scholarly journals Intermediate reactions in protein synthesis by the isolated cytoplasmic-membrane fraction of Bacillus megaterium

1959 ◽  
Vol 73 (2) ◽  
pp. 369-376 ◽  
Author(s):  
G D Hunter ◽  
P. Brookes ◽  
A. R. Crathorn ◽  
J. A. V. Butler
Keyword(s):  
Protein Synthesis ◽  
Bacillus Megaterium ◽  
Membrane Fraction ◽  
Cytoplasmic Membrane

FACTORS INVOLVED IN PROTEIN SYNTHESIS IN BACILLUS MEGATERIUM

1962 ◽  
Vol 40 (6) ◽  
pp. 709-716 ◽  
Author(s):  
Peter B. Hill
Keyword(s):  
Protein Synthesis ◽  
Snake Venom ◽  
Bacillus Megaterium ◽  
Ribonucleic Acid ◽  
Membrane Fraction ◽  
Orotic Acid ◽  
Similar Reduction

An isolated membrane fraction of lysed protoplasts of Bacillus megaterium incorporated S35methionine and C14orotic acid into proteinaceous and ribonucleic acid material respectively.After treatment of the membrane fraction with snake venom, a reduction in S35methionine incorporation was noted. Disruption of the phospholipid components in the isolated membrane caused a similar reduction in S35methionine incorporation. Evidence presented indicated the involvement of phospholipoprotein and ribonucleic acid in protein synthesis in the membrane of B. megaterium.

FACTORS INVOLVED IN PROTEIN SYNTHESIS IN BACILLUS MEGATERIUM

1962 ◽  
Vol 40 (1) ◽  
pp. 709-716
Author(s):  
Peter B. Hill
Keyword(s):  
Protein Synthesis ◽  
Snake Venom ◽  
Bacillus Megaterium ◽  
Ribonucleic Acid ◽  
Membrane Fraction ◽  
Orotic Acid ◽  
Similar Reduction

An isolated membrane fraction of lysed protoplasts of Bacillus megaterium incorporated S35methionine and C14orotic acid into proteinaceous and ribonucleic acid material respectively.After treatment of the membrane fraction with snake venom, a reduction in S35methionine incorporation was noted. Disruption of the phospholipid components in the isolated membrane caused a similar reduction in S35methionine incorporation. Evidence presented indicated the involvement of phospholipoprotein and ribonucleic acid in protein synthesis in the membrane of B. megaterium.

scholarly journals The High-Molecular-Weight Cytochrome c Cyc2 of Acidithiobacillus ferrooxidans Is an Outer Membrane Protein

2002 ◽  
Vol 184 (1) ◽  
pp. 313-317 ◽  
Author(s):  
Andrés Yarzábal ◽  
Gaël Brasseur ◽  
Jeanine Ratouchniak ◽  
Karen Lund ◽  
Danielle Lemesle-Meunier ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Outer Membrane ◽  
High Molecular Weight ◽  
Acidithiobacillus Ferrooxidans ◽  
Ferrous Iron ◽  
Membrane Fraction ◽  
Cytoplasmic Membrane ◽  
Respiratory Pathway ◽  
Membrane Components ◽  
Membrane Level

ABSTRACT A high-molecular-weight c-type cytochrome, Cyc2, and a putative 22-kDa c-type cytochrome were detected in the membrane fraction released during spheroplast formation from Acidithiobacillus ferrooxidans. This fraction was enriched in outer membrane components and devoid of cytoplasmic membrane markers. The genetics, as well as the subcellular localization of Cyc2 at the outer membrane level, therefore make it a prime candidate for the initial electron acceptor in the respiratory pathway between ferrous iron and oxygen.

scholarly journals The Action of Bacteriophage Ω8 on Two Strains of Escherichia coli 08

Microbiology ◽  
2000 ◽  
Vol 81 (1) ◽  
pp. 131-144 ◽  
Author(s):  
Barbara Wallenfels ◽  
K. Jann
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Phage Particle ◽  
Cytoplasmic Membrane ◽  
Cellular Respiration ◽  
Bacterial Strains ◽  
Viral Dna ◽  
Killing Effect ◽  
E Coli ◽  
Phage Propagation

Bacteriophage Ω8 is propagated in Escherichia coli E56b (08: K27-:H-), a non-capsulated strain. Another non-capsulated strain, E. coli 2398 (08:K?-:H-), is killed by bacteriophage Ω8 without phage propagation. This strain was formerly believed to be E. coli 093:K?-:H-, cross-reacting with strain E56b. We have established chemical and serological identity of the 08-specific lipopolysaccharides of the two strains. The 08-specific lipopolysaccharides of both strains inhibited the infection of Escherichia coli E56b with bacteriophage Ω8 equally well. The adsorption rate constants of Ω8 were identical for the two strains of E. coli 08. Evidence was obtained with 32P-labelled bacteriophage Ω8 for penetration of viral DNA into both bacterial strains. In host strain E56b, phage particle synthesis occurred normally. In strain 2398 the viral DNA was not degraded but its expression was blocked. The killing effect of Ω8 on E. coli strain 2398 is supposed to be due to damage of the cytoplasmic membrane, which could not be reversed under the influence of viral information. This was indicated by a blockage of cellular respiration, β-galactoside transport and RNA as well as protein synthesis.

Control of protein synthesis during the development of Acetabularia

Development ◽  
1971 ◽  
Vol 26 (2) ◽  
pp. 323-338
Author(s):  
Gabriel Ceron ◽  
E. Marshall Johnson
Keyword(s):  
Protein Synthesis ◽  
Membrane Fraction ◽  
Developmental Stages ◽  
Soluble Fraction ◽  
Protein Species ◽  
General Phenomenon ◽  
Protein Patterns ◽  
Electrophoretic Patterns ◽  
Zone Electrophoresis ◽  
Autoradiographic Analysis

Proteins from the soluble, chloroplastic and cell membrane fractions of axenically grown Acetabularia were analysed by zone electrophoresis. Incorporation of [14C]leucine into different proteins was measured by autoradiographic analysis of the electrophoretic patterns. The protein patterns from the soluble fraction remain constant with respect to the number of detectable bands but change with respect to the relative synthetic rates at various developmental stages. The protein patterns from the membrane fraction change with respect to both the number of protein species and the relative synthetic rates. The analysis of the synthetic performance of enucleated cells revealed that most of the proteins from the soluble and the membrane fractions continue to be synthesized in the absence of the nucleus and that the changes that normally occur in the protein patterns of the membrane fraction at the time of cap formation also take place in enucleated cells. This is taken as an indication that the control of the synthesis of the proteins studied is of extranuclear nature. It was also found that chloroplasts are capable of synthesizing all the components of the chloroplastic protein spectrum at least 4 weeks after enucleation. Some of the chloroplastic proteins can also be synthesized by purified chloroplasts in extracellular conditions. The possibility of extranuclear control of protein synthesis being a rather general phenomenon during the development of Acetabularia is discussed.

Phleomycin-stimulated solubilization of deoxyribonucleic acid in Escherichia coli. II. Inhibition of solubilization by bacteriophage T4

1976 ◽  
Vol 22 (5) ◽  
pp. 645-653 ◽  
Author(s):  
Larry D. Farrell ◽  
Harvard Reiter
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Deoxyribonucleic Acid ◽  
Cytoplasmic Membrane ◽  
Bacteriophage T4 ◽  
Continuous Exposure ◽  
Dna Endonuclease ◽  
Molecular Weights ◽  
Dependent Inhibition ◽  
Antibiotic Inhibition

Phleomycin-stimulated solubilization of Escherichia coli DNA is inhibited by infecting the cells with mutants of bacteriophage T4 before treatment with the antibiotic, inhibition requiring phage-specified protein synthesis. Two different modes of inhibition can be differentiated by infecting with mutants which are defective in an early state (gene den A−; endonuclease II-independent inhibition) or a late stage (gene 46−; endonuclease II-dependent inhibition) of phage-directed degradation of host DNA. Endonuclease II-independent inhibition results from interference with phleomycin-induced release of host DNA from the cytoplasmic membrane. In the presence of endonuclease II, the host DNA is converted to fragments, with average molecular weights of 106 daltons, the further degradation of which is not promoted by continuous exposure of the cells to phleomycin.

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