Isolation and characterization of a novel dynein that contains C and A heavy chains from sea urchin sperm flagellar axonemes.
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.
Yokota
E
E
Department of Biology, College of Arts and Sciences, University of Tokyo, Japan.
Mabuchi
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I
D000818:Animals; D002499:Centrifugation, Density Gradient; D004398:Dyneins / Q000737:chemistry / Q000302:isolation & purification* / Q000648:ultrastructure; D008297:Male; D008854:Microscopy, Electron; D015394:Molecular Structure; D011233:Precipitin Tests; D012617:Sea Urchins / Q000737:chemistry / Q000201:enzymology; D013082:Sperm Tail / Q000737:chemistry* / Q000201:enzymology; D013347:Subcellular Fractions / Q000737:chemistry / Q000201:enzymology
D004398:Dyneins