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A cytoplasmic dynein heavy chain in sea urchin embryos *
Author(s) -
Gibbons Ian R.,
Asai David J.,
Tang WenJing Y.,
Gibbons Barbara H.
Publication year - 1992
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/0248-4900(92)90432-z
Subject(s) - dynein , biology , sea urchin , gene isoform , dynactin , strongylocentrotus purpuratus , microbiology and biotechnology , embryo , microtubule , cytoplasm , dynein atpase , messenger rna , biochemistry , gene
Summary— By making the hypothetis 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 β‐heavy chain, like that of tubulin, increases 2–3‐fold after deciliation of the embryos, whereas the expression of the second dynein isoforms, like that of actin, is essentially unaffected. This second isoform is believed to be the cytoplasmic dynein of sea urchin embryos.