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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Protein CoAlation: a redox-linked post-translational modification.

Steven C Ley1, Luiz Pedro S de Carvalho2

  • 1The Francis Crick Institute, London, U.K.

The Biochemical Journal
|August 12, 2017
PubMed
Summary
This summary is machine-generated.

Scientists discovered a new way to identify proteins modified by Coenzyme A (CoA). This "CoAlation" modification impacts metabolic enzymes and may play a key role in how cells respond to stress.

Keywords:
coenzyme Ametabolismpost-translational modification

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Metabolism

Background:

  • Metabolic pathways are regulated by signaling and transcriptional cascades.
  • Metabolites can also directly regulate cellular processes.
  • Post-translational modifications influence protein function and cellular responses.

Purpose of the Study:

  • To develop a method for identifying proteins reversibly modified by Coenzyme A (CoA).
  • To investigate the role of CoA modification in cellular stress responses.
  • To determine if CoA modification affects protein activity.

Main Methods:

  • Development of a novel antibody and mass spectrometry-based technique.
  • Analysis of the 'CoAlated proteome' under oxidative and metabolic stress conditions.
  • Assay of protein activity for CoAlated proteins.

Main Results:

  • A new method successfully identified proteins reversibly modified by CoA.
  • Analysis revealed a significant number of metabolic enzymes are 'CoAlated'.
  • CoAlation was demonstrated to alter the activity of target proteins.

Conclusions:

  • CoAlation is a widespread post-translational modification.
  • CoAlation of metabolic enzymes is prevalent under stress conditions.
  • This modification likely plays a crucial role in the metabolic adaptation to stress.