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    Calcium control of waveform in isolated flagellar axonemes of Chlamydomonas

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    Authors
    Bessen, Matthew
    Fay, Rose B.
    Witman, George B.
    UMass Chan Affiliations
    Department of Cell Biology
    Document Type
    Journal Article
    Publication Date
    1980-08-01
    Keywords
    Adenosine Triphosphatases
    Calcium
    Cell Membrane
    Cell-Free System
    Chlamydomonas
    Dynein ATPase
    Flagella
    Microtubules
    Movement
    Algae
    Cell Biology
    Investigative Techniques
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    Link to Full Text
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111489
    Abstract
    The effect of Ca(++) on the waveform of reactivated, isolated axonemes of chlamydomonas flagella was investigated. Flagella were detached and isolated by the dibucaine procedure and demembranated by treatment with the detergent Nonidet; the resulting axomenes lack the flagellar membrane and basal bodies. In Ca(++)-buffered reactivation solutions containing 10(-6) M or less free Ca(++), the axonemes beat with a highly asymmetrical, predominantly planar waveform that closely resembled that of in situ flagella of forward swimming cells. In solutions containing 10(-4) M Ca(++), the axonemes beat with a symmetrical waveform that was very similar to that of in situ flagella during backward swimming. In 10(-5) M Ca(++), the axonemes were predominantly quiescent, a state that appears to be closely associated with changes in axomenal waveform or direction of beat in many organisms. Experiments in which the concentrations of free Ca(++), not CaATP(--) complex were independently varied suggested that free Ca(++), not CaATP(--), was responsible for the observed changes. Analysis of the flagellar ATPases associated with the isolated axonemes and the nonidet- soluble membrane-matrix fraction obtained during preparation of the axonemes showed that the axonemes lacked the 3.0S Ca(++)-activated ATPase, almost all of which was recovered in the membrane-matrix fraction. These results indicate that free Ca(++) binds directly to an axonemal component to alter flagellar waveform, and that neither the 3.0S CaATPase nor the basal bodies are directly involved in this change.
    Source

    J Cell Biol. 1980 Aug;86(2):446-55.

    DOI
    10.1083/jcb.86.2.446
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/26543
    PubMed ID
    6447155
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    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1083/jcb.86.2.446
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