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  • 1
    Publication Date: 2005-03-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altman, Sidney -- Bassler, Bonnie L -- Beckwith, Jon -- Belfort, Marlene -- Berg, Howard C -- Bloom, Barry -- Brenchley, Jean E -- Campbell, Allan -- Collier, R John -- Connell, Nancy -- Cozzarelli, Nicholas R -- Craig, Nancy L -- Darst, Seth -- Ebright, Richard H -- Elledge, Stephen J -- Falkow, Stanley -- Galan, Jorge E -- Gottesman, Max -- Gourse, Richard -- Grindley, Nigel D F -- Gross, Carol A -- Grossman, Alan -- Hochschild, Ann -- Howe, Martha -- Hurwitz, Jerard -- Isberg, Ralph R -- Kaplan, Samuel -- Kornberg, Arthur -- Kustu, Sydney G -- Landick, Robert C -- Landy, Arthur -- Levy, Stuart B -- Losick, Richard -- Long, Sharon R -- Maloy, Stanley R -- Mekalanos, John J -- Neidhardt, Frederick C -- Pace, Norman R -- Ptashne, Mark -- Roberts, Jeffrey W -- Roth, John R -- Rothman-Denes, Lucia B -- Salyers, Abigail -- Schaechter, Moselio -- Shapiro, Lucy -- Silhavy, Thomas J -- Simon, Melvin I -- Walker, Graham -- Yanofsky, Charles -- Zinder, Norton -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1409-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746409" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Warfare ; *Biomedical Research/economics ; *Bioterrorism ; Financing, Government ; *Microbiology ; *National Institutes of Health (U.S.) ; Peer Review, Research ; Public Health ; *Research Support as Topic ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2004-02-28
    Description: We determined the minimal portion of Escherichia coli RNA polymerase (RNAP) holoenzyme able to accomplish promoter melting, the crucial step in transcription initiation that provides RNAP access to the template strand. Upon duplex DNA binding, the N terminus of the beta' subunit (amino acids 1 to 314) and amino acids 94 to 507 of the sigma subunit, together comprising less than one-fifth of RNAP holoenzyme, were able to melt an extended -10 promoter in a reaction remarkably similar to that of authentic holoenzyme. Our results support the model that capture of nontemplate bases extruded from the DNA helix underlies the melting process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, Brian A -- Gruber, Tanja M -- Gross, Carol A -- GM 57755/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1382-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Stomatology and Microbiology and Immunology, University of California, San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14988563" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Bacterial/chemistry/genetics/*metabolism ; DNA, Superhelical/chemistry/genetics/metabolism ; DNA-Directed RNA Polymerases/chemistry/*metabolism ; Escherichia coli/*enzymology/*genetics ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Tertiary ; Sigma Factor/chemistry/*metabolism ; Templates, Genetic ; Transcription, Genetic ; Zinc Fingers
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2013-05-21
    Description: In Gram-negative bacteria, outer-membrane integrity is essential for survival and is monitored by the sigma(E) stress-response system, which initiates damage-repair pathways. One activating signal is unassembled outer-membrane proteins. Using biochemical and genetic experiments in Escherichia coli, we found that off-pathway intermediates in lipopolysaccharide transport and assembly provided an additional required signal. These distinct signals, arising from disruptions in the transport and assembly of the major outer-membrane components, jointly determined the rate of proteolytic destruction of a negative regulator of the sigma(E) transcription factor, thereby modulating the expression of stress-response genes. This dual-signal system permits a rapid response to dysfunction in outer-membrane biogenesis, while buffering responses to transient fluctuations in individual components, and may represent a broad strategy for bacteria to monitor their interface with the environment.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3928677/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3928677/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lima, Santiago -- Guo, Monica S -- Chaba, Rachna -- Gross, Carol A -- Sauer, Robert T -- AI-084442/AI/NIAID NIH HHS/ -- AI-16892/AI/NIAID NIH HHS/ -- F32 AI084442/AI/NIAID NIH HHS/ -- GM-36278/GM/NIGMS NIH HHS/ -- R01 AI016892/AI/NIAID NIH HHS/ -- R01 GM036278/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 May 17;340(6134):837-41. doi: 10.1126/science.1235358.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23687042" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*metabolism ; Biological Transport ; Carrier Proteins/metabolism ; Cell Membrane/*metabolism ; Escherichia coli/genetics/*metabolism ; Escherichia coli Proteins/metabolism ; Lipid A/metabolism ; Lipopolysaccharides/*metabolism ; Membrane Proteins/metabolism ; Proteolysis ; Sigma Factor/metabolism ; *Signal Transduction ; *Stress, Physiological ; Transcription Factors/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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