Regulation of lysyl-tRNA synthetase expression by histone-like protein H-NS of Escherichia coli

Ito, Koichi; Oshima, Taku; Mizuno, Takeshi; Nakamura, Yoshikazu

doi:10.1128/jb.176.23.7383-7386.1994

Cited by 14 publications

(7 citation statements)

References 34 publications

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“…The rationale for undertaking such an inter-kingdom protein substitution was based on the following considerations: (i) H-NS regulates the expression of several genes in Escherichia and Salmonella (Higgins et al, 1990;Dorman, 1991); (ii) many H-NS-regulated genes have curved promoter regions Dersch et al, 1993;Ito et al, 1994) note that we have shown here that the bgl regulatory region contains curved DNA; (iii) H-NS acts as a transcriptional regulator by binding to curved DNA (Owen-Hughes et al, 1992;; (iv) Btcd binds tightly to curved DNA (Mazin et al, 1994a,b), as does H-NS (Yamada et al, 1990;Mizuno, 1992); and (v) mammalian proteins involved in DNA and RNA transactions have been found to substitute for their E.coli prototypes (Kodama et al, 1991;O'Connor and Laval, 1991;Sweasy and Loeb, 1992;Sakumi etal., 1993;Kim and Loeb, 1995). Not all of H-NS functions can be replaced by Btcd functions Btcd does not fully substitute for H-NS.…”

Section: Discussionmentioning

confidence: 99%

Btcd, a mouse protein that binds to curved DNA, can substitute in Escherichia coli for H-NS, a bacterial nucleoid protein.

1996

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In an Escherichia coli mutant devoid of H‐NS, a bacterial nucleoid protein, mouse protein Btcd was able to substitute for H‐NS in two tested functions. It restored cell motility and repression of the expression of the bgl operon. Btcd1, a mutant Btcd protein deleted of its zinc finger and thus having reduced DNA binding, failed to substitute for H‐NS. Mouse protein Btcd was shown to repress the bgl operon at the level of transcription initiation and to bind preferentially to a curved DNA fragment encompassing the bgl promoter. These effects of Btcd on bacterial gene transcription can be accounted for by the binding of Btcd or H‐NS to a curved DNA sequence near a promoter. A few mammalian proteins have been shown to substitute for their Escherichia prototypes involved in DNA and RNA transactions. The efficiency of Btcd protein in substituting for H‐NS in Escherichia suggests its possible involvement in regulating gene expression in mouse cells.

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Section: Discussionmentioning

confidence: 99%

Btcd, a mouse protein that binds to curved DNA, can substitute in Escherichia coli for H-NS, a bacterial nucleoid protein.

1996

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“…H-NS prevents the transcription of rRNA by binding to the rrn promoter (47). It also regulates negatively lysU, which codes for lysyl-tRNA synthetase (14). The growth temperature is an important environmental determinant regulating the expression of hns.…”

Section: Discussionmentioning

confidence: 99%

The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

Michel¹,

Lehoux²,

Depret³

et al. 1997

J Bacteriol

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The psychrotrophic bacterium Pseudomonas fragi was subjected to cold shocks from 30 or 20 to 5°C. The downshifts were followed by a lag phase before growth resumed at a characteristic 5°C growth rate. The analysis of protein patterns by two-dimentional gel electrophoresis revealed overexpression of 25 or 17 proteins and underexpression of 12 proteins following the 30-or 20-to-5°C shift, respectively. The two downshifts shared similar variations of synthesis of 20 proteins. The kinetic analysis distinguished the induced proteins into cold shock proteins (Csps), which were rapidly but transiently overexpressed, and cold acclimation proteins (Caps), which were more or less rapidly induced but still overexpressed several hours after the downshifts. Among the cold-induced proteins, four low-molecular-mass proteins, two of them previously characterized as Caps (CapA and CapB), and heat acclimation proteins (Haps) as well as heat shock proteins (Hsps) for the two others (TapA and TapB) displayed higher levels of induction. Partial amino acid sequences, obtained by microsequencing, were used to design primers to amplify by PCR the four genes and then determine their nucleotide sequences. A BamHI-EcoRI restriction fragment of 1.9 kb, containing the complete coding sequence for capB, was cloned and sequenced. The four peptides belong to the family of small nucleic acid-binding proteins as CspA, the major Escherichia coli Csp. They are likely to play a major role in the adaptative response of P. fragi to environmental temperature changes.

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“…Chromosomal replacements of ApaH (open reading frame only) with yeast Apa2, a stabilized ApaH variant (ApaH_D7), and ApaH mutants with impaired enzymatic activity. LysU's expression is thought to be triggered by heat stress, and it has thus been suggested to act primarily as an Ap4A synthetase [38,39]. significantly reduced -≤ 0.02 lM compared to 0.2 lM in the wild-type (Table 1), yet within the perturbation range expected for a signaling molecule.…”

Section: Regulation Of Apahmentioning

confidence: 99%

Diadenosine tetraphosphate (Ap4A) – an E. coli alarmone or a damage metabolite?

et al. 2017

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Under stress, metabolism is changing: specific up- or down-regulation of proteins and metabolites occurs as well as side effects. Distinguishing specific stress-signaling metabolites (alarmones) from side products (damage metabolites) is not trivial. One example is diadenosine tetraphosphate (Ap4A) - a side product of aminoacyl-tRNA synthetases found in all domains of life. The earliest observations suggested that Ap4A serves as an alarmone for heat stress in Escherichia coli. However, despite 50 years of research, the signaling mechanisms associated with Ap4A remain unknown. We defined a set of criteria for distinguishing alarmones from damage metabolites to systematically classify Ap4A. In a nutshell, no indications for a signaling cascade that is triggered by Ap4A were found; rather, we found that Ap4A is efficiently removed in a constitutive, nonregulated manner. Several fold perturbations in Ap4A concentrations have no effect, yet accumulation at very high levels is toxic due to disturbance of zinc homeostasis, and also because Ap4A's structural overlap with ATP can result in spurious binding and inactivation of ATP-binding proteins. Overall, Ap4A met all criteria for a damage metabolite. While we do not exclude any role in signaling, our results indicate that the damage metabolite option should be considered as the null hypothesis when examining Ap4A and other metabolites whose levels change upon stress.

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Regulation of lysyl-tRNA synthetase expression by histone-like protein H-NS of Escherichia coli

Cited by 14 publications

References 34 publications

Btcd, a mouse protein that binds to curved DNA, can substitute in Escherichia coli for H-NS, a bacterial nucleoid protein.

Btcd, a mouse protein that binds to curved DNA, can substitute in Escherichia coli for H-NS, a bacterial nucleoid protein.

The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

Diadenosine tetraphosphate (Ap4A) – an E. coli alarmone or a damage metabolite?

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