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Vol. 9, Issue 2, 237-247, February 1998
Department of Biological Sciences, Purdue University, West
Lafayette, Indiana, 47907-1392
Recent studies have revealed the expression of multiple putative
cytoplasmic dynein heavy chain (DHC) genes in several organisms, with
each gene encoding a separate protein isoform. This finding is
consistent with the hypothesis that different isoforms do different things, as is the case for the axonemal dyneins. Furthermore, the large
number of tasks ascribed to cytoplasmic dynein suggests that there may
be additional isoforms not yet identified. Two of the mammalian
cytoplasmic dynein heavy chains are DHC1a and DHC1b. DHC1a is
conventional cytoplasmic dynein and is found in all organisms examined.
DHC1b is expressed in organisms that have multiple dyneins, and has
been implicated in the intracellular trafficking of molecules in
unciliated and ciliated cells. In the present study, we examined the
DHC1b protein from rat testis. Testis cytoplasmic dynein contains a
large amount of dynein heavy chain reactive with an antibody raised
against a peptide sequence of rat DHC1b. The testis anti-DHC1b
immunoreactive protein is slightly smaller than testis DHC1a, as
assessed by SDS-PAGE. In Northern blots, the DHC1b mRNA is smaller than
the DHC1a mRNA. In sucrose gradients made in low ionic strength, DHC1a
sedimented at approximately 20S, and the anti-1b immunoreactive heavy
chains sedimented in a broad band centered at approximately 14S. The V1-photolysis reaction of individual sucrose gradient fractions revealed three distinct patterns of photolysis, suggesting that there
are at least three separate 1b-like heavy chain isoforms in testis.
Using a high-stringency Western blotting protocol, the anti-1b antibody
and the anti-DHC2 antibody recognized the same heavy chain and
specifically bound to one of the three 1b-like heavy chains. We
conclude that rat testis contains three 1b-like dynein heavy chains,
and one of these is the product of the DHC1b/DHC2 gene previously
identified.
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