Temperature-Induced Derepression of Tryptophan Biosynthesis in a Tryptophanyl-Transfer Ribonucleic Acid Synthetase Mutant of
            <i>Bacillus subtilis</i>

Steinberg, William M.

doi:10.1128/jb.117.3.1023-1034.1974

Cited by 31 publications

(5 citation statements)

References 39 publications

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“…In tryptophan-dependent growth. The latter strain is deficient in tRNA Trp charging when grown at elevated tem-the comparable trpS1 temperature-sensitive strain the AT level with the wild-type rtpLP construct was elevated peratures (Steinberg, 1974;Sarsero et al, 2000b). The chromosomal at operon was deleted from both of these appreciably (Figure 3, compare lane 3 with lane 1).…”

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confidence: 93%

Features of a Leader Peptide Coding Region that Regulate Translation Initiation for the Anti-TRAP Protein of B. subtilis

Chen¹,

Yanofsky

2004

Molecular Cell

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The rtpA gene of Bacillus subtilis encodes the Anti-TRAP protein, AT. AT can bind and inhibit the TRAP regulatory protein, preventing TRAP from promoting transcription termination in the trpEDCFBA operon leader region. AT synthesis is upregulated transcriptionally and translationally in response to the accumulation of uncharged tRNA(Trp). Here we analyze AT's translational regulation by rtpLP, a 10 residue leader peptide coding region located immediately preceding the rtpA Shine-Dalgarno sequence. Our findings suggest that, whenever the charged tRNA(Trp) level is sufficient to allow the ribosome translating rtpLP to reach its stop codon, it blocks the adjacent rtpA Shine-Dalgarno sequence, inhibiting AT synthesis. However, when there is a charged tRNA(Trp) deficiency, the translating ribosome presumably stalls at one of three adjacent rtpLP Trp codons. This stalling exposes the rtpA Shine-Dalgarno sequence, permitting AT synthesis. RNA-RNA pairing may also influence AT synthesis. Production of AT would inactivate TRAP, thereby increasing trp operon expression.

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confidence: 93%

Features of a Leader Peptide Coding Region that Regulate Translation Initiation for the Anti-TRAP Protein of B. subtilis

Chen¹,

Yanofsky

2004

Molecular Cell

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“…The regulation of the tryptophan operon ( trp ), mediated by the Trp repressor and transcriptional attenuation, has been widely studied in bacteria [ 35 ]. Bacillus subtilis harbors a temperature-sensitive tryptophanyl-tRNA synthetase where it was observed that at high temperatures, when the bacterium growth is reduced but not suppressed, the trp operon was induced [ 36 ]. This process is likely mediated by the reduced availability of the trp attenuator protein TRAP [ 37 , 38 ].…”

Section: Resultsmentioning

confidence: 99%

Osmotic stress induces long-term biofilm survival in Liberibacter crescens

et al. 2022

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Citrus greening, also known as Huanglongbing (HLB), is a devastating citrus plant disease caused predominantly by Liberibacter asiaticus. While nearly all Liberibacter species remain uncultured, here we used the culturable L. crescens BT-1 as a model to examine physiological changes in response to the variable osmotic conditions and nutrient availability encountered within the citrus host. Similarly, physiological responses to changes in growth temperature and dimethyl sulfoxide concentrations were also examined, due to their use in many of the currently employed therapies to control the spread of HLB. Sublethal heat stress was found to induce the expression of genes related to tryptophan biosynthesis, while repressing the expression of ribosomal proteins. Osmotic stress induces expression of transcriptional regulators involved in expression of extracellular structures, while repressing the biosynthesis of fatty acids and aromatic amino acids. The effects of osmotic stress were further evaluated by quantifying biofilm formation of L. crescens in presence of increasing sucrose concentrations at different stages of biofilm formation, where sucrose-induced osmotic stress delayed initial cell attachment while enhancing long-term biofilm viability. Our findings revealed that exposure to osmotic stress is a significant contributing factor to the long term survival of L. crescens and, possibly, to the pathogenicity of other Liberibacter species.

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“…A temperature-sensitive tryptophanyl-tRNA synthetase mutant of B. subtilis was recently isolated by Steinberg and Anagnostopoulos (25). They reported that at elevated temperatures both anthranilate synthase and tryptophan synthase-B were coordinately derepressed (24). The possibility that tryptophanmediated control ofhistidinol phosphate aminotransferase in these mutants was in some way altered from that resulting from tryptophan limitation was investigated.…”

Section: Resultsmentioning

confidence: 99%

“…At least two regulatory loci have been implicated in the control of tryptophan biosynthesis in B. subtilis (19,24). Steinberg (24) isolated a strain that had a temperature-sensitive tryptophanyl-tRNA synthetase.…”

Section: Resultsmentioning

confidence: 99%

Regulation of histidinol phosphate aminotransferase synthesis by tryptophan in Bacillus subtilis

Weigent¹,

Nester²

1976

J Bacteriol

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The effect of tryptophan on the synthesis of histidinol phosphate aminotransferase and prephenate dehydrogenase has been examined. The genes specifying two enzymes for tryptophan biosynthesis (anthranilate synthase and tryptophan synthase-B) were found to be derepressed in a temporal sequence according to their chromosomal location. The genes for histidinol phosphate aminotransferase and prephenate dehydrogenase were derepressed simultaneously approximately 8 min after tryptophan synthase-B. When excess tryptophan was added to a derepressed culture, the pattern of repression of trpE (anthranilate synthase), trpB (tryptophan synthase-B), hisH (histidinol phosphate aminotransferase), and tyrA (prephenate dehydrogenase) was found to be simultaneous. Methyl tryptophan-resistant mutants, which synthesize elevated levels of the tryptophan enzymes, also synthesized elevated levels of histidinol phosphate aminotransferase. Qualitatively similar data were obtained in a temperaturesensitive tryptophanyl-transfer ribonucleic acid synthetase mutant grown at elevated temperatures. The time at which messenger ribonucleic acid was synthesized for anthranilate synthase, tryptophan synthase-B, histidinol phosphate aminotransferase, and prephenate dehydrogenase in the presence of actinomycin D indicated that ordered enzyme synthesis was a result of ordered transcription of the corresponding portion of the genome. The effect of the drug rifampin on enzyme synthesis was also examined. The addition of this drug halted the transcription of anthranilate synthase very rapidly, but later regions of the tryptophan region continued to be transcribed. The transcription of the hisH and tyrA genes was also shut off rapidly after rifampin was added. The significance of these observations to the control of transcription of the hisH gene by tryptophan is discussed.

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Temperature-Induced Derepression of Tryptophan Biosynthesis in a Tryptophanyl-Transfer Ribonucleic Acid Synthetase Mutant of Bacillus subtilis

Cited by 31 publications

References 39 publications

Features of a Leader Peptide Coding Region that Regulate Translation Initiation for the Anti-TRAP Protein of B. subtilis

Features of a Leader Peptide Coding Region that Regulate Translation Initiation for the Anti-TRAP Protein of B. subtilis

Osmotic stress induces long-term biofilm survival in Liberibacter crescens

Regulation of histidinol phosphate aminotransferase synthesis by tryptophan in Bacillus subtilis

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