Experimental dissection of flagellar surface motility in Chlamydomonas.
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.
D000936:Antigen-Antibody Complex; D001665:Binding Sites; D002696:Chlamydomonas / Q000502:physiology* / Q000648:ultrastructure; D002918:Chymotrypsin / Q000378:metabolism; D003078:Colchicine / Q000494:pharmacology; D003572:Cytochalasins / Q000494:pharmacology; D005407:Flagella / Q000648:ultrastructure*; D008560:Membrane Fluidity; D009068:Movement; D014357:Trypsin / Q000378:metabolism; D014747:Vinblastine / Q000494:pharmacology
D000936:Antigen-Antibody Complex; D003572:Cytochalasins; D014747:Vinblastine; D002918:Chymotrypsin; D014357:Trypsin; D003078:Colchicine