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Disorder-mediated interactions target proteins to specific condensates.

Nancy De La Cruz1, Prashant Pradhan1, Reshma T Veettil1

  • 1Laboratory of Nuclear Organization, Cecil H. and Ida Green Center for Reproductive Biology Sciences, Division of Basic Research, Department of Obstetrics and Gynecology, Department of Molecular Biology, Hamon Center for Regenerative Science and Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

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Biomolecular condensates achieve distinct compositions through specific protein interactions. Intrinsically disordered regions (IDRs) of proteins are key to this selective partitioning, controlling cellular biochemistry spatially.

Keywords:
IDRbiomolecular condensatescondensate compositioncondensate functionintrinsically disordered regionsnuclear organizationspecificity

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Selective compartmentalization regulates cellular biochemistry.
  • Membrane-bound organelles use semi-permeable barriers, while biomolecular condensates use constituent interactions.
  • Protein intrinsically disordered regions (IDRs) drive dynamic condensate formation, but their role in compositional specificity is unclear.

Purpose of the Study:

  • To investigate if distinct biomolecular condensate compositions arise from dynamic interactions.
  • To determine the role of intrinsically disordered regions (IDRs) in selective protein partitioning into condensates.

Main Methods:

  • Comparative analysis of proteins differentially partitioned by two distinct biomolecular condensates.
  • Assessing the necessity and sufficiency of IDRs for selective partitioning.
  • Investigating the impact of sequence features within IDRs on partitioning specificity.
  • Experimentally swapping IDRs to observe effects on protein targeting and biochemical activity.

Main Results:

  • Distinct biomolecular condensate compositions arise from specific IDR-mediated interactions.
  • The IDRs of differentially partitioned proteins are both necessary and sufficient for selective partitioning.
  • Specific sequence features within IDRs dictate partitioning, and altering these features changes partitioning specificity.
  • Swapping entire IDRs successfully retargets proteins and their associated biochemical activities to different condensates.

Conclusions:

  • IDR-mediated interactions provide a mechanism for targeting proteins to specific biomolecular condensates.
  • This IDR-driven targeting enables precise spatial regulation of biochemical activities within the cell.
  • The findings reveal a fundamental principle governing condensate composition and cellular organization.