Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm.
Axonemes isolated from the sperm of the sea urchin, Tripneustes gratilla, were briefly digested with trypsin. The digested axonemes retained their typical structure of a cylinder of nine doublet-tubules surrounding a pair of single tubules. The digestion modified the axonemes so that the subsequent addition of 0.1 mM ATP caused them to disintegrate actively into individual tubules and groups. The nucleotide specificity and divalent-cation requirements of this disintegration reaction paralleled those of flagellar motility, suggesting that the underlying mechanisms were closely related. Observations by dark-field microscopy showed that the disintegration resulted from active sliding between groups of the outer doublet-tubules, together with a tendency for the partially disintegrated axoneme to coil into a helix. Our evidence supports the hypothesis that the propagated bending waves of live-sperm tails are the result of ATP-induced shearing forces between outer tubules which, when resisted by the native structure, lead to localized sliding and generate an active bending moment.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D005407:Flagella / Q000166:cytology / Q000187:drug effects*; D008297:Male; D008854:Microscopy, Electron; D012617:Sea Urchins; D013094:Spermatozoa / Q000166:cytology / Q000187:drug effects*; D014357:Trypsin / Q000494:pharmacology*
D000255:Adenosine Triphosphate; D014357:Trypsin