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  • 1
    Language: English
    In: Cell, 1981, Vol.25(3), pp.585-586
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
    Source: ScienceDirect Journals (Elsevier)
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  • 2
    Language: English
    In: Cell, 22 September 2016, Vol.167(1), pp.111-121.e13
    Description: Bacterial small RNAs (sRNAs) have been implicated in various aspects of post-transcriptional gene regulation. Here, we demonstrate that sRNAs also act at the level of transcription termination. We use the gene, which encodes a general stress sigma factor σ , as a model system, and show that sRNAs DsrA, ArcZ, and RprA bind the 5′UTR to suppress premature Rho-dependent transcription termination, both in vitro and in vivo. sRNA-mediated antitermination markedly stimulates transcription of  during the transition to the stationary phase of growth, thereby facilitating a rapid adjustment of bacteria to global metabolic changes. Next generation RNA sequencing and bioinformatic analysis indicate that Rho functions as a global “attenuator” of transcription, acting at the 5′UTR of hundreds of bacterial genes, and that its suppression by sRNAs is a widespread mode of bacterial gene regulation. Bacterial small RNAs balance the Rho-dependent termination pathway to prevent premature transcription termination, extending the role of these RNA regulators beyond post-transcriptional control.
    Keywords: Transcription Termination ; Antitermination ; Rho ; Srna ; Sigma Factor ; Stress Response ; Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 3
    Article
    Article
    Language: English
    In: Cell, 2004, Vol.118(1), pp.1-2
    Description: Small regulatory RNAs can act by pairing with their target messages, targeting themselves and the mRNA for degradation; Lenz et al. (this issue of Cell) now report that multiple small RNAs are essential regulators of the quorum-sensing systems of Vibrio species, including the regulation of virulence in V. cholerae.
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 4
    Language: English
    In: Cell, 1981, Vol.23(1), pp.1-2
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 5
    Language: English
    In: Cell, 1981, Vol.24(1), pp.225-233
    Description: The Ion gene of E. coli controls the stability of two bacteriophage lambda proteins. The functional half-life of the phage N gene product, measured by complementation, is increased about 5-fold in Ion mutant strains, from 2 min to 10 min. The chemical half-life of N protein, determined by its disappearance on polyacrylamide gels following pulse-chase labeling, increases about three-fold in Ion cells. In contrast to its effect on the N protein, the Ion mutation produces a 50% decrease in the chemical half-life of cII protein. The decay rate of many other phage proteins, including the unstable gene O product, remains unaffected by a host Ion defect. A Ion mutation alters lambda physiology in two ways. First, upon infection, the phage enters the lytic pathway predominantly. This may result from the deficiency of cII protein caused by its decreased stability, since cII product is required for establishment of lysogeny. Second, brief thermal induction of a Ion (lambda c1857) lysogen leads irreversibly to lysis; repression cannot be restablished and the treated cells are committed to forming infective centers. Although N product is normally required for rapid commitment, Ion lysogens become committed more rapidly than Ion+ lysogens, even in the absence of N function. These results identify for the first time native proteins whose stability is affected by the Lon proteolytic pathway. They also indicate that the Lon system may be important in regulating gene expression in E. coli.
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 6
    Language: English
    In: Cell, 1997, Vol.91(4), pp.435-438
    Description: Much of our current knowledge about specific steps in energy-dependent degradation and the role of accessory factors comes from studies of the prokaryotic ATP-dependent proteases, ClpAP and ClpXP, which are complexes of separately encoded ATPase and peptidase subunits, and the homomeric Lon and FtsH proteases, in which both functions are encoded within single polypeptide chains. We would like to propose that the similarity in structure between the ClpAP or ClpXP proteases and the 26S proteasome, despite their apparent evolutionary unrelatedness, reflects underlying similarities in the biochemical mechanism of protein degradation. The existence of ClpYQ (HslUV), a hybrid between a protease homologous to the proteasome and a Clp ATPase, reinforces this suggestion.
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 7
    Language: English
    In: Cell, 1992, Vol.68(5), pp.989-994
    Description: The 21 kd NusG protein is essential for E. coli viability. Cells depleted for NusG were defective for factor-dependent transcription termination. Rho-induced polarity in the gal operon and the Rho-dependent lambda tR1 and lambda tL1 terminators were suppressed in NusG-deficient cells. NusG depletion inactivated the phage HK022 Nun termination factor. In contrast, the factor-independent lambda tl terminator was fully active in NusG-depleted cells and could be suppressed by phage lambda N function.
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 8
    In: Cell, Nov 10, 2000, Vol.103(4), p.552(2)
    Keywords: Book Reviews ; Storz, Gisela ; Hengge-aronis, Regine
    ISSN: 0092-8674
    Source: Cengage Learning, Inc.
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  • 9
    Review
    Review
    Language: English
    In: Cell, 2000, Vol.103(4), pp.552-553
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
    Source: ScienceDirect Journals (Elsevier)
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