A cytoplasmic dynein heavy chain in sea urchin embryos.
By making the hypothesis that the pattern of conserved sequence residues in the vicinity of the hydrolytic ATP-binding site of dynein would resemble that in myosins from a broad variety of sources, we designed degenerate oligonucleotide primers capable of amplifying this region of multiple dynein isoforms from sea urchin embryo poly(A)+ RNA. Quantification of the expression of two of these dynein isoforms has shown that the level of mRNA encoding for the beta-heavy chain, like that of tubulin, increases 2-3-fold after deciliation of the embryos, whereas the expression of the second dynein isoform, like that of actin, is essentially unaffected. This second isoform is believed to be the cytoplasmic dynein of sea urchin embryos.
Gibbons
I R
IR
Pacific Biomedical Research Center, Kewalo Marine Laboratory, University of Hawaii, Honolulu 96813.
Asai
D J
DJ
Tang
W J
WJ
Gibbons
B H
BH
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003593:Cytoplasm / Q000201:enzymology*; D004398:Dyneins / Q000032:analysis* / Q000737:chemistry; D007527:Isoenzymes / Q000032:analysis* / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012617:Sea Urchins / Q000196:embryology* / Q000201:enzymology*; D016415:Sequence Alignment
D007527:Isoenzymes; D004398:Dyneins