| Experimental dissection of flagellar surface motility in Chlamydomonas. | |
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MedLine Citation:
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PMID: 7400220 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Experiments have explored the possible relationships between the flagellar surface motility of chlamydomonas, visualized as translocation of polystyrene beads by paralyzed (pf) mutants (Bloodgood, 1977, J. Cell Biol. 15:983-989), and the capacity of gametic flagella to participate in the mating reaction. While vegetative and gametic flagella bind beads with equal efficiencies and are capable of transporting them along entire flagellar lengths, beads on vegetative flagella are primarily associated with the proximal half of the flagella whereas those of gametic flagella exhibit no such preference. This difference may relate to the "tipping" response of gametes during sexual flagellar agglutination (Goodenough and Jurivich, 1978, J. Cell Biol. 79:680-693). Colchicine, vinblastine, chymotrypsin, cytochalasins B and D, and anti-beta-tubulin antiserum are all able to inhibit the binding of beads to the flagellar suface. Trysin digestion and an antiserum directed against whole chlamydomonas flagella have no effect on the ability of flagella to bind beads, but the beads remain immobile. These results suggest that at least two flagellar activities participate in surface motility: (a) bead binding, which may involve a tubulin-like component at the flagellar surface; and (b) bead translocation, which may depend on a second component (e.g. an ATPase) of the flagellar surface. Surface motility is shown to be distinct from gametic adhesiveness per se, but it may participate in concentrating dispersed agglutinins, in driving them toward the flagellar tips, and/or in generating a signal-to-fuse from the flagellar tips to the cell body. Directly supporting these concepts is the observation that bound beads remain immobilized at the flagellar tips during the "tip-locking" stage of pf x pf matings, and the observation that bound ligands such as antibody fail to be tipped by trypsinized flagella. |
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Authors:
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J L Hoffman; U W Goodenough |
Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of cell biology Volume: 86 ISSN: 0021-9525 ISO Abbreviation: J. Cell Biol. Publication Date: 1980 Aug |
Date Detail:
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Created Date: 1980-10-27 Completed Date: 1980-10-27 Revised Date: 2010-09-13 |
Medline Journal Info:
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Nlm Unique ID: 0375356 Medline TA: J Cell Biol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 656-65 Citation Subset: IM |
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| MeSH Terms | |
Descriptor/Qualifier:
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Antigen-Antibody Complex Binding Sites Chlamydomonas / physiology*, ultrastructure Chymotrypsin / metabolism Colchicine / pharmacology Cytochalasins / pharmacology Flagella / ultrastructure* Membrane Fluidity Movement Trypsin / metabolism Vinblastine / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Antigen-Antibody Complex; 0/Cytochalasins; 64-86-8/Colchicine; 865-21-4/Vinblastine; EC 3.4.21.1/Chymotrypsin; EC 3.4.21.4/Trypsin |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
| Full Text | |
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Journal Information Journal ID (nlm-ta): J Cell Biol ISSN: 0021-9525 ISSN: 1540-8140 Publisher: The Rockefeller University Press |
Article Information Download PDF  Print publication date: Day: 1 Month: 8 Year: 1980 Volume: 86 Issue: 2 First Page: 656 Last Page: 665 ID: 2111476 Publisher Id: 862656 PubMed Id: 7400220 |
| Experimental dissection of flagellar surface motility in chlamydomonas | |
| JL Hoffman | |
| UW Goodenough | |
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