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Eukaryotic Post-Translational Regulation definitions

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  • Post-Translational Modification
    Covalent chemical change to a protein after translation, altering its activity, stability, or marking it for breakdown.
  • PTM
    Abbreviation for modifications that occur to proteins after translation, impacting their function or fate.
  • Protein Activity
    Functional state of a protein, which can be switched on or off by chemical changes after synthesis.
  • Protease
    Enzyme that breaks down proteins by cleaving polypeptide bonds, producing amino acids.
  • Polypeptide Bond
    Chemical linkage between amino acids in a protein, targeted for cleavage during protein degradation.
  • Protein Degradation
    Process of breaking down proteins into amino acids, often to remove damaged or unneeded proteins.
  • Ubiquitination
    Attachment of a small peptide tag to a protein, signaling it for destruction by cellular enzymes.
  • Ubiquitin
    Small peptide that serves as a tag for proteins destined for breakdown by cellular machinery.
  • Ubiquitin Ligase
    Enzyme responsible for attaching a peptide tag to proteins, marking them for degradation.
  • Cytoplasm
    Cellular compartment where protein modifications and tagging for degradation typically occur.
  • Gene Expression
    Overall process by which genetic information leads to functional proteins, regulated at multiple stages.
  • Amino Acid
    Building block of proteins, released when enzymes break down polypeptide chains.
  • Modification Tag
    Chemical group or peptide added to a protein to alter its function or signal its removal.
  • Inactive Protein
    Form of a protein that lacks functional activity, often requiring modification to become active or be degraded.
  • Misfolded Protein
    Protein with incorrect three-dimensional structure, often targeted for removal to maintain cellular health.