Axonemes paralyzed by the presence of dyneins unable to use ribose-modified ATP
| Autor: | Charlotte K. Omoto, Ellen Lark |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Axoneme
ATPase Dynein Chlamydomonas reinhardtii macromolecular substances Substrate analog Binding Competitive Microtubules Substrate Specificity chemistry.chemical_compound Adenosine Triphosphate Cell Movement Structural Biology Dynein ATPase Ribose Animals ortho-Aminobenzoates Binding Sites biology Chlamydomonas Dyneins Cell Biology biology.organism_classification Cell biology Kinetics chemistry Biochemistry Mutation biology.protein |
| Zdroj: | Cell Motility and the Cytoskeleton. 27:161-168 |
| ISSN: | 1097-0169 0886-1544 |
| Popis: | Substrate analogs are useful for studying the structures of active sites and for distinguishing between similar enzyme activities. Fluorescent ribose-modified ATP analogs were used to investigate the functional differences between dynein ATPases. These analogs reactivate (support the movement of) sea urchin sperm axonemes, yet they do not reactivate wild-type Chalmydomonas axonemes. Surprisingly, the analogs reactivate the axonemes of mutants completely missing the outer arm dyneins. Competition experiments using ATP and these analogs provide strong evidence that the analogs bind to all dynein active sites but fail to release a subset of dyneins from rigor. We suggest that this subset of Chlamydomonas outer arm dyneins unable to use the analogs remains in rigor in the presence of the analogs and paralyzes the axoneme. © 1994 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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