Synaptonemal complexes and meiosis in myxomycetes

Synaptonemal complexes (SC) have been observed in spores 18–24 hr past cleavage in natural fruitings of Physarum cinereum, P. bogoriense, Hemitrichia stipitata, Tubifera ferruginosa, and Arcyria incarnata. Laboratory fruitings of Arcyria cinerea, Stemonitis herbatica, and a homothallic isolate of Physarum pusillum also have SC's present in spores during the same postcleavage period. The presence of these paired chromosomes of meiotic prophase in spores of species collected in nature and in a diversity of taxa suggests that the usual position of meiosis in Myxomycetes is inside the postcleavage spore. Criteria are proposed for evaluating the validity of the SC as an indicator of meiosis.     

Evidence that free GPI glycolipids are essential for growth of Leishmania mexicana.

The cell surface of the parasitic protozoan Leishmania mexicana is coated by glycosylphosphatidylinositol (GPI)-anchored glycoproteins, a GPI-anchored lipophosphoglycan and a class of free GPI glycolipids. To investigate whether the anchor or free GPIs are required for parasite growth we cloned the L.mexicana gene for dolichol-phosphate-mannose synthase (DPMS) and attempted to create DPMS knockout mutants by targeted gene deletion. DPMS catalyzes the formation of dolichol-phosphate mannose, the sugar donor for all mannose additions in the biosynthesis of both the anchor and free GPIs, except for a alpha1-3-linked mannose residue that is added exclusively to the free GPIs and lipophosphoglycan anchor precursors. The requirement for dolichol-phosphate-mannose in other glycosylation pathways in L.mexicana is minimal. Deletion of both alleles of the DPMS gene (lmdpms) consistently resulted in amplification of the lmdpms chromosomal locus unless the promastigotes were first transfected with an episomal copy of lmdpms, indicating that lmdpms, and possibly GPI biosynthesis, is essential for parasite growth. As evidence presented in this and previous studies indicates that neither GPI-anchored glycoproteins nor lipophosphoglycan are required for growth of cultured parasites, it is possible that the abundant and functionally uncharacterized free GPIs are essential membrane components.     

Typification of Linnaean taxa of annual Poaceae: Poeae related to Vulpia and Desmazeria

STACE, C. A. & JARVIS, C. E., 1985. TypiHcation of Linnaean taxa of annual Poaceae: Poeae related to Vulpia and Desmazeria. The status and typification of 15 Linnaean species of annual grasses related to Vulpia and Desmazeria are discussed. Of these 15, eight are represented by holotypes or lectotypes in LINN, two by lectotypes in Herb. A. van Royen (L), and one by a neotype in LINN. One (Festuca marina) is based on a pre-Linnaean polynomial and is represented by a lectotype in Herb. Sloane (BM); one (Cynosurus durus) has no known type specimens and we have chosen a Barrelier (1714) illustration as lectotype; one (Nardus aristatus) is an illegitimate name change for Nardus incurvus Gouan, for which we have selected a Scheuchzer (1719) illustration as lectotype; and finally Festuca incrassala appeared on a cancelled page of Species Plantarum and has no nomenclatural standing.     

State of aggregation of the (Ca2+ + Mg2+)-ATPase studied using saturation-transfer electron spin resonance

The state of aggregation of the (Ca2+ + Mg2+)-ATPase in the membrane of sarcoplasmic reticulum and in reconstituted membrane systems has been studied using saturation-transfer electron spin resonance (ST-ESR). Saturation-transfer ESR spectra show that in the sarcoplasmic reticulum, the ATPase is relatively free to rotate, with an effective rotational correlation time of approx. 33 microseconds at 4 degrees C, consistent with a monomeric or dimeric structure. The rate of rotation is observed to decrease with decreasing molar ratio of lipid to protein. In reconstituted systems, rotational motion of the ATPase on the millisecond time scale ceases when the lipids are in the gel phase. Addition of decavanadate, which causes the formation of crystalline arrays in negatively stained electron micrographs, results in only a small reduction in rotation rate for the ATPase in the membrane. The experiments are interpreted in terms of a short-lived (on the millisecond time scale) protein-protein interaction, with the formation of crystalline clusters of ATPase molecules which form and melt rapidly.