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Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
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Investigating ROS, RNS, and H2S-Sensitive Signaling Proteins.

Eleanor Williams1,2, Matthew Whiteman3, Mark E Wood4

  • 1Faculty of Health and Applied Sciences, University of the West of England, Bristol, UK.

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|June 1, 2019
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Summary
This summary is machine-generated.

Identifying protein thiol modifications is crucial for understanding cellular signaling. This study details methods using fluorescent probes and mass spectrometry in model organisms like Arabidopsis thaliana and Caenorhabditis elegans.

Keywords:
5′-Iodoacetamide fluoresceinGlutathioneGlyceraldehyde 3-phosphate dehydrogenaseHistidine kinaseHydrogen peroxideHydrogen sulfideNitric oxideReactive nitrogen speciesReactive oxygen speciesStomatal guard cellsThiol labeling

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Protein modification, particularly of cysteine thiols, regulates protein function and cellular processes.
  • Reactive species like ROS, RNS, H2S, and glutathione can modify protein thiols.
  • Identifying these modifications is essential for understanding physiological changes.

Purpose of the Study:

  • To present and discuss methods for identifying protein thiol modifications.
  • To highlight the utility of fluorescent thiol derivatives coupled with mass spectrometry.
  • To demonstrate the confirmation of these modifications using biochemical assays and genetic mutants.

Main Methods:

  • Utilizing fluorescent thiol derivatives for labeling modified thiols.
  • Employing mass spectrometry to identify specific thiol sites on proteins.
  • Confirming modifications through biochemical assays and genetic analysis in model organisms.

Main Results:

  • Successful identification of protein thiol modifications in Arabidopsis thaliana and Caenorhabditis elegans.
  • Demonstration of the combined power of fluorescent labeling, mass spectrometry, and biochemical validation.
  • Establishment of robust methodologies applicable across diverse biological systems.

Conclusions:

  • The described techniques provide powerful tools for studying protein thiol modifications.
  • These methods are valuable for investigating cellular signaling pathways in various organisms, including humans.
  • Further application of these methods will advance our understanding of protein function and organismal physiology.