Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu

Liquid-liquid phase separation (LLPS) has emerged as a crucial biological phenomenon underlying the sequestration of macromolecules (such as proteins and nucleic acids) into membraneless organelles in cells. Unstructured and intrinsically disordered domains are known to facilitate multivalent intera...

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Published in:Nature communications 2023-10, Vol.14 (1), p.6199-6199, Article 6199
Main Authors: Poudyal, Manisha, Patel, Komal, Gadhe, Laxmikant, Sawner, Ajay Singh, Kadu, Pradeep, Datta, Debalina, Mukherjee, Semanti, Ray, Soumik, Navalkar, Ambuja, Maiti, Siddhartha, Chatterjee, Debdeep, Devi, Jyoti, Bera, Riya, Gahlot, Nitisha, Joseph, Jennifer, Padinhateeri, Ranjith, Maji, Samir K.
Format: Article
Language:English
Subjects:
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Condensates
Electrostatic properties
Humanities and Social Sciences
Hydrophobicity
Liquid phases
Macromolecules
multidisciplinary
Nucleic acids
Organelles
Phase separation
Polyethylene glycol
Polypeptides
Proteins
Science
Science (multidisciplinary)
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Summary:Liquid-liquid phase separation (LLPS) has emerged as a crucial biological phenomenon underlying the sequestration of macromolecules (such as proteins and nucleic acids) into membraneless organelles in cells. Unstructured and intrinsically disordered domains are known to facilitate multivalent interactions driving protein LLPS. We hypothesized that LLPS could be an intrinsic property of proteins/polypeptides but with distinct phase regimes irrespective of their sequence and structure. To examine this, we studied many (a total of 23) proteins/polypeptides with different structures and sequences for LLPS study in the presence and absence of molecular crowder, polyethylene glycol (PEG-8000). We showed that all proteins and even highly charged polypeptides (under study) can undergo liquid condensate formation, however with different phase regimes and intermolecular interactions. We further demonstrated that electrostatic, hydrophobic, and H-bonding or a combination of such intermolecular interactions plays a crucial role in individual protein/peptide LLPS. In this work, the authors report that proteins/polypeptides with diverse sequences and structures can form liquid condensates, however with varying phase regimes and different modes of intermolecular interactions, spanning from electrostatic, hydrophobic and H-bond.
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-023-41864-9