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  • 1
    Article
    Article
    Language: English
    In: Annual Review of Microbiology, Vol.681(1)
    ISSN: 0066-4227
    E-ISSN: 1545-3251
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  • 2
    Article
    Article
    Language: English
    In: Annual Review of Microbiology, Vol.691(1)
    ISSN: 0066-4227
    E-ISSN: 1545-3251
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  • 3
    Article
    Article
    Language: English
    In: Annual Review of Microbiology, 2017, Vol.71, p.i-ii
    ISSN: 0066-4227
    E-ISSN: 1545-3251
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  • 4
    Article
    Article
    Language: English
    In: Annual Review of Microbiology, Vol.671(1)
    ISSN: 0066-4227
    E-ISSN: 1545-3251
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  • 5
    Article
    Article
    Language: English
    In: Annual Review of Microbiology, Vol.701(1)
    ISSN: 0066-4227
    E-ISSN: 1545-3251
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  • 6
    Article
    Article
    Language: English
    In: Annual review of microbiology, 08 September 2018, Vol.72, pp.i-ii
    Keywords: Editorial Policies–History ; History, 20th Century–History ; History, 21st Century–History ; Microbiology–History ; Molecular Biology–History ; Periodicals As Topic–History;
    ISSN: 00664227
    E-ISSN: 1545-3251
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  • 7
    Language: English
    In: Annual Review of Microbiology, 2011, Vol.65, p.189-213
    Description: Under conditions of nutrient deprivation or stress, or as cells enter stationary phase, Escherichia coli and related bacteria increase the accumulation of RpoS, a specialized sigma factor. RpoS-dependent gene expression leads to general stress resistance of cells. During rapid growth, RpoS translation is inhibited and any RpoS protein that is synthesized is rapidly degraded. The complex transition from exponential growth to stationary phase has been partially dissected by analyzing the induction of RpoS after specific stress treatments. Different stress conditions lead to induction of specific sRNAs that stimulate RpoS translation or to induction of small-protein antiadaptors that stabilize the protein. Recent progress has led to a better, but still far from complete, understanding of how stresses lead to RpoS induction and what RpoS-dependent genes help the cell deal with the stress.
    Keywords: Hfq ; (p)ppGpp ; RssB ; sRNA ; ClpXP
    ISSN: 0066-4227
    E-ISSN: 1545-3251
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  • 8
    Language: English
    In: Annual review of microbiology, 08 September 2018, Vol.72, pp.111-139
    Description: RcsB, a response regulator of the FixJ/NarL family, is at the center of a complex network of regulatory inputs and outputs. Cell surface stress is sensed by an outer membrane lipoprotein, RcsF, which regulates interactions of the inner membrane protein IgaA, lifting negative regulation of a phosphorelay. In vivo evidence supports a pathway in which histidine kinase RcsC transfers phosphate to phosphotransfer protein RcsD, resulting in phosphorylation of RcsB. RcsB acts either alone or in combination with RcsA to positively regulate capsule synthesis and synthesis of small RNA (sRNA) RprA as well as other genes, and to negatively regulate motility. RcsB in combination with other FixJ/NarL auxiliary proteins regulates yet other functions, independent of RcsB phosphorylation. Proper expression of Rcs and its targets is critical for success of Escherichia coli commensal strains, for proper development of biofilm, and for virulence in some pathogens. New understanding of how the Rcs phosphorelay works provides insight into the flexibility of the two-component system paradigm.
    Keywords: Bglj ; Gade ; Colanic Acid ; Motility ; Two-Component System
    ISSN: 00664227
    E-ISSN: 1545-3251
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  • 9
    Language: English
    In: 2004, Vol.58, p.303-328
    Description: ▪ Abstract  Small noncoding RNAs have been found in all organisms, primarily as regulators of translation and message stability. The most exhaustive searches have taken place in E. coli , resulting in identification of more than 50 small RNAs, or 1%–2% of the number of protein-coding genes. One large class of these small RNAs uses the RNA chaperone Hfq; members of this class act by pairing to target messenger RNAs. Among the members of this class are DsrA and RprA, which positively regulate rpoS translation, OxyS, which negatively regulates rpoS translation and fhlA translation, RyhB, which reapportions iron use in the cell by downregulating translation of many genes that encode Fe-containing proteins, and Spot 42, which changes the polarity of translation in the gal operon. The promoters of these small RNAs are tightly regulated, frequently as part of well-understood regulons. Lessons learned from the study of small RNAs in E. coli can be applied to finding these important regulators in other organisms.
    Keywords: Hfq ; DsrA ; OxyS ; RyhB ; Spot 42
    ISSN: 0066-4227
    E-ISSN: 15453251
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  • 10
    Language: English
    In: Annual Review of Cell and Developmental Biology, 2003, Vol.191(1), p.565-587
    Description: ▪ Abstract   Proteolysis by cytoplasmic, energy-dependent proteases plays a critical role in many regulatory circuits, keeping basal levels of regulatory proteins low and rapidly removing proteins when they are no longer needed. In bacteria, four families of energy-dependent proteases carry out degradation. In all of them, substrates are first recognized and bound by ATPase domains and then unfolded and translocated to a sequestered proteolytic chamber. Substrate selection depends not on ubiquitin but on intrinsic recognition signals within the proteins and, in some cases, on adaptor or effector proteins that participate in delivering the substrate to the protease. For some, the activity of these adaptors can be regulated, which results in regulated proteolysis. Recognition motifs for proteolysis are frequently found at the N and C termini of substrates. Proteolytic switches appear to be critical for cell cycle development in Caulobacter crescentus , for proper sporulation in Bacillus subtilis , and for the transition in and out of stationary phase in Escherichia coli . In eukaryotes, the same proteases are found in organelles, where they also play important roles.
    Keywords: Clp ; Lon ; FtsH ; Hsl ; chaperone
    ISSN: 1081-0706
    E-ISSN: 1530-8995
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