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Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.

Alaji Bah1, Julie D Forman-Kay2

  • 1From the Program in Molecular Structure & Function, The Hospital for Sick Children, Toronto, Ontario M5G 0A4 and the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada alaji.bah@sickkids.ca.

The Journal of Biological Chemistry
|February 7, 2016
PubMed
Summary
This summary is machine-generated.

Post-translational modifications (PTMs) alter intrinsically disordered proteins (IDPs) by changing their structure and function. New tools allow studying these PTM-mediated regulatory mechanisms in IDPs.

Keywords:
intrinsically disordered proteinpost-translational modification (PTM)protein conformationprotein-DNA interactionprotein-protein interactionregulation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Intrinsically disordered proteins (IDPs) lack stable structures but are crucial in cellular processes.
  • Post-translational modifications (PTMs) significantly impact IDP structure and function.
  • PTMs can shift IDPs between disordered, ordered, monomeric, and phase-separated states.

Purpose of the Study:

  • To discuss biological processes regulated by PTMs in IDPs.
  • To present tools for creating homogenous PTM-modified IDPs.
  • To explore PTM-mediated regulatory mechanisms in IDPs.

Main Methods:

  • Review of existing literature on PTMs and IDPs.
  • Discussion of biological roles of PTM-regulated IDPs.
  • Presentation of novel methodologies for IDP modification.

Main Results:

  • PTMs induce significant structural changes in IDPs by altering their energy landscapes.
  • PTMs can trigger local structural changes or global disorder-to-order transitions.
  • PTMs regulate diverse biological processes involving IDPs.

Conclusions:

  • PTM regulation is a key mechanism controlling IDP function.
  • Homogenously modified IDPs are essential for studying PTM effects.
  • Advanced tools facilitate research into PTM-mediated IDP regulation.