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Journal of Cell Science, Vol 107, Issue 2 345-351, Copyright © 1994 by Company of Biologists


JOURNAL ARTICLES

Isolation and characterization of a novel dynein that contains C and A heavy chains from sea urchin sperm flagellar axonemes

E Yokota and I Mabuchi
Department of Biology, College of Arts and Sciences, University of Tokyo, Japan.

A novel dynein (C/A dynein), which is composed of C and A heavy chains, two intermediate chains and several light chains, was isolated from sea urchin sperm flagella. The C/A dynein was released by the treatment with 0.7 M NaCl plus 5 mM ATP from the axonemes depleted of outer arm 21 S dynein. Sedimentation coefficient of this dynein was estimated by sucrose density gradient centrifugation to be 22-23 S. The C/A dynein particle appeared to be composed of three distinct domains; two globular head domains and one rod domain as seen by negative staining electron microscopy. The mobility of 'A' heavy chain of C/A dynein on SDS-gel electrophoresis was similar to that of A heavy chains (A alpha and A beta) of 21 S dynein. However, UV-cleavage patterns of C and A heavy chains of C/A dynein were different from those of A heavy chains of 21 S dynein. Furthermore, an antiserum raised against A heavy chain of C/A dynein did not crossreact with A heavy chains of 21 S dynein. Under the conditions in which the C/A dynein was released, some of inner arms were removed concomitantly from axonemes as observed by electron microscopy. These results suggested that C/A dynein is a component of the inner arms.


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J. Cell Sci.Home page
E Yokota and I Mabuchi
C/A dynein isolated from sea urchin sperm flagellar axonemes. Enzymatic properties and interaction with microtubules
J. Cell Sci., January 2, 1994; 107(2): 353 - 361.
[Abstract] [PDF]




© The Company of Biologists Ltd 1994