THE EFFECT OF 3000–4000 Å LIGHT ON THE SYNTHESIS OF β-GALACTOSIDASE AND BACTERIOPHAGES BY ESCHERICHIA COLI B

1967 ◽  
Vol 13 (1) ◽  
pp. 69-79 ◽  
Author(s):  
S. J. Webb ◽  
J. Singh Bhorjee

The irradiation of Escherichia coli B with sublethal doses of 3000–4000 Å light prevented the microorganisms from manufacturing β-galactosidase and T2 and T7 coliphages. Inhibition occurred only if the cells were irradiated immediately after their contact with the inducer lactose or infection with T2 and T7 phages. If, before irradiation the cells were allowed to incubate for 15 min after the addition of lactose or the coliphages to the cells, little effect of the light was found. The uptake of uracil and amino acids by washed cells was more rapid in the first 15 min than during later time periods while thymine uptake did not begin until the first 15 min had elapsed. The 3000–4000 Å light inhibited the uptake of arginine and thymine but not uracil or glutamic acid. The addition of 5% inositol inhibited the synthesis of β-galactosidase and the uptake of14C-labelled metabolites. Since there was a strong correlation between the degree to which arginine and thymine uptakes were inhibited by the light or inositol, it appears that the production of a protein during the first 15 min is intimately connected with DNA replication and the synthesis of induced enzymes.

1975 ◽  
Vol 21 (6) ◽  
pp. 828-833 ◽  
Author(s):  
C. Simard ◽  
A. Mardini ◽  
L. M. Bordeleau

The molecular weight, sedimentation coefficient, and amino acids composition were determined on five tryptophanases (TPases) from Escherichia coli B and E. aurescens, Shigella alkalescens, and Proteus vulgaris and P. morganii. These TPases have identical sedimentation profile and coefficient (9.6 S), and the same molecular weight (220 000). Each enzyme is constituted of four identical subunits having a molecular weight of 55 000. The amino acids composition of these TPases is very similar, with the exception of P. morganii and P. vulgaris TPases which present significative variations in basic amino acids and tryptophan content. The species differentiation of the coli group cannot be made on their TPase characteristics only, contrary to P. morganii and P. vulgaris which can be differentiated between them and from the coli group. [Journal translation]


2020 ◽  
Vol 117 (46) ◽  
pp. 28572-28575
Author(s):  
Masayori Inouye ◽  
Risa Takino ◽  
Yojiro Ishida ◽  
Keiko Inouye

Among the 20 amino acids, three of them—leucine (Leu), arginine (Arg), and serine (Ser)—are encoded by six different codons. In comparison, all of the other 17 amino acids are encoded by either 4, 3, 2, or 1 codon. Peculiarly, Ser is separated into two disparate Ser codon boxes, differing by at least two-base substitutions, in contrast to Leu and Arg, of which codons are mutually exchangeable by a single-base substitution. We propose that these two different Ser codons independently emerged during evolution. In this hypothesis, at the time of the origin of life there were only seven primordial amino acids: Valine (coded by GUX [X = U, C, A or G]), alanine (coded by GCX), aspartic acid (coded by GAY [Y = U or C]), glutamic acid (coded by GAZ [Z = A or G]), glycine (coded by GGX), Ser (coded by AGY), and Arg (coded by CGX and AGZ). All of these were derived from GGX for glycine by single-base substitutions. Later in evolution, another class of Ser codons, UCX, were derived from alanine codons, GCX, distinctly different from the other primordial Ser codon, AGY. From the analysis of theEscherichia coligenome, we find extensive disparities in the usage of these two Ser codons, as some genes use only AGY for Ser in their genes. In contrast, others use only UCX, pointing to distinct differences in their origins, consistent with our hypothesis.


1971 ◽  
Vol 17 (7) ◽  
pp. 865-869 ◽  
Author(s):  
B. Sue Criswell ◽  
Judith H. Marston ◽  
Wayne A. Stenback ◽  
S. H. Black ◽  
Herman L. Gardner

The fine structure of Haemophilus vaginalis 594 (ATCC 14018) was examined by electron microscopy, and the biochemical composition of its cell wall was determined. For comparison, similar studies were done with a Gram-positive bacterium, Bacillus megaterium KM, and a Gram-negative bacterium, Escherichia coli B. Both Haemophilus vaginalis 594 and Escherichia coli B possessed a multiple-layered cell wall containing 11 to 14 amino acids, a low mucopeptide content, and no teichoic acid. In contrast, Bacillus megaterium KM had a thick, amorphous cell wall with five amino acids, high mucopeptide content, and detectable amounts of teichoic acid. Haemophilus vaginalis 594 resembled Escherichia coli, a member of the Gram-negative group of organisms. The structural and biochemical properties of Haemophilus vaginalis, which are described in detail, may prove useful in determining the ultimate taxonomic position of this species.


1957 ◽  
Vol 3 (7) ◽  
pp. 967-974 ◽  
Author(s):  
J. M. McLaughlan

Cystine, cysteinesulphinic acid (CSA), and other closely related sulphur-containing amino acids inhibited growth of Escherichia coli 113-3, particularly in aerobic conditions. The cystine inhibition was completely prevented by aspartic acid, partially reversed by pantothenic acid or β-alanine and slightly reversed by lysine or thiamine. The inhibitory effect of CSA was completely or partially reversed by aspartic acid, lysine, glutamic acid, proline, ornithine, or homoserine. Aspartic acid and glutamic acid appeared to reverse the inhibition competitively while lysine seemed to reverse the inhibition in a noncompetitive manner. Reversal of the inhibitory effect of relatively high concentrations of CSA by lysine was not complete, however, unless methionine was also present. Possible mechanisms of the cystine and CSA inhibition are discussed.


1967 ◽  
Vol 13 (3) ◽  
pp. 257-269
Author(s):  
S. J. Webb ◽  
Janet L. Walker

When cells of Escherichia coli B were grown in a glucose – amino acid medium and then transferred to a minimal medium containing lactose or isopropyl-β-D-thiogalactopyranoside as a sole source of carbon, no induction of β-galactosidase occurred unless one or several amino acids were supplied. Of the amino acids tested, aspartic acid was the most effective and its ability to initiate the synthesis of the enzyme was increased by the addition of arginine. In the presence of these two, or all of the amino acids, there was a lag period of 10 min before enzyme synthesis occurred. The duration of the lag period was unaffected by the addition of nucleic acid bases or succinate to the induction medium. Succinate or glutamate partially inhibited the synthesis of the enzyme, whereas glucose, inositol, or chloramphenicol completely suppressed it. With the exception of that produced by chloramphenicol, inhibition was dependent on the time at which the inhibitor was added. If inhibitors were added after the 10-min lag period, they had no apparent effect until 45 min had elapsed. Cells transferred after 15 min from one induction medium to another displayed for 30 min the induction characteristics of the first medium. It appears that a process occurring during the early 15-min period determines the rate at which enzymes will be synthesized for the next 30 min and that the action of inhibitors is to prevent this process. The process seems to require intact DNA and amino acids and it is suggested that it determines the specificity and quantity of mRNA manufactured.


Sign in / Sign up

Export Citation Format

Share Document