Über die Untersuchungen von A. H. Blaauw,betreffend die Beziehung zwischen Lichtintensität und Beleuchtungsdauer bei der phototropischen Krümmung von Keimlingen vonAvena sativa

Ohne ZusammenfassungProceedings of the Meetings of Saturday September 26, 1908.Die vorliegende Übersetzung, zu der Herr Prof. Went mich gütigst autorisierte, rechtfertigt sich durch die in theoretischer, ganz besonders aber in methodologischer Hinsicht überaus wichtigen Ergebnisse Blaauws. Die Untersuchung bestätigt zunächst ein Gesetz, das der Übersetzer für die Abhängigkeit der Präsentationszeit von der Lichtintensität festgestellt hat (die diesbezügliche Abhandlung war Herrn Prof. Went zur Zeit, als er dieses Referat schrieb, noch nicht zu Gesicht gekommen), verfolgt aber diese Gesetzmäßigkeit innerhalb wesentlich weiterer Grenzen. Die Feststellung ganz besonders, daß bei entsprechend intensiver Beleuchtung die Präsentationszeit bis auf 1/1000 Sekunde sinkt, zusammengehalten mit den Tatsachen der feinen Unterschiedsempfind-lichkeit der Pflanzen (Wiesner) und der außerordentlich kurzen Perzeptions-zeit (Fitting), muß die reizphysiologische Methodik reformieren und sie zu ebenso exaktem Arbeiten anspornen, wie es bei psychophysischen Experimenten längst der Fall ist.     

Physiology of the ECL cells.

The enterochromaffin-like (ECL) cells of the oxyntic mucosa (fundus) of the stomach produce, store and secrete histamine, chromogranin A-derived peptides such as pancreastatin, and an unanticipated but as yet unidentified peptide hormone. The cells are stimulated by gastrin and pituitary adenylate cyclase activating peptide and suppressed by somatostatin and galanin. Choline esters and histamine seem to be without effect on ECL cell secretion. The existence of a gastrin-ECL cell axis not only explains how gastrin stimulates acid secretion but also may help to explore the functional significance of the ECL cells with respect to the nature and bioactivity of its peptide hormone. From the results of studies of gastrectomized/fundectomized and gastrin-treated rats, it has been speculated that the anticipated ECL-cell peptide hormone acts on bone metabolism.     

Chromosomal location and cloning of the gene (trmD) responsible for the synthesis of tRNA (m1G) methyltransferase in Escherichia coli K-12

Summary The trmD gene, which governs the formation of 1-methyl-guanosine (m¹G) in transfer ribonucleic acid (tRNA), has been located by phage P1 transduction at 56 min on the chromosomal map of Escherichia coli. Cotransduction to tyrA at 56 min is 80%. From the Clarke and Carbon collection a ColE1-tyrA ⁺ hybrid plasmid was isolated, which carried the trmD ⁺ gene and was shown to over-produce the tRNA (m¹G)methyltransferase. By subcloning restriction enzyme fragments in vitro, the trmD ⁺ gene was located to a 3.4 kb DNA fragment 6.5 kb clockwise from the tyrA ⁺ gene. The mutation trmD1, which renders the tRNA (m¹G) methyltransferase temperaturesensitive both in vivo and in vitro could be complemented by trmD ⁺ plasmids. These results suggest that the gene trmD ⁺ is the structural gene for the tRNA (m¹G)methyltransferase (EC 2.1.1.3.1).     

The membrane topology of proton-pumping Escherichia coli transhydrogenase determined by cysteine labeling.

The membrane topology of proton-pumping nicotinamide-nucleotide transhydrogenase from Escherichia coli was determined by site-specific chemical labeling. A His-tagged cysteine-free transhydrogenase was used to introduce unique cysteines in positions corresponding to potential membrane loops. The cysteines were reacted with fluorescent reagents, fluorescein 5-maleimide or 2-[(4'-maleimidyl)anilino]naphthalene-6-sulfonic acid, in both intact cells and inside-out vesicles. Labeled transhydrogenase was purified with a small-scale procedure using a metal affinity resin, and the amount of labeling was measured as fluorescence on UV-illuminated acrylamide gels. The difference in labeling between intact cells and inside-out vesicles was used to discriminate between a periplasmic and a cytosolic location of the residues. The membrane region was found to be composed of 13 helices (four in the alpha-subunit and nine in the beta-subunit), with the C terminus of the alpha-subunit and the N terminus of the beta-subunit facing the cytosolic and periplasmic sides, respectively. These results differ from previous models with regard to both number of helices and the relative location and orientation of certain helices. This study constitutes the first in which all transmembrane segments of transhydrogenase have been experimentally determined and provides an explanation for the different topologies of the mitochondrial and E. coli transhydrogenases.