Messenger Ribonucleic Acid Synthesis and Degradation in
            <i>Escherichia coli</i>
            During Inhibition of Translation

Pato, Martin L.; Bennett, Peter M.; Meyenburg, Kaspar von

doi:10.1128/jb.116.2.710-718.1973

Cited by 66 publications

(37 citation statements)

References 28 publications

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“…It has been postulated that polypeptides might be synthesized on correspondingly small fragments of mRNA in CHL-treated cells (29). However, we and others have found only sizable mRNA chains (primarily 12S to 16S) on ribosomes after CHL treatment or EFG inactivation (Fig.…”

Section: Discussionmentioning

confidence: 57%

Polypeptide Formation and Polyribosomes in Escherichia coli Treated with Chloramphenicol

1974

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In Escherichia coli cultures maximally inhibited with chloramphenicol, formation of polypeptides still.continued at a slow, constant rate for at least 90 min. The rate of leucine incorporation was reduced to 0.5%, but methionine was only reduced to 2%, suggesting that chains are normally initiated with methionine but are prematurely released at a short chain length. Consistent with this possibility was the distribution of the products on Sephadex columns: a range of peptides longer than 4 and shorter than 60 to 70 residues was seen. Less than 10% of the peptides broke down during a chase with cold amino acids, and during continuous labeling they accumulated progressively. On the average, one peptide was formed per ribosome every 5 min. Peptide synthesis in the presence of chloramphenicol was still dependent on ribosome translocation; it stopped in a mutant with an inactivated temperature-sensitive elongation factor G. But even in the absence of translocation, new messenger ribonucleic acid (mRNA) chains were found joined to one or a few ribosomes. The chains had a size distribution comparable to that of mRNA from polyribosomes of growing cells. They were stabilized for an average time of about 5 min, but were more rapidly degraded after puromycin was added to the cells. This suggests that stabilization may be related to the average time spent by a ribosome on an mRNA chain, with or without polypeptide formation. 582 on August 1, 2020 by guest

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Section: Discussionmentioning

confidence: 57%

Polypeptide Formation and Polyribosomes in Escherichia coli Treated with Chloramphenicol

1974

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“…The peptide chain elongation rates calculated from these lag times are 14.1 amino acids s-1 in exponentially growing cells, about 9.4 amino acids s-1 in cells starved for 15 rain and 1 h, and 7.3 amino acids s-1 in cells starved for 2.5 h. Thus, during the starvation period studied, the bulk mRNA half-life increased 2.2-fold while the rate of peptide chain elongation decreased 1.9fold. This can be compared to the results of Pato et al [9] demonstrating that a 1.6-fold decrease in the rate of peptide chain elongation using fusidic acid (0.25/zg m1-1) resulted in a 1.7-fold increase in bulk mRNA stability. It is possible that the reduced rate of peptide chain elongation during the initial phase of glucose starvation is a direct or indirect effect of the accumulation of ppGpp [211.…”

Section: The Peptide Chain Elongation Rate Decreases Rapidly As a Conmentioning

confidence: 72%

“…Since the rate of ribosome elongation has been implicated in affecting the stability of mRNA [7][8][9][10], we determined the peptide chain elongation rate in exponentially growing and glucosestarved cells by measuring the lag time before synthesis of the first /3-galactosidase molecule after addition of IPTG ( Fig. 3) Fig.…”

Section: The Peptide Chain Elongation Rate Decreases Rapidly As a Conmentioning

confidence: 99%

“…Furthermore, several investigators have demonstrated that reducing the rate of peptide chain elongation by treatment of cells with specific drugs lead to a reduced rate of mRNA decay (e.g. [7][8][9][10]). Based on such observations, it has been proposed that targets for nucleolytic attack may be protected by the proximity of ribosomes and that the probability of exposing such targets decrease when the ribosomes are slowed down or stalled [7,9].…”

Section: Introductionmentioning

confidence: 99%

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Effects of starvation for exogenous carbon on functional mRNA stability and rate of peptide chain elongation in Escherichia coli

Albertson

1994

FEMS Microbiology Letters

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The decay rate of the potential to synthesize proteins after complete inhibition of transcription by rifampicin was analyzed to determine the functional mRNA stability of exponentially growing and glucose-starved Escherichia coli B and K12 cells. We found the following: (i) The half-life of the mRNA pool increased 2.2-fold during a period of 2 h of starvation (from 1.8 min in exponentially growing cells to 4.0 min for cells starved for 2 h); (ii) the effect on transcript stability appeared to be global since transcripts of genes that were induced, repressed or unaltered in their expression during starvation exhibited more or less the same increased stability; (iii) the rate of peptide chain elongation, as measured by the synthesis time for beta-galactosidase, decreased 1.9-fold during the starvation period studied and may, at least in part, account for the global stabilization of transcripts in starved cells.

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“…1). The en-hancement of bulk mRNA stability is apparently characteristic of inhibited translation and is not a peculiarity of arginine starvation (25,31). We then studied the effect of both leucine and arginine deprivation on the rate of degradation of argECBH mRNA in an arg-leuauxotroph ofE.…”

Section: Resultsmentioning

confidence: 99%

Effect of arginine on the stability and size of argECBH messenger ribonucleic acid in Escherichia coli

Krzyzek¹,

Rogers²

1976

J Bacteriol

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The chemical stability of argECBH messenger ribonucleic acid (mRNA) produced by Escherichia coli was found to be unaltered during steady-state repression by arginine. During extreme arginine deprivation, the increase in arg-ECBH mRNA stability was related to general effects of amino acid starvation on mRNA stability. Thus a mechanism whereby argECBH gene expression is regulated by altering the decay rate of this mRNA is not consistent with our data. Sucrose gradient analysis followed by hybridization revealed that both heavy (14S) and light (8S) components of argECBH mRNA were produced by cells of E. coli K-12 grown without arginine, whereas predominantly light (8S) mRNA was produced by cells grown with arginine. A functional argR gene and the EC portion of the argECBH cluster were found essential for the arginine restriction of heavy-mRNA production. Experiments suggest that light arg-ECBH mRNA did not arise from heavy message, and 80% of both light and heavy mRNA was found bound to ribosomes. The data appear most consistent with the notion that a second site of control by arginine regulates the amounts of light and heavy arginine mRNA in the cell either by early termination of transcription or by endonucleolytic processing. Consideration of these data in conjunction with those of the accompanying report (Krzyzek and Rogers, 1976) permits the tentative conclusion that light argECBH mRNA is not translated into active enzymes and is thus responsible for the discrepancy between the high content of hybridizable mRNA and low rates of enzyme synthesis found during arginine repression.In the accompanying report (17) we presented evidence that physiological repression of the argECBH operon of Escherichia coli by arginine could not be explained solely by transcriptional control due to arginine repressor-operator interactions. The discrepancy between levels of argECBH messenger ribonucleic acid (mRNA) and rates of enzyme synthesis coded for by this operon during arginine repression led us to propose a second site of control that somehow effects the eventual translation ofthis message.Both genetic data (8, 12) and mRNA determinations (24, 26) have shown that the arg-ECBH cluster is transcribed bidirectionally from an internal control region located between the argE and argC loci that contains at least one arginine repressor binding site. We observed physiological repression of argECBH mRNA by arginine (29), and further experiments indicated that arginine together with the argR protein signals transcriptional control by reducing the initiation of synthesis of this mRNA (16), presumably at the promoter-operator sites within the cluster.The proposed second-site regulatory devices that follow first-site regulation of initiation of specific mRNA synthesis and result in lowered translational efficiency of mRNA are usually termed "translational control" or "post-transcriptional control." However, this gray zone between initiation of mRNA production and final appearance of enzyme activity actually includes at least four distinct p...

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Messenger Ribonucleic Acid Synthesis and Degradation in Escherichia coli During Inhibition of Translation

Cited by 66 publications

References 28 publications

Polypeptide Formation and Polyribosomes in Escherichia coli Treated with Chloramphenicol

Polypeptide Formation and Polyribosomes in Escherichia coli Treated with Chloramphenicol

Effects of starvation for exogenous carbon on functional mRNA stability and rate of peptide chain elongation in Escherichia coli

Effect of arginine on the stability and size of argECBH messenger ribonucleic acid in Escherichia coli

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