Axial Filament

Author(s):  
Jan W. Gooch
Keyword(s):  
Author(s):  
Ezzatollah Keyhani ◽  
Larry F. Lemanski ◽  
Sharon L. Lemanski

Energy for sperm motility is provided by both glycolytic and respiratory pathways. Mitochondria are involved in the latter pathway and conserve energy of substrate oxidation by coupling to phosphorylation. During spermatogenesis, the mitochondria undergo extensive transformation which in many species leads to the formation of a nebemkem. The nebemkem subsequently forms into a helix around the axial filament complex in the middle piece of spermatozoa.Immature spermatozoa of axolotls contain numerous small spherical mitochondria which are randomly distributed throughout the cytoplasm (Fig. 1). As maturation progresses, the mitochondria appear to migrate to the middle piece region where they become tightly packed to form a crystalline-like sheath. The cytoplasm in this region is no longer abundant (Fig. 2) and the plasma membrane is now closely apposed to the outside of the mitochondrial layer.


2018 ◽  
Vol 53 (13) ◽  
pp. 1847-1864 ◽  
Author(s):  
K Bilisik ◽  
E Sapanci

The fracture toughness (mode-I) properties of nanostitched para-aramid/phenolic multiwall carbon nanotube prepreg composites were investigated. The fracture toughness (GIC) of the stitching and nanostitched composites showed 42-fold and 41-fold (beam theory), 18-fold and 21-fold (modified beam theory) increase compared to the control, respectively. The prepreg para-aramid stitching yarn and nanostitched yarn were dominant parameters. The toughness resistance to arrest crack growth in the nanostitched composite was primarily due to nanostitching fiber bridging and pull-out, and was secondarily due to nanotubes and biaxial fiber bridging and pull-out. The failed surfaces of the nanostitched and stitching composites had tensile filament failures in the aramid stitching fibers where filament/matrix/nanotube debonding and axial filament fibrillar splitting were found. The results indicated that stitching yarn and the nanotubes arrested the crack propagation. Therefore, the nanostitched and stitched para-aramid/phenolic composites displayed a better damage resistance performance compared to those of the control or nanotube composites.


1984 ◽  
Vol 98 (3) ◽  
pp. 834-846 ◽  
Author(s):  
H G de Couet ◽  
S Stowe ◽  
A D Blest

Infiltration of compound eyes of crayfish, Cherax destructor, with the thiol protease inhibitor Ep-475 or with trifluoperazine prior to fixation for electron microscopy was found to stabilize an axial filament of 6-12 nm diam within each rhabdomeral microvillus of the photoreceptors. Rhabdoms isolated from retinal homogenates by sucrose gradient centrifugation under conditions that stabilize cytoskeletal material contained large amounts of a 42-kd polypeptide that co-migrated with insect flight muscle actin in one- and two-dimensional PAGE, inhibited pancreatic DNase l, and bound to vertebrate myosin. Vertebrate skeletal muscle actin added to retinal homogenates did not co-purify with rhabdoms, implying that actin was not a contaminant from nonmembranous structures. DNase l inhibition assays of detergent-lysed rhabdoms indicated the presence of large amounts of filamentous actin provided ATP was present. Monomeric actin in such preparations was completely polymerizable only after 90 min incubation with equimolar phalloidin. More than half of the actin present could be liberated from the membrane by sonication, indicating a loose association with the membrane. However, a large proportion of the actin was tightly bound to the rhabdomeral membrane, and washing sonicated membrane fractions with solutions of a range of ionic strengths and nonionic detergents failed to remove it. Antibodies to scallop actin only bound to frozen sections of rhabdoms after gentle permeabilization and very long incubation periods, probably because of steric hindrance and the hydrophobicity of the structure. The F-actin probe nitrobenzoxadiazol phallacidin bound to rhabdoms and labeled F-actin aggregates in other retinal components, but rhabdom fluorescence was not abolished by preincubation with phalloidin. The biochemical data indicate the existence of two distinct actin-based cytoskeletal systems, one being closely membrane associated. The other may possibly constitute the axial filament, although the evidence for this is equivocal.


1970 ◽  
Vol 18 (1) ◽  
pp. 21 ◽  
Author(s):  
CS Sapsford ◽  
CA Rae ◽  
KW Cleland

The first components of the sheath to develop are two longitudinal columns, characterized by alternating light and dark bands. The columns, which lie on opposite sides of the future principal piece, are initially associated with the axial filament complex but soon make contact with the plasma membrane. Subsequently a layer of moderately dense material grows outwards from the lateral aspects of each column. The outgrowths lie just beneath the tail plasma membrane and contain evenly spaced filaments which are connected with the dark bands of the columns. The outgrowths from corresponding sides of each column eventually meet each other and the filaments they contain join end-to-end. Some parts of the sheath, separated from the plasma membrane by an expansion of the cytoplasm of the intraspermatid tail, become invested by membrane bound vacuoles. The filaments form into groups, and filaments within groups converge to produce the anlagen of the ribs of the mature sheath. The filaments lose their identity in these anlagen, which, like the columns, develop much finer filamentous structures. The ribs, and subsequently the columns, lose contact with the tail plasma membrane. The mature sheath, the ultrastructure of which is described in detail, is developed by further modification of the rib anlagen and longitudinal columns.


2020 ◽  
Vol 202 (20) ◽  
Author(s):  
Clare Willis ◽  
Jeff Errington ◽  
Ling Juan Wu

ABSTRACT During sporulation of Bacillus subtilis, the cell cycle is reorganized to generate separated prespore and mother cell compartments, each containing a single fully replicated chromosome. The process begins with reorganization of the nucleoid to form an elongated structure, the axial filament, in which the two chromosome origins are attached to opposite cell poles, with the remainder of the DNA stretched between these sites. When the cell then divides asymmetrically, the division septum closes around the chromosome destined for the smaller prespore, trapping the origin-proximal third of the chromosome in the prespore. A translocation pore is assembled through which a DNA transporter, SpoIIIE/FtsK, transfers the bulk of the chromosome to complete the segregation process. Although the mechanisms involved in attaching origin regions to the cell poles are quite well understood, little is known about other aspects of axial filament morphology. We have studied the behavior of the terminus region of the chromosome during sporulation using time-lapse imaging of wild-type and mutant cells. The results suggest that the elongated structure involves cohesion of the terminus regions of the sister chromosomes and that this cohesion is resolved when the termini reach the asymmetric septum or translocation pore. Possible mechanisms and roles of cohesion and resolution are discussed. IMPORTANCE Endospore formation in Firmicutes bacteria provides one of the most highly resistant life forms on earth. During the early stages of endospore formation, the cell cycle is reorganized so that exactly two fully replicated chromosomes are generated, before the cell divides asymmetrically to generate the prespore and mother cell compartments that are critical for the developmental process. Decades ago, it was discovered that just prior to asymmetrical division the two chromosomes enter an unusual elongated configuration called the axial filament. This paper provides new insights into the nature of the axial filament structure and suggests that cohesion of the normally separated sister chromosome termini plays an important role in axial filament formation.


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