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Preserving condensate structure and composition by lowering sequence complexity.

Amogh Sood¹, Bin Zhang¹

¹Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.

Biorxiv : the Preprint Server for Biology

|December 11, 2023

Summary

Intrinsically disordered proteins (IDPs) form biological condensates. Specific interactions drive ordered condensates, while non-specific interactions create disorganized ones, influencing cellular organization.

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Chemical Dimerization-Induced Protein Condensates on Telomeres

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Area of Science:

Cellular Biology
Biophysics
Protein Science

Background:

Biological condensates organize cellular chemistry by selectively partitioning biomolecules.
Intrinsically disordered proteins (IDPs) are key components due to their flexibility and multivalent interactions.
Understanding the sequence-structure-function relationship of IDPs in condensates is crucial.

Approach:

Extended the "stickers and spacers" model to include non-specific spacer-spacer interactions.
Analyzed the impact of specific sticker-sticker interactions versus non-specific spacer interactions on condensate properties.
Investigated the role of evolutionary pressures on IDP sequences and condensate formation.

Key Points:

Non-specific spacer interactions promote phase separation but lead to disorganized condensates.
Specific sticker-sticker interactions are essential for forming structurally defined and compositionally controlled condensates.
Low complexity domains in IDPs may have evolved to suppress spurious interactions and promote functional condensate assembly.

Conclusions:

The balance between specific and non-specific interactions dictates condensate organization and function.
IDP sequence features, particularly low complexity domains, are critical for forming biologically relevant condensates.
This work provides a theoretical framework for understanding the molecular grammar of intrinsically disordered proteins in phase separation.