm Tail ◽  
Brain Tubulin ◽  
Sea Urchin Sperm

scholarly journals Initiation of brain tubulin assembly by a high molecular weight flagellar protein factor.

1976 ◽  
Vol 71 (1) ◽  
pp. 322-331 ◽  
Author(s):  
R A Bloodgood ◽  
J L Rosenbaum
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Sea Urchin ◽  
Chick Brain ◽  
Tubulin Dimer ◽  
Protein Factor ◽  
Flagellar Protein ◽  
Brain Tubulin ◽  
Sea Urchin Sperm

A protein factor found within the flagella of Chlamydomonas and sea urchin sperm is capable of stimulating the initiation of calf and chick brain tubulin dimer assembly in vitro.

C/A dynein isolated from sea urchin sperm flagellar axonemes. Enzymatic properties and interaction with microtubules

1994 ◽  
Vol 107 (2) ◽  
pp. 353-361 ◽  
Author(s):  
E. Yokota ◽  
I. Mabuchi
Keyword(s):  
Atpase Activity ◽  
Sea Urchin ◽  
Maximal Inhibition ◽  
Heavy Chains ◽  
Lower Molecular Mass ◽  
Cross Bridges ◽  
Polypeptide Chains ◽  
Brain Tubulin ◽  
Sea Urchin Sperm

C/A dynein is a novel dynein isolated from sea urchin sperm flagellar axonemes. It is composed of C and A heavy chains and some additional lower molecular mass polypeptide chains. The characterization of ATPase activity and the interaction of this dynein with microtubules polymerized from calf brain tubulin were investigated in this study. The ATPase activity of C/A dynein (0.3-0.4 mumol Pi/min per mg) was about one half that of outer arm 21 S dynein (0.6-0.8 mumol Pi/min per mg) at 25 degrees C. Vanadate inhibited the ATPase activity with a half-maximal inhibition at 1 microM. C/A dynein absorbed to the glass surface was able to translocate the microtubules towards its plus end. The velocity of the microtubule movement in the presence of 1 mM ATP was 4.0 to 4.5 microns/s at 22 degrees C. C/A dynein binds to and bundles the microtubules even in the presence of ATP. Cross-bridges were found between adjacent microtubules in the bundle with an axial periodicity of about 24 nm. The ATPase activity of C/A dynein was enhanced up to several-fold by the microtubules at concentration as low as 1 mg/ml. On the other hand, 21 S dynein bound to the microtubules with 24 nm axial periodicity only in the absence of ATP. Its ATPase activity was not activated by the microtubules. From these results, it is concluded that the manner of interaction with microtubules of C/A dynein is different from that of the outer arm dynein.

X-ray and optical diffraction studies on the outer fibres of sea-urchin sperm tail flagella

1972 ◽  
Vol 257 (1) ◽  
pp. 30-36 ◽  
Author(s):  
Takashi Yamaguchi ◽  
Masao Hayashi ◽  
Katsuzo Wakabayashi ◽  
Sugie Higashi-Fujime
Keyword(s):  
Sea Urchin ◽  
Optical Diffraction ◽  
Sperm Tail ◽  
X Ray ◽  
Sea Urchin Sperm

scholarly journals SELECTIVE EXTRACTION OF ISOLATED MITOTIC APPARATUS

1971 ◽  
Vol 48 (2) ◽  
pp. 324-339 ◽  
Author(s):  
Thomas Bibring ◽  
Jane Baxandall
Keyword(s):  
Sea Urchin ◽  
Protein Extraction ◽  
Sedimentation Coefficient ◽  
Selective Extraction ◽  
Major Protein ◽  
Mitotic Apparatus ◽  
Sperm Tail ◽  
Microtubule Protein ◽  
Related Proteins ◽  
Sea Urchin Sperm

Mitotic apparatus isolated from sea urchin eggs has been treated with meralluride sodium under conditions otherwise resembling those of its isolation. The treatment causes a selective morphological disappearance of microtubules while extracting a major protein fraction, probably consisting of two closely related proteins, which constitutes about 10% of mitotic apparatus protein. Extraction of other cell particulates under similar conditions yields much less of this protein. The extracted protein closely resembles outer doublet microtubule protein from sea urchin sperm tail in properties considered typical of microtubule proteins: precipitation by calcium ion and vinblastine, electrophoretic mobility in both acid and basic polyacrylamide gels, sedimentation coefficient, molecular weight, and, according to a preliminary determination, amino acid composition. An antiserum against a preparation of sperm tail outer doublet microtubules cross-reacts with the extract from mitotic apparatus. On the basis of these findings it appears that microtubule protein is selectively extracted from isolated mitotic apparatus by treatment with meralluride, and is a typical microtubule protein.

scholarly journals The axonemal axis and Ca2+-induced asymmetry of active microtubule sliding in sea urchin sperm tails.

1986 ◽  
Vol 102 (6) ◽  
pp. 2042-2052 ◽  
Author(s):  
W S Sale
Keyword(s):  
Sea Urchin ◽  
Pair Interaction ◽  
Central Pair ◽  
Sperm Tail ◽  
Lytechinus Pictus ◽  
Motile Cells ◽  
Definition Of ◽  
Triton X ◽  
Explicit Discussion ◽  
Sea Urchin Sperm

Structural studies of stationary principal bends and of definitive patterns of spontaneous microtubule sliding disruption permitted description of the bending axis in sea urchin sperm tail axonemes. Lytechinus pictus sperm were demembranated in a buffer containing Triton X-100 and EGTA. Subsequent resuspension in a reactivation buffer containing 0.4 mM CaCl2 and 1.0 mM MgATP2- resulted in quiescent, rather than motile, cells and each sperm tail axoneme took on an extreme, basal principal bend of 5.2 rad. Thereafter, such flagellar axonemes began to disrupt spontaneously into two subsets of microtubules by active sliding requiring ATP. Darkfield light microscopy demonstrated that subset "1" is composed of microtubules from the inside edge of the principal bend. Subset "2" is composed of microtubules from the outside edge of the principal bend and always scatters less light in darkfield than subset 1. Subset 2, which always slides in the proximal direction, relative to subset 1, results in a basal loop of microtubules, and the subset 2 loop is restricted to the bend plane during sliding disruption. Electron microscopy revealed that doublets 8, 9, 1, 2, 3 and the central pair comprise subset 1, and doublets 4, 5, the bridge, 6, and 7 comprise subset 2. The microtubules of isolated subset 2 are maintained in a circular arc in the absence of spoke-central pair interaction. Longitudinal sections show that the bending plane bisects the central pair. We therefore conclude that the bend plane passes through doublet 1 and the 5-6 bridge and that doublet 1 is at the inside edge of the principal bend. Experimental definition of the axis permits explicit discussion of the location of active axonemal components which result in Ca2+-induced stationary basal bends and explicit description of components responsible for alternating basal principal and reverse bends.

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