Presentation Title

Phase Separation in the Cell

Format of Presentation

Poster to be presented the Friday of the conference

Abstract

Protein’s function is closely related to its structure: the polypeptide chain needs to be folded to its maximum stability state in order to carry out its function properly. The amino acid sequence of the polypeptide is the primary structure and will acquire secondary structure by the formation of hydrogen bonds. The tertiary structure is the overall tridimensional conformation and its folding is driven by hydrophobic interactions and reinforced by ionic interactions and hydrogen bonds. The protein folding process is tightly regulated in the cell because protein function depends on its conformation.

Although we attribute to each protein a defined structure and biological function, many have been found to have alternative folding patterns. This phenomenon was initially proposed to explain neurodegenerative diseases such as mad cow disease by the Prion Hypothesis and gained a Nobel Prize in 1997. Prions, meaning the protein in its alternative folding pattern, can lead a mammal’s neurones to death without macroscopic evidence but spongiform appearance under microscope. However, prion domains are relatively abundant among species. They share overall amino acidic composition rather than specific sequence, have low hydrophobicity and are intrinsically disordered and flexible.

These features permit the formation of amyloid-like aggregates, which give rise to the prion-related phenotypes as well as to the recently discovered and surprising ability to drive phase separation in the cell -- meaning biomolecular condensation inside the cell.

This poster reviews the important roles of this phenomenon in crucial processes like heterochromatin formation or nuclear-pore-transport filtering, and also the condensate’s physicochemical properties.

Department

Biological Sciences

Faculty Advisor

Don Nelson

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Phase Separation in the Cell

Protein’s function is closely related to its structure: the polypeptide chain needs to be folded to its maximum stability state in order to carry out its function properly. The amino acid sequence of the polypeptide is the primary structure and will acquire secondary structure by the formation of hydrogen bonds. The tertiary structure is the overall tridimensional conformation and its folding is driven by hydrophobic interactions and reinforced by ionic interactions and hydrogen bonds. The protein folding process is tightly regulated in the cell because protein function depends on its conformation.

Although we attribute to each protein a defined structure and biological function, many have been found to have alternative folding patterns. This phenomenon was initially proposed to explain neurodegenerative diseases such as mad cow disease by the Prion Hypothesis and gained a Nobel Prize in 1997. Prions, meaning the protein in its alternative folding pattern, can lead a mammal’s neurones to death without macroscopic evidence but spongiform appearance under microscope. However, prion domains are relatively abundant among species. They share overall amino acidic composition rather than specific sequence, have low hydrophobicity and are intrinsically disordered and flexible.

These features permit the formation of amyloid-like aggregates, which give rise to the prion-related phenotypes as well as to the recently discovered and surprising ability to drive phase separation in the cell -- meaning biomolecular condensation inside the cell.

This poster reviews the important roles of this phenomenon in crucial processes like heterochromatin formation or nuclear-pore-transport filtering, and also the condensate’s physicochemical properties.