THE EFFECT OF ACTINOBOLIN ON NUCLEIC ACID AND PROTEIN SYNTHESIS IN ESCHERICHIA COLI

1966 ◽  
Vol 12 (3) ◽  
pp. 515-520 ◽  
Author(s):  
D. E. Hunt ◽  
R. F. Pittillo ◽  
E. P. Johnson ◽  
F. C. Moncrief
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Nucleic Acid ◽  
Mechanism Of Action ◽  
Rna Synthesis ◽  
The Other ◽  
Cross Resistance ◽  
Inhibition Of Protein Synthesis

Actinobolin inhibits protein synthesis in Escherichia coli. When the antibiotic is added to a culture at the time of inoculation, RNA synthesis is also inhibited. Inhibition of RNA synthesis appears to be a consequence of inhibition of protein synthesis. Cross-resistance experiments suggest that the mechanism of action of actinobolin differs from that of the other inhibitors of protein synthesis, chloramphenicol and sparsomycin. Phenylalanine prevents the action of actinobolin provided the amino acid and antibiotic are added simultaneously; this effect is not observed if the phenylalanine is added 1 hour after the addition of the antibiotic. Evidence is presented that the mechanism by which phenylalanine prevents inhibition by actinobolin differs from that which has been suggested for azaserine and p-fluorophenylalanine.

MICROBIOLOGICAL STUDIES ON THE MECHANISM OF ACTION OF SPARSOMYCIN

1966 ◽  
Vol 12 (4) ◽  
pp. 595-604 ◽  
Author(s):  
Edward R. Bannister ◽  
Dale E. Hunt ◽  
Robert F. Pittillo
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Mechanism Of Action ◽  
Rna Synthesis ◽  
Primary Site ◽  
Cross Resistance ◽  
E Coli

A primary site of sparsomycin attack in Escherichia coli appears to be inhibition of synthesis of protein, which occurs at concentrations of sparsomycin that do not affect DNA or RNA synthesis. Sparsomycin interferes with the normal excretion of amino acids by E. coli. Some cross-resistance was observed between a culture resistant to sparsomycin and cultures resistant to other inhibitors of protein synthesis.

Relationship between ppGpp levels and rates of protein and RNA synthesis in Escherichia coli

1976 ◽  
Vol 54 (3) ◽  
pp. 291-295 ◽  
Author(s):  
Gillian Chaloner-Larsson ◽  
Hiroshi Yamazaki
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Inverse Relationship ◽  
Rna Synthesis ◽  
Amino Acid Starvation ◽  
Cellular Proteins ◽  
Mrna Species ◽  
Protein And Rna Synthesis ◽  
Rna And Protein Synthesis

When amino acid starvation is ended in stringent (relA+) strains of Escherichia coli, the rates of RNA and protein synthesis as well as their accumulation return to normal more slowly in spoT− strains than in the spoT+ strains. The level of ppGpp accumulated declines more slowly in the spoT− strains than in the spoT+ strains. Thus, there is an inverse relationship between ppGpp levels and the rates of RNA and protein synthesis. The slow resumption of protein synthesis in the spoT−relA+ strains could therefore be explained in terms of the limited synthesis of mRNA species coding for the bulk of cellular proteins.

Infection of Escherichia coli with bacteriophages

1969 ◽  
Vol 27 ◽  
pp. 370-371
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Nucleic Acid ◽  
Cell Surface ◽  
Virus Type ◽  
Infection Process ◽  
Adsorption Site ◽  
The Other ◽  
Specific Receptors ◽  
Bacterial Receptors

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.

scholarly journals Lethal Action of Quinolones against a Temperature-Sensitive dnaB Replication Mutant of Escherichia coli

2006 ◽  
Vol 50 (1) ◽  
pp. 362-364 ◽  
Author(s):  
Xilin Zhao ◽  
Muhammad Malik ◽  
Nymph Chan ◽  
Alex Drlica-Wagner ◽  
Jian-Ying Wang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Dna Replication ◽  
Nalidixic Acid ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Lethal Action ◽  
Inhibition Of Protein Synthesis

ABSTRACT Inhibition of DNA replication in an Escherichia coli dnaB-22 mutant failed to block quinolone-mediated lethality. Inhibition of protein synthesis by chloramphenicol inhibited nalidixic acid lethality and, to a lesser extent, ciprofloxacin lethality in both dnaB-22 and wild-type cells. Thus, major features of quinolone-mediated lethality do not depend on ongoing replication.

scholarly journals Activities of Atazanavir (BMS-232632) against a Large Panel of Human Immunodeficiency Virus Type 1 Clinical Isolates Resistant to One or More Approved Protease Inhibitors

2003 ◽  
Vol 47 (4) ◽  
pp. 1324-1333 ◽  
Author(s):  
Richard J. Colonno ◽  
Alexandra Thiry ◽  
Kay Limoli ◽  
Neil Parkin
Keyword(s):  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
The Other ◽  
Clinical Isolates ◽  
Cross Resistance ◽  
Resistance Profile ◽  
Immunodeficiency Virus

ABSTRACT To evaluate the cross-resistance profile of the human immunodeficiency virus type 1 protease inhibitor (PI) atazanavir (BMS-232632), a panel of 551 clinical isolates exhibiting a wide array of PI resistance profiles and a variety of genotypic patterns were assayed for susceptibility to atazanavir and six other PIs: amprenavir, indinavir, lopinavir, nelfinavir, ritonavir, and saquinavir. In general, reductions in atazanavir susceptibility in vitro required several amino acid changes and were relatively modest in degree, and susceptibility was retained among isolates resistant to one or two of the currently approved PIs. There was a clear trend toward loss of susceptibility to atazanavir, as isolates exhibited increasing levels of cross-resistance to multiple PIs. Atazanavir appeared to have a distinct resistance profile relative to each of the other six PIs tested based on susceptibility comparisons against this panel of resistant isolates. Analysis of the genotypic profiles of 943 PI-susceptible and -resistant clinical isolates identified a strong correlation between the presence of amino acid changes at specific residues (10I/V/F, 20R/M/I, 24I, 33I/F/V, 36I/L/V, 46I/L, 48V, 54V/L, 63P, 71V/T/I, 73C/S/T/A, 82A/F/S/T, 84V, and 90M) and decreased susceptibility to atazanavir. While no single substitution or combination of substitutions was predictive of atazanavir resistance (change, >3.0-fold), the presence of at least five of these substitutions correlated strongly with loss of atazanavir susceptibility. Mutations associated with reduced susceptibility to each of the other six PIs were also determined.

Sign in / Sign up

Export Citation Format

Share Document