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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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Updated: Jun 28, 2026

Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
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Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications

Published on: October 30, 2013

Post-translational modifications guard yeast from misaspartylation.

Michaël Ryckelynck1, Caroline A Paulus, Magali Frugier

  • 1ISIS-ULP, Laboratoire de Biologie Chimique, Strasbourg, France.

Biochemistry
|October 30, 2008
PubMed
Summary

Yeast cells control aspartyl-tRNA synthetase (AspRS) levels to prevent errors in protein synthesis. This study found a new mechanism involving N-terminal modifications that further limits AspRS activity and toxicity.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Yeast Genetics

Background:

  • Yeast aspartyl-tRNA synthetase (AspRS) is regulated post-transcriptionally to maintain cellular homeostasis.
  • This regulation ensures accurate amino acid attachment to tRNAs, preventing translation errors.

Purpose of the Study:

  • To investigate the consequences of artificially increasing AspRS concentration in vivo.
  • To identify additional cellular mechanisms that control AspRS activity and prevent toxicity.

Main Methods:

  • In vivo manipulation of AspRS levels in yeast.
  • Analysis of tRNA misacylation and post-translational stress markers.
  • Identification of post-translational modifications on AspRS.

Main Results:

  • Elevated AspRS levels did not lead to tRNA misaspartylation or associated stress.
  • A novel cellular mechanism, involving post-translational modifications in the AspRS N-terminal extension, was identified.
  • This mechanism appears to reduce the likelihood of AspRS binding to noncognate tRNAs.

Conclusions:

  • Yeast employs a sophisticated, multi-layered regulatory system to control AspRS.
  • Post-translational modifications in the AspRS N-terminus act as a critical "cellular lock" to prevent enzyme toxicity.
  • This finding enhances our understanding of translational control and enzyme regulation.