ON THE ORIGINS OF THE OVULE AND CUPULE IN LYGINOPTERID PTERIDOSPERMS

Camp, Wendell H., and Mary M. Hubbard. (U. Connecticut, Storrs.) On the origins of the ovule and cupule in Lyginopterid pteridosperms. Amer. Jour. Bot. 50(3): 235–243. Illus. 1963.—The recently described Eurystoma angulare of the Lower Carboniferous with its naked, dichotomously branched, ovule-bearing branch truss may be taken conceptually as a starting point in a series of evolutionary reductions and modifications involving other known forms which ultimately led to the cupule surrounding the solitary ovule of later lyginopterids. It is postulated that the integuments of these ovules also were derived from dichotomously branched lateral trusses which immediately subtended the primitive megasporangia, but of less complexity than that which produced the cupule. Eurystoma indicates that ovules evolved independently of leaves; therefore, ovules cannot be thought of as having been derived from leaf tissues. Evidence is presented indicating that, although these pteridosperms produced ovules of considerable complexity, they did not bear seeds but dropped the pollinated ovules before fertilization. The already specialized organization of the ovules of the Lower Carboníferous pteridosperms indicates that the group must have originated in the Devonian. The structure of the Lyginopterid ovule is reinterpreted, indicating a basic similarity to that of the angiospermous ovule.     

Calretinin: Modulator of neuronal excitability

Calretinin is a member of the calcium-binding protein EF-hand family first identified in the retina. As with the other 200-plus calcium-binding proteins, calretinin serves a range of cellular functions including intracellular calcium buffering, messenger targeting, and is involved in processes such as cell cycle arrest, and apoptosis. Calcium-binding proteins including calretinin are expressed differentially in neuronal subpopulations throughout the vertebrate and invertebrate nervous system and their expression has been used to selectively target specific cell types and isolate neuronal networks. More recent experiments have revealed that calretinin plays a crucial role in the modulation of intrinsic neuronal excitability and the induction of long-term potentiation (LTP). Furthermore, selective knockout of calretinin in mice produces disturbances of motor coordination and suggests a putative role for calretinin in the maintenance of calcium dynamics underlying motor adaptation.     

Mitochondria DNA synthesis in oocytes of Xenopus laevis

The process of attachment was studied in primary mouse kidney epithelial cell cultures by means of reflexion contrast microscopy, a method developed for studying the cell membrane-substrate relationship. The first in a series of events is simple adherence to the substrate, called close contact. This phenomenon is associated with the greatest extension of lamellar cytoplasm and the fewest number of cell nuclei/unit area. The nuclei of such cells are in close contact with the bottom portion of the cell membrane. Approx. 24 h after planting, as the cultures become more crowded, cells develop a different kind of attachment to the substrate—focal contacts—that are correlated with a decrease in lamellar cytoplasm. Cells detached from the substrate after close contact formation readily reattach, while cells detached after formation of focal contacts do not reattach. After incubation for periods greater than 5 days, the dense cultures degenerate and cells lose their attachment to the glass surface.     

A β-1,4-endoglucanase-encoding gene from Cellulomonas pachnodae

 A gene library of Cellulomonas pachnodae was constructed in Escherichia coli and was screened for endoglucanase activity. Five endoglucanase-positive clones were isolated that carried identical DNA fragments. The gene, designated cel6A, encoding an endoglucanase enzyme, belongs to the glycosyl hydrolase family 6 (cellulase family B). The recombinant Cel6A had a molecular mass of 53 kDa, a pH optimum of 5.5, and a temperature optimum of 50–55 °C. The recombinant endoglucanase Cel6A bound to crystalline cellulose and beech litter. Based on amino acid sequence similarity, a clear cellulose-binding domain was not distinguished. However, the regions in the Cel6A amino acid sequence at the positions 262–319 and 448–473, which did not show similarity to any of the known family-6 glycosyl hydrolases, may be involved in substrate binding. Received: 14 January 1999 / Received revision: 29 March 1999 / Accepted: 6 April 1999     

FINE STRUCTURE OF CHLOROPLASTS IN “GREEN ISLANDS” AND IN SURROUNDING CHLOROTIC AREAS OF BARLEY LEAVES INFECTED BY POWDERY MILDEW

The fine structure of mesophyll chloroplasts in green islands and in adjacent chlorotic areas of barley leaves infected with Erysiphe graminis (DC.) was compared with healthy non-inoculated tissue. Chloroplasts in green islands were persistent. Green-island chloroplast grana were enlarged and fewer in number than in healthy tissue. In contrast, cells in chlorotic areas had fewer chloroplasts and their lamellae showed progressive degeneration and fragmentation. The lamellae often resembled aberrant prolamellar bodies. As lamellar degeneration progressed there was a marked increase in the amount of osmophilic material within the chloroplasts.