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dc.contributor.authorBessen, Matthew
dc.contributor.authorFay, Rose B.
dc.contributor.authorWitman, George B.
dc.date2022-08-11T08:08:04.000
dc.date.accessioned2022-08-23T15:41:04Z
dc.date.available2022-08-23T15:41:04Z
dc.date.issued1980-08-01
dc.date.submitted2008-12-15
dc.identifier.citation<p>J Cell Biol. 1980 Aug;86(2):446-55.</p>
dc.identifier.issn0021-9525 (Print)
dc.identifier.doi10.1083/jcb.86.2.446
dc.identifier.pmid6447155
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26543
dc.description.abstractThe 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=6447155&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111489
dc.subjectAdenosine Triphosphatases
dc.subjectCalcium
dc.subjectCell Membrane
dc.subjectCell-Free System
dc.subjectChlamydomonas
dc.subjectDynein ATPase
dc.subjectFlagella
dc.subjectMicrotubules
dc.subjectMovement
dc.subjectAlgae
dc.subjectCell Biology
dc.subjectInvestigative Techniques
dc.titleCalcium control of waveform in isolated flagellar axonemes of Chlamydomonas
dc.typeJournal Article
dc.source.journaltitleThe Journal of cell biology
dc.source.volume86
dc.source.issue2
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/47
dc.identifier.contextkey682200
html.description.abstract<p>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.</p>
dc.identifier.submissionpathcellbiology_pp/47
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages446-55


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