A conditionally lethal mutation of Escherichia coli affecting the gene coding for ribosomal protein S2 (rpsB).

Localized P1 mutagenesis has been used to isolate conditionally lethal mutations in the four-minute region of the Escherichia coli genome. One such mutation, ts25, has been mapped at about 3.7 minutes between the popC and dapD genes. This mutation leads to thermosensitivity of growth and impaired in vivo assembly of 30 S ribosomal subunits at 42 °C. The strain carrying the mutation has an altered S2 ribosomal protein as judged by (1) its inability to maintain stable complex with the ribosome under mild washing conditions and (2) its altered electrophoretic mobility.Spontaneous reversion to temperature independence can restore both the normal assembly in vivo of 30 S ribosomal subunits at 42 °C and the normal electrophoretic behaviour of the S2 ribosomal protein in vitro.We conclude therefore that the ts25 mutation affects the structural gene for ribosomal protein S2 (rpsB).     

Pentagastrin and adenosine 3',5'-cyclic monophosphate stimulated secretion of somatostatin from perfused rat gastric mucosa.

Immunoreactive somatostatin is secreted by rat gastric mucosa perifused $\text{in vitro}$. Somatostatin release is stimulated by pentagastrin and cyclic AMP with theophylline. These results suggest that gastric mucosal somatostatin may have a paracrine action as feedback inhibitor of gastrin secretion.     

Valine-resistant plants from in vitro selected tobacco cells

Summary Growth inhibition of protoplasts and cells of tobacco (Nicotiana tabacum L.) occurs when 0.1 to 10 mM L-valine is present in the culture medium but not if L-isoleucine is simultaneously added. Mesophyll protoplasts from haploid tobacco were submitted to ultraviolet irradiation and cell colonies derived from these protoplasts were plated in a medium containing valine. Plants were regenerated from five presumptive resistant calli and retested for valine-resistance. Among the recovered plants two were definitely resistant to valine. This trait was transmitted in sexual crosses as a mendelian character.     

Immune response gene(s) controlling the humoral antilysozyme response (Ir-Lys) linked to the major histocompatibility complexSL-A in the pig

A genetic control of humoral immune response in pigs against hen egg-white lysozyme was shown to be linked to the major histocompatibility complexSLA. This control was detected when high antigen doses were used for immunization. It was more prominent with small immunizing doses of lysozyme. Under these latter conditions,SL- A heterozygous individuals exhibited a higher response than correspondingSL- A homozygous animals, suggesting a complementation phenomenon between several genes, at least one of which is linked to the porcine MHC,SL- A.     

Méthylations biologiques chez le crabe Carcinus maenas; inhibition in vitro par une fraction purifiée extraite des glandes androgènes

Extracts from muscles, testis, seminal vesicles and ovaries of the Crab, Carcinus maenas, have been studied in vitro, in presence of [¹⁴C]-methyl S-adenosylmethionine, with an E. coli tRNA as methyl acceptor. The highest level of methylases is found in the testis. It has been reported previously that a purified fraction extracted from the androgenic glands of Carcinus maenas inhibits the vitellogenesis in ovaries. We now show that the same fraction inhibits tRNA methylation in an extract of testis as methylase; a 50 per cent inhibition is obtained with about 10 μg of a purified fraction corresponding to 15 glands. With an enzymatic preparation from the ovaries, a 50 per cent inhibition of the tRNA methylase is observed with the purified extract from 4 glands.     

Studies of soluble rat liver mitochondrial acid ATPases: II. Structural and immunological properties of ATPase 1

We described previously the existence of a soluble ATPase activity in rat liver mitochondria [1]. The purification and catalytic properties have been described [2]. In a continuation of these experiments, we have studied the immunologic and structural properties of one molecular form of this enzyme: ATPase I.We have prepared the antiserum anti-ATPase I and demonstrated the purity of our enzyme preparation by immunodiffusion and immunoelectrophoresis. An immunohistochemical method also confirmed the localization of ATPase I in the soluble fraction of mitochondria.The molecular weight of ATPase I was measured by G 100 Sephadex gel filtration and was found to be 18,400; electrophoresis on polyacrylamide gels gave a value of 18,600. The pHi of ATPase I was found to be 7,2.Amino acid analysis showed high amounts of aspartic acid, glutamic acid, serine and glycine. The molecular weight calculated from the total amino acid residues was found to be 17,000.Alanine is the NH2 terminal amino acid.The peptide maps obtained after degrading ATPase I with cyanogen bromide or trypsin are in accordance with the methionine, lysine and arginine residues we found in the ATPase I molecule.ATPase I does not appear to be a glycoprotein.     

Presence de pollens d'Hamamelis (Hamamelidaceae,Angiospermae) dans le pliocene du Sud de la France

Pollen-analysis shows the presence of the genus Hamamelis in the pliocene flora of southern France. It contributesto the knowledge of the past distribution of taxa which are now extinct in western Europe.     

L'espece Pecopteris simoni (Zeiller, 1886–1888)sunonyme posterieur de Palaeoweichselia defrancei (Brongniart, 1828)

Recent examination of the type specimen of Pecopris simoni ZEILLER (1) leads to the conclusion of the identityof that species with Palaeoweichselia defrancei (BRONGNIART) (2), which is also confirmed by the stratigraphic occurence.     

Carbohydrate-peptide linkage in glycoproteins

The secondary structure of the peptide segment around the carbohydrate-peptide linkage in glycoproteins was predicted by using the Chou and Fasman determination. Such a study was carried out for 9 O-glycosidically linkages and 28 N-glycosidically linkages. In the case of O-glycosidically linkages, the residue Ser or Thr involved in the linkage always belongs to a β-turn. In the case of N-glycosidically linkages, 19 out of the 28 Asn studied belong to a β-turn. A predicted determination concerning the whole protein moiety of 9 glycoproteins in order to obtain some information concerning the spatial organization of the entire glycoprotein was carried out also. It seems that carbohydrate moiety takes place outside the glycoprotein.