Characterization of a Gene Family Encoding SEA (Sea-urchin Sperm Protein, Enterokinase and Agrin)-Domain Proteins with Lectin-Like and Heme-Binding Properties from Schistosoma japonicum

The separation and purification of histone H1 from the sperm of the sea-urchin Sphaerechinus granularis is described. Physical studies were used to compare this histone H1 molecule with H1 histones from other species. C.d. and 270 MHz n.m.r. spectroscopy indicate that, despite significant compositional differences from other sea-urchin sperm H1 histones, their secondary and tertiary structures are very similar. A large difference in helicity was, however, found between S. granularis histone H1 and calf thymus histone H1, and their n.m.r. and fluorescence spectra also differ considerably. It is concluded that secondary structure and tertiary structure have not been conserved in the evolution of the H1 histone family.

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Characterization of the Highly Variable Immune Response Gene Family, He185/333, in the Sea Urchin, Heliocidaris erythrogramma

PLoS ONE ◽

10.1371/journal.pone.0062079 ◽

2014 ◽

Vol 9 (10) ◽

pp. e62079 ◽

Cited By ~ 11

Author(s):

Mattias O. Roth ◽

Adam G. Wilkins ◽

Georgina M. Cooke ◽

David A. Raftos ◽

Sham V. Nair

Keyword(s):

Immune Response ◽

Gene Family ◽

Sea Urchin ◽

Immune Response Gene ◽

Response Gene ◽

Heliocidaris Erythrogramma

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

Journal of Cell Science ◽

10.1242/jcs.107.2.353 ◽

1994 ◽

Vol 107 (2) ◽

pp. 353-361 ◽

Cited By ~ 1

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.

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