Mutation in Saccharomyces cerevisiae Conferring Streptomycin and Cold Sensitivity by Affecting Ribosome Formation and Function

A cold-sensitive, streptomycin-sensitive mutant of Saccharomyces cerevisiae accumulates a 28S ribonucleoprotein particle when grown at low temperature. This particle contains 17S ribosomal ribonculeic acid which is degraded when exposed to ribonuclease. The particle does not serve as a precursor to 60 and 40S ribosomal subunits nor is it turned over when growth is allowed to resume at the permissive temperature; rather it is only diluted by growth. That streptomycin sensitivity (allelic with cold sensitivity) is ribosomal is evidenced by the inhibition of protein synthesis in vitro by streptomycin and the binding of labeled streptomycin to the mutant but not the parental 40S ribosomal subunit.     

The macronuclear envelope of Tetrahymena pyriformis GL in different physiological states

Summary Macronuclear envelopes were isolated from the ciliated protozoan Tetrahymena pyriformis GL, negatively stained and examined in the electron microscope. The frequency of central granules in the macronuclear pores was evaluated in five different physiological states: (1) stationary phase of growth, (2) exponential phase of growth, (3) heat-synchronized cultures at the end of the heat-synchronization treatment, (4) heat-synchronized cultures at the beginning of the first division, (5) heat-synchronized cultures at the end of the first division.The percentage of pores containing a central granule was markedly enhanced in heatsynchronized cultures at the end of the first division, i.e. a state known for an increase in ribosome formation. Actinomycin D was found to cause a significant decrease in central granule frequency.The observed alterations in central granule frequency seem to confirm the hypotheses which consider the central granule as representing a ribonucleoprotein particle in transit from nucleus to cytoplasm through the nuclear pore.For careful technical assistance I am indebted to Miss Marianne Whiter as well as to Drs. H. Falk, W.W. Franke and P. Sitte for helpful discussions. This work was supported in part by the Deutsche Forschungsgemeinschaft.     

Die Fimbrien von Rhizobium lupini 1/50, sta-

Zusammenfassung Die Fimbrien (oder Pili) einer nicht sternbildenden Mutante (1–50, sta^-) von Rhizobium lupini wurden elektronenmikroskopisch untersucht. Die Fimbien sind peritrich an der Bakterienzelle inseriert, und zwar während der exponentiellen Wachstumsphase meist einzeln. In der stationären Phase nehmen die Fimbrien an Zahl und Länge kontinuierlich stark zu; sie sind dann häufig büschelweise inseriert. Zusammen mit den oft zopfbildenden Geißeln verflechten sie sich zu einem ausgedehnten Netzwerk. Die Aneinanderlagerung der Fimbrien erfolgt unspezifisch durch Kohäsion; durch ebenfalls unspezifische Adhäsion haften sie auf dem Substrat.Die Fimbrien haben ca. 30 Å Durchmesser und sind röhrenförmig gebaut. Ihre lichte Weite beträgt 8 bis 10 Å. Ein allgemeines Bauschema der Fimbrien wird diskutiert. In der Diskussion über die allgemeine Funktion aller Arten von Fimbrien wird ihre Haftfähigkeit herausgestellt. Die Fimbrien der Mutante 1/50, sta^- sind wegen ihres geringen Innendurchmessers nicht als Transportröhren für doppelsträngige DNS und wahrscheinlich auch nicht für einzelsträngige DNS oder RNS geeignet.

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The fimbriae of Rhizobium lupini 1/50, sta^-

Summary The fimbriae (pili) of a non-starforming mutant (1/50, sta^-) of Rhizobium lupini were studied under the electron microscope. In the exponential phase of growth, fimbriae are singly, peritrichously inserted. During stationary growth these fimbriae increase by number and length. Together with the larger flagella they often form an extended reticulum. The fimbriae often stick together by unspecific cohesion forces; their attachment to the substrate can be explained by unspecific adhesion.The outer diameter of the fimbriae is 30 Å, the inner diameter 8 to 10 Å.The tubelike structure of fimbriae (pili) is discussed in terms of a general model.The most obvious general function of all types of fimbriae is their connecting power.The inner dimension of the fimbriae of the 1/50, sta^-—mutant exclude a model where they function as transport tubes for double-stranded DNA and probably for single stranded DNA or RNA either.

     

Microbodies (peroxisomes) in the toad,Bufo marinus

Summary Microbodies (peroxisomes), a group of cytoplasmic organelles enriched in catalase, are demonstrated in the toad, Bufo marinus, by light and electron microscopy by means of a cytochemical staining procedure that demonstrates the peroxidatic activity of catalase with diaminobenzidine (DAB). Amphibian microbodies are similar to those of other classes in their fine structure and localization in hepatocytes and kidney, where they are prominent in the proximal tubular cells. Nucleoids are present only in renal microbodies. In the proximal renal tubule an unusual group of large brown granules are identified as lysosomes by their acid phosphatase, -glucosaminidase and -glucuronidase activities.This work was supported by U.S. Public Health Service Grants Nos. NS-06856 and HD 00674. We wish to thank Dr. Richard M. Hays who generously supplied us with toads; Dr. Alex B. Novikoff for making available facilities for ultramicrotomy, Miss Betty De Prest for technical assistance; Miss Marianne Van Hooren for preparation of the photomicrographs.