Biochemical Analysis of a Mutant Tetrahymena Lacking Outer Dynein Arms

Autor:	Anita Schwandt, Susan A. Ludmann, David G. Pennock, Connie S. Bricker, Xuejun Konc
Rok vydání:	1993
Předmět:	Gel electrophoresis Axoneme Cilium Mutant Dynein Protozoan Proteins Tetrahymena Dyneins macromolecular substances Biology biology.organism_classification Microbiology Tetrahymena thermophila Cell biology Radial spoke Cell Movement Dynein ATPase Mutation Animals Electrophoresis Polyacrylamide Gel
Zdroj:	The Journal of Eukaryotic Microbiology. 40:650-660
ISSN:	1550-7408 1066-5234
DOI:	10.1111/j.1550-7408.1993.tb06123.x
Popis:	Tetrahymena thermophila mutants homozygous for the oad mutation become nonmotile when grown at the restrictive temperature, and axonemes isolated from nonmotile mutants lack approximately 90% of their outer dynein arms. Electrophoretic analyses of axonemes isolated from nonmotile mutants (oad axonemes) indicate they contain significantly fewer of the 22 S dynein heavy chains that axonemes isolated from wild-type cells (wild-type axonemes) contain. The 22 S dynein heavy chains that remain in axonemes isolated from nonmotile, oad mutants are assembled into 22 S dynein particles that exhibit wild-type levels of ATPase activity. Two-dimensional gel electrophoresis of oad axonemes show that they are deficient in no proteins other than those proteins thought to be components of 22 S dynein. This report is the first formal proof that outer dynein arms in Tetrahymena cilia are composed of 22 S dynein.
Databáze:	OpenAIRE
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