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  • Gottesman, Susan  (227)
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  • 1
    Language: English
    In: Nature, 03 November 2016, Vol.539(7627), pp.38-39
    Description: Bacteria are expert at adapting to changing lifestyles. Dealing with damaged or misfolded proteins is a key challenge during adaptation to stressful conditions such as high temperature. In such situations, chaperone proteins restore unfolded proteins...
    Keywords: Garbage ; Phosphates
    ISSN: 00280836
    E-ISSN: 1476-4687
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  • 2
    Language: English
    In: Nature, March 31, 2011, Vol.471(7340), p.588(2)
    Keywords: Nucleases -- Physiological Aspects ; Nucleases -- Research ; Rna Interference -- Physiological Aspects ; Rna Interference -- Research ; Restriction-modification System -- Physiological Aspects ; Restriction-modification System -- Research
    ISSN: 0028-0836
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  • 3
    In: Nature, 2011, Vol.471(7340), p.588
    Keywords: RNA, Bacterial -- Genetics ; RNA, Guide -- Genetics ; Ribonuclease III -- Metabolism ; Streptococcus Pyogenes -- Genetics;
    ISSN: 0028-0836
    E-ISSN: 14764687
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  • 4
    Article
    Article
    Language: English
    In: Nature, 3/2011, Vol.471(7340), pp.588-589
    Description: [...] the use of a core RNase rather than a Cas-specific protein provides a clear example of crosstalk between the CRISPR system and bacterial metabolism. [...] Deltcheva et al. find that all of these elements (tracrRNA, Csn1 and RNase III) are necessary for immunity - that is, for S. pyogenes to destroy...
    Keywords: Bacterial Proteins–Chemistry ; Bacterial Proteins–Genetics ; Bacterial Proteins–Immunology ; Bacterial Proteins–Metabolism ; Biological Evolution–Genetics ; DNA, Viral–Metabolism ; DNA, Viral–Genetics ; Models, Biological–Genetics ; Plasmids–Metabolism ; RNA Interference–Biosynthesis ; RNA Precursors–Genetics ; RNA Precursors–Immunology ; RNA Processing, Post-Transcriptional–Metabolism ; RNA, Bacterial–Genetics ; RNA, Bacterial–Metabolism ; RNA, Bacterial–Genetics ; RNA, Bacterial–Immunology ; RNA, Guide–Metabolism ; Ribonuclease III–Virology ; Streptococcus Pyogenes;
    ISSN: 0028-0836
    E-ISSN: 1476-4687
    Source: Nature Publishing Group (via CrossRef)
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  • 5
    Language: English
    In: Nature, Nov 3, 2016, Vol.539(7627), p.38(2)
    Keywords: Phosphates -- Health Aspects ; Microbial Colonies -- Health Aspects
    ISSN: 0028-0836
    E-ISSN: 14764687
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  • 6
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 21 April 2015, Vol.112(16), pp.5159-64
    Description: RpoS, the stationary phase/stress sigma factor of Escherichia coli, regulates a large cohort of genes important for the cell to deal with suboptimal conditions. Its level increases quickly in the cell in response to many stresses and returns to low levels when growth resumes. Increased RpoS results from increased translation and decreased RpoS degradation. Translation is positively regulated by small RNAs (sRNAs). Protein stability is positively regulated by anti-adaptors, which prevent the RssB adaptor-mediated degradation of RpoS by the ClpXP protease. Inactivation of aceE, a subunit of pyruvate dehydrogenase (PDH), was found to increase levels of RpoS by affecting both translation and protein degradation. The stabilization of RpoS in aceE mutants is dependent on increased transcription and translation of IraP and IraD, two known anti-adaptors. The aceE mutation also leads to a significant increase in rpoS translation. The sRNAs known to positively regulate RpoS are not responsible for the increased translation; sequences around the start codon are sufficient for the induction of translation. PDH synthesizes acetyl-CoA; acetate supplementation allows the cell to synthesize acetyl-CoA by an alternative, less favored pathway, in part dependent upon RpoS. Acetate addition suppressed the effects of the aceE mutant on induction of the anti-adaptors, RpoS stabilization, and rpoS translation. Thus, the bacterial cell responds to lowered levels of acetyl-CoA by inducing RpoS, allowing reprogramming of E. coli metabolism.
    Keywords: Clpxp ; Rpos ; Rssb ; Acetyl Coa ; Pyruvate Dehydrogenase ; Protein Biosynthesis ; Proteolysis ; Stress, Physiological ; Bacterial Proteins -- Metabolism ; Escherichia Coli -- Metabolism ; Sigma Factor -- Metabolism
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 7
    Language: English
    In: Science, 27 July 2001, Vol.293(5530), pp.614-615
    Description: Kuroda et al in a study describe the molecular components that enable cells to adapt to an environmental downshift, when a period of feast abruptly ends and leaner times roll around. Polyphosphate's importance in protein degradation is discussed.
    Keywords: Physical sciences -- Chemistry -- Chemical compounds -- Ribonucleoproteins ; Physical sciences -- Chemistry -- Chemical compounds -- Ribonucleoproteins ; Biological sciences -- Biology -- Cytology -- Ribonucleoproteins ; Health sciences -- Medical sciences -- Nutritional science -- Ribonucleoproteins ; Physical sciences -- Chemistry -- Chemical compounds -- Ribonucleoproteins ; Physical sciences -- Chemistry -- Chemical compounds -- Ribonucleoproteins ; Biological sciences -- Biology -- Cytology -- Ribonucleoproteins ; Biological sciences -- Biology -- Cytology -- Ribonucleoproteins ; Physical sciences -- Physics -- Microphysics -- Ribonucleoproteins ; Biological sciences -- Biochemistry -- Metabolism -- Ribonucleoproteins
    ISSN: 00368075
    E-ISSN: 10959203
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  • 8
    In: Molecular Microbiology, December 2011, Vol.82(6), pp.1545-1562
    Description: A major class of small bacterial RNAs (sRNAs) regulate translation and mRNA stability by pairing with target mRNAs, dependent upon the RNA chaperone Hfq. Hfq, related to the Lsm/Sm families of splicing proteins, binds the sRNAs and stabilizes them and stimulates pairing with mRNAs . Although Hfq is abundant, the sRNAs, when induced, are similarly abundant. Therefore, Hfq may be limiting for sRNA function. We find that, when overexpressed, a number of sRNAs competed with endogenous sRNAs for binding to Hfq. This correlated with lower accumulation of the sRNAs (presumably a reflection of the loss of Hfq binding), and lower activity of the sRNAs in regulating gene expression. Hfq was limiting for both positive and negative regulation by the sRNAs. In addition, deletion of the gene for an expressed and particularly effective competitor sRNA improved the regulation of genes by other sRNAs, suggesting that Hfq is limiting during normal growth conditions. These results support the existence of a hierarchy of sRNA competition for Hfq, modulating the function of some sRNAs.
    Keywords: Messenger Rna ; Protein Binding ; Gene Expression ; Genes ; Escherichia Coli ; Proteins;
    ISSN: 0950-382X
    E-ISSN: 1365-2958
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  • 9
    Language: English
    In: Journal of Bacteriology, Feb, 2014, Vol.196(3-4), p.754(8)
    Description: The stationary phase/general stress response sigma factor RpoS (sigma S) is necessary for adaptation and restoration of homeostasis in stationary phase. As a physiological consequence, its levels are tightly regulated at least at two levels. Multiple small regulatory RNA molecules modulate its translation, in a manner that is dependent on the RNA chaperone Hfq and the rpoS 5' untranslated region. ClpXP and the RssB adaptor protein degrade RpoS, unless it is protected by an anti-adaptor. We here find that, in addition to these posttranscriptional levels of regulation, tRNA modification also affects the steady-state levels of RpoS. We screened mutants of several RNA modification enzymes for an effect on RpoS expression and identified the miaA gene, encoding a tRNA isopentenyltransferase, as necessary for full expression of both an rpoS750-lacZ translational fusion and the RpoS protein. This effect is independent of rpoS, the regulatory RNAs, and RpoS degradation. RpoD steady-state levels were not significantly different in the absence of MiaA, suggesting that this is an RpoS-specific effect. The rpoS coding sequence is significantly enriched for leu codons that use MiaA-modified tRNAs, compared to rpoD and many other genes. Dependence on MiaA may therefore provide yet another way for RpoS levels to respond to growth conditions.
    Keywords: Escherichia Coli -- Research ; Escherichia Coli -- Physiological Aspects ; Post-translational Modifications -- Analysis ; Transfer Rna -- Research ; Translational Research
    ISSN: 0021-9193
    Source: Cengage Learning, Inc.
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  • 10
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 3 May 2011, Vol.108(18), pp.7403-7407
    Description: Eukaryotic PIN (PilT N-terminal) domain proteins are ribonucleases involved in quality control, metabolism and maturation of mRNA and rRNA. The majority of prokaryotic PIN-domain proteins are encoded by the abundant vapBC toxin—antitoxin loci and inhibit translation by an unknown mechanism. Here we show that enteric VapCs are site-specific endonucleases that cleave tRNAfMet in the anticodon stem-loop between nucleotides +38 and +39 in vivo and in vitro. Consistently, VapC inhibited translation in vivo and in vitro. Translation-reactions could be reactivated by the addition of VapB and extra charged tRNA fMet . Similarly, ectopic production of tRNAfMet counteracted VapC in vivo. Thus, tRNAfMet is the only cellular target of VapC. Depletion of tRNAfMet by vapC induction was bacteriostatic and stimulated ectopic translation initiation at elongator codons. Moreover, addition of chloramphenicol to cells carrying vapBC induced VapC activity. Thus, by cleavage of tRNAfMet , VapC simultaneously may regulate global cellular translation and reprogram translation initiation.
    Keywords: Physical sciences -- Chemistry -- Chemical compounds -- Antitoxins ; Physical sciences -- Chemistry -- Chemical compounds -- Antitoxins ; Biological sciences -- Biology -- Genetics -- Antitoxins ; Biological sciences -- Biochemistry -- Biomolecules -- Antitoxins ; Physical sciences -- Chemistry -- Chemical compounds -- Antitoxins ; Biological sciences -- Biology -- Genetics -- Antitoxins ; Biological sciences -- Biology -- Genetics -- Antitoxins ; Biological sciences -- Biology -- Cytology -- Antitoxins ; Health sciences -- Medical sciences -- Immunology -- Antitoxins ; Biological sciences -- Biology -- Genetics -- Antitoxins
    ISSN: 00278424
    E-ISSN: 10916490
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