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Isolation of dynein heavy chain complementary dna from trout testis which predict an extensive carboxyl terminal alpha helical coiled coil domain

, : Isolation of dynein heavy chain complementary dna from trout testis which predict an extensive carboxyl terminal alpha helical coiled coil domain. EMBO (European Molecular Biology Organization) Journal 8(6): 1727-1734

A Mg2+-dependent ATPase activity has been purified from trout sperm axonemes which has properties characteristic of a dynein ATPase. A polyclonal antiserum prepared against the dynein heavy chains has been used to isolate dynein heavy chain (DYHC) cDNAs from a troup testis .lambda.gt11 cDNA expression library. .beta.-galactosidase fusion proteins produced in .lambda.gt11 by these trout cDNAs cross-reacted with a heterologous anti-sea urchin dynein antiserum. Northern blot analyses demonstrated that the RNA transcripts detected have sizes (7.5-12 kb) consistent with those expected for the dynein heavy chains. All the DYHC cDNAs encode portions of a highly unusual DNA coding sequence comprised of 21 bp direct repeats. The predicted open reading frame of this repeat is Ile/Leu-His-Val-Ile-Gln-Tyr-Ser and is characteristic of an extensive .alpha.-helical coiled-coil domain. The presence of an in-frame translation termination codon indicates that this domain is located at the carboxyl-terminus of the DYHC. Southern blot analyses demonstrated a low, if not single, copy number for this gene and conservation of this domain in other vertebrates. DYHC transcripts reach their highest level in testis, but are also abundant in brain tissue.


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