Sertoli cell cytoplasts in the semen of the spiny dogfish Squalus acanthias

The fine structure of Squalus acanthias (Elasmobranchii) semen was investigated to determine the cellular component responsible for the steroidogenic activity previously demonstrated in the seminal plasma of this species. Semen was found to consist of bundles of spermatozoa, many of which were encased in a sleeve of cytoplasm restricted to the tail region; large, dense bodies lacking a limiting membrane and numerous anuclear cytoplasmic remnants containing lipid droplets, mitochondria, areas of agranular reticulum, and possibly unreleased spermatozoa. These remnants, which we have termed cytoplasts, morphologically resemble in appearance Sertoli cells of S. acanthias at the time of spermiation. This structural similarity, plus the fact that many elasmobranch species slough the apical regions of Sertoli cells during the release of spermatozoa, indicates that the cytoplasts present in the semen of S. acanthias originate from Sertoli cells. Furthermore, the occurrence in these cytoplasts of organelles normally associated with steroid synthesis strongly suggests these structures are the source of steroidogenic enzymes in the semen of S. acanthias. The steroidal contribution to the semen by Sertoli cell cytoplasts may be necessary for either maturation or maintenance of spermatozoa in the excurrent reproductive ducts of S. acanthias.     

The peculiarities of Blastocrithidia triatomae

Blastocrithidia triatomae parasitizes triatomine bugs, the vectors of Chagas disease. Co-cultivation with a host-derived cell line permits continuous culture but the host cells are destroyed. Removal of the reduviid cells induces the formation of drought-resistant cysts, but the factors that induce encystment are unknown. Excystment is triggered after the onset of blood digestion in the insect host, a transition that is associated with unusual ultrastructural alterations. Günter Schaub, Dagmar Reduth and Mary Pudney believe that B. triatomae is a good candidate for the biological control of Chagas disease, not least because of its capacity to form highly resistant cysts in vitro.     

Effect of Lincocin Treatment on the Greening Process in Bean (Phaseolus vulgaris) Leaves

The effect of lincocin (a plastid protein synthesis inhibitor) treatment on the greening process of bean (Phaseolus vulgaris L.) leaves have been studied. In comparison with control leaves treated ones had a decreased rate of chloroplast development. They had a marked chlorophyll deficiency and a decreased chlorophyll a/b ratio. Some long and short wavelength forms of chlorophyll a were lacking as evidenced from the absorption spectra at 25°C and the fluorescence spectra at 77°K. The –¹⁴CO₂ fixation was inhibited by 80–90% in treated leaves. The fluorescence induced by the measuring light was greater in the treated leaves than in the control ones, and the kinetics of the decline of the relative fluorescence intensity were also different. Electron microscopic studies showed macrogranum-like structures and incomplete membrane vesicles in the treated plastids. After longer treatment a destruction of membranes was observed. The results indicate some structural and functional membrane deficiencies and instability of the membranes.     

Lecithotrophic development and metamorphosis in the Indo-West Pacific brittle star Ophiomastix venosa (Echinodermata: Ophiuroidea)

Summary

The larval development of the ophiocomid ophiuroid Ophiomastix venosais described using SEM. The gastrula transforms into a uniformly ciliated early larva which progressively changes into a lecithotrophic late premetamorphic larva with a continuous bilateral ciliated band. This stage is short-lived and equivalent to a highly reduced ophiopluteus. Comparisons between O. venosa and other ophiuroid species whose development has been investigated suggest that, whatever the developmental mode (lecithotrophic or planktotrophic), a pluteus stage always occurs in ophiuroids with planktonic development. Two metamorphic stages were identified, the late metamorphic larva differing from the early one by the closure of the larval mouth. The appearance of the permanent mouth marks the end of the metamorphosis. The postlarva still possesses remnants of larval features. The transformation of the reduced ophiopluteus into a barrel-shaped metamorphic larva with transverse ciliated bands, a vitellaria larva, is followed. The possible occurrence of a unique type of metamorphic larva in non-brooding ophiuroids is discussed. Verification of this, however, needs further SEM investigations on metamorphic larva from species having “regular” planktotrophic development.     

Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation

Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation.     

Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 reductase family of enzymes

There is a mounting body of evidence to suggest that enzyme motions are linked to function, although the design of informative experiments aiming to evaluate how this motion facilitates reaction chemistry is challenging. For the family of diflavin reductase enzymes, typified by cytochrome P450 reductase, accumulating evidence suggests that electron transfer is somehow coupled to large-scale conformational change and that protein motions gate the electron transfer chemistry. These ideas have emerged from a variety of experimental approaches, including structural biology methods (i.e. X-ray crystallography, electron paramagnetic/NMR spectroscopies and solution X-ray scattering) and advanced spectroscopic techniques that have employed the use of variable pressure kinetic methodologies, together with solvent perturbation studies (i.e. ionic strength, deuteration and viscosity). Here, we offer a personal perspective on the importance of motions to electron transfer in the cytochrome P450 reductase family of enzymes, drawing on the detailed insight that can be obtained by combining these multiple structural and biophysical approaches.