Using NMR metabolomics to investigate tricarboxylic acid cycle-dependent signal transduction in Staphylococcus epidermidis.
J Biol Chem. 2010 Nov 19;285(47):36616-24
Authors: Sadykov MR, Zhang B, Halouska S, Nelson JL, Kreimer LW, Zhu Y, Powers R, Somerville GA
Staphylococcus epidermidis is a skin-resident bacterium and a major cause of biomaterial-associated infections. The transition from residing on the skin to residing on an implanted biomaterial is accompanied by regulatory changes that facilitate bacterial survival in the new environment. These regulatory changes are dependent upon the ability of bacteria to "sense" environmental changes. In S. epidermidis, disparate environmental signals can affect synthesis of the biofilm matrix polysaccharide intercellular adhesin (PIA). Previously, we demonstrated that PIA biosynthesis is regulated by tricarboxylic acid (TCA) cycle activity. The observations that very different environmental signals result in a common phenotype (i.e. increased PIA synthesis) and that TCA cycle activity regulates PIA biosynthesis led us to hypothesize that S. epidermidis is "sensing" disparate environmental signals through the modulation of TCA cycle activity. In this study, we used NMR metabolomics to demonstrate that divergent environmental signals are transduced into common metabolomic changes that are "sensed" by metabolite-responsive regulators, such as CcpA, to affect PIA biosynthesis. These data clarify one mechanism by which very different environmental signals cause common phenotypic changes. In addition, due to the frequency of the TCA cycle in diverse genera of bacteria and the intrinsic properties of TCA cycle enzymes, it is likely the TCA cycle acts as a signal transduction pathway in many bacteria.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Biochim Biophys Acta. 2011 Aug 8;
Authors: Mertz B, Struts AV, Feller SE, Brown MF
Abstract
Rhodopsin has served as the primary model for studying G protein-coupled receptors (GPCRs)-the largest group in the human genome, and consequently a primary target for pharmaceutical development. Understanding the functions and activation mechanisms of...
A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.
A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.
Related Articles A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.
Structure. 2010 Dec 8;18(12):1559-1569
Authors: Call ME, Chou JJ
One of the most fundamental problems in cell biology concerns how cells communicate with their surroundings through surface receptors. The last few decades have seen major advances in understanding the mechanisms of receptor-ligand...
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Structure of key protein for cellular signal transduction elucidated - News-Medical.n
Structure of key protein for cellular signal transduction elucidated - News-Medical.net
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Structure of key protein for cellular signal transduction elucidated
News-Medical.net
Using NMR spectroscopy, Professor Michael Sattler and his team elucidated the spatial structure of the Qua1 region of Sam68, which is responsible for the ...
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09-10-2010 12:58 PM
[NMR paper] 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conf
1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
Eur J Biochem. 1993 Feb 1;211(3):555-62
Authors: Turner DL, Williams RJ
The redox-state dependent changes in chemical shift, which have...
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08-21-2010 11:53 PM
[NMR paper] 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Es
1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Related Articles 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Biochemistry. 1991 Oct 15;30(41):10043-57
Authors: Pelton JG, Torchia DA, Meadow ND, Wong CY, Roseman S
IIIGlc is an 18.1-kDa signal-transducing phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase...
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Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR/x-ray crystallography
Spincore.com are advertising a postdoc NMR position. It sounds pretty interesting.
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Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR /x-ray crystallography
Case Medical School, Cleveland, Ohio, USA
How are signaling events transmitted from one protein to another? To answer this question we are looking to add a postdoctoral co-workers to our interdisciplinary team. Our interest is to understand protein-protein interactions, protein structure and dynamics in the context of cell signaling...
Using NMR metabolomics to investigate tricarboxylic acid cycle-dependent signal transduction in Staphylococcus epidermidis.
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