Morphology of nexin links in relation to interdoublet sliding in the sperm flagellum.
In this work, we examine whether the "nexin" linkages of the flagellum can extend in length to accommodate interdoublet sliding. Flagellar bends of large angle were induced in bull spermatozoa by hypotonic treatment. It is argued that this produces large interdoublet displacements that are, nevertheless, still within physiological limits. Such flagella were examined by the rapid-freeze, deep-etch technique and the nexin linkages identified by their position in relation to the inner dynein arms and by their straplike, bipartite, morphology. They were found to bridge perpendicularly (or occasionally at an angle) between the A- and B-tubules of adjacent doublets. The nexin linkages were no more than approximately nm in length, even in regions in which approximately 200 nm of sliding could be inferred. Variable registration between adjacent nexin rows gave some further support to the assumption that sliding had indeed taken place. From this, it is concluded that elastic deformation of the links, such as would accommodate interdoublet sliding, does not occur; some form of displacement must occur between nexin and the adjacent B-tubule.
Bozkurt
H H
HH
Department of Physiology, School of Medical Sciences, University of Bristol, United Kingdom.
Woolley
D M
DM
D000818:Animals; D002352:Carrier Proteins / Q000648:ultrastructure*; D002417:Cattle; D004398:Dyneins / Q000648:ultrastructure; D005613:Freeze Etching; D007038:Hypotonic Solutions / Q000494:pharmacology; D008297:Male; D008854:Microscopy, Electron; D008869:Microtubule-Associated Proteins; D013081:Sperm Motility; D013082:Sperm Tail / Q000187:drug effects / Q000648:ultrastructure*
D002352:Carrier Proteins; D007038:Hypotonic Solutions; D008869:Microtubule-Associated Proteins; C484652:microtubule nexin; D004398:Dyneins