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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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Published on: August 8, 2017

Protein disorder prevails under crowded conditions.

C S Szasz1, A Alexa, K Toth

  • 1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary.

Biochemistry
|June 4, 2011
PubMed
Summary
This summary is machine-generated.

Cellular crowding influences protein structure. Intrinsically disordered proteins (IDPs) show limited structural changes under crowding, suggesting disorder is their physiological state.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cellular Biophysics

Background:

  • High macromolecular concentrations within cells, known as crowding, alter chemical equilibria.
  • This phenomenon can influence protein aggregation and folding, particularly for intrinsically disordered proteins (IDPs) lacking defined structures in vitro.
  • Understanding crowding effects on IDPs is crucial for comprehending their physiological roles.

Purpose of the Study:

  • To investigate the structural response of three intrinsically disordered proteins (IDPs) to cellular crowding conditions.
  • To compare the structural states of IDPs in dilute versus crowded environments.
  • To determine if crowding induces significant structural changes or pre-formation of binding-competent states in IDPs.

Main Methods:

  • Studied three IDPs: α-casein, MAP2c, and p21(Cip1).
  • Applied crowding agents: Dextran and Ficoll 70 (up to 40%) and trimethylamine N-oxide (TMAO) (up to 3.6 M).
  • Utilized diverse biophysical techniques: fluorescence spectroscopy, acrylamide quenching, ANS binding, FCS, and CD spectroscopy (far-UV and near-UV).

Main Results:

  • Crowding induced limited structural changes in IDPs, consistent with their functional requirements.
  • α-Casein exhibited minimal structural alterations under crowding.
  • MAP2c and p21(Cip1) showed signs of local structuring and global compaction, especially with TMAO, suggesting pre-formation of binding-competent conformations.
  • These changes were less pronounced than cooperative folding transitions observed in globular proteins.

Conclusions:

  • Intrinsically disordered proteins (IDPs) remain in a state of rapidly interconverting structural ensembles even under crowding.
  • Cellular crowding causes subtle structural adaptations in IDPs, potentially priming them for partner binding.
  • Structural disorder is confirmed as the native physiological state for these studied IDPs.