Characterization of hnRNPK protein structural transitions and interactions

Brian Le

doi:10.26182/7tj7-s311

Characterization of hnRNPK protein structural transitions and interactions

Brian Le

School of Molecular Sciences

Research output: Thesis › Doctoral Thesis

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Abstract

This thesis demonstrates the structural properties and RNA-binding functions of the human protein heterogeneous nuclear ribonucleoprotein K (hnRNPK) in four distinct states; aggregate, monomer, fibrillar hydrogel, and phase-separated state; using structural and biophysical analysis methods. A variety of experiments have successfully identified factors driving hnRNPK protein to transition into four aforementioned states. Additionally, the use of stabilizing additives enables reversible transitions of hnRNPK between monomeric and aggregate states. The insights provided by this thesis unravel an exciting prospect of state transitions in the cell, allowing biological materials to transform between physical states, and coordinating cellular mechanisms under stress.

Original language	English
Qualification	Doctor of Philosophy
Awarding Institution	The University of Western Australia
Supervisors/Advisors	Bond, Charlie, Supervisor Fox, Archa, Supervisor Swaminatha Iyer, Iyer, Supervisor
Award date	28 Jun 2022
DOIs	https://doi.org/10.26182/7tj7-s311
Publication status	Unpublished - 2021

Embargo information

Embargoed from 05/08/2022 to 01/07/2023. Made publicly available on 01/07/2023.

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10.26182/7tj7-s311

THESIS - DOCTOR OF PHILOSOPHY - LE, Quang Dung Brian - 2022
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Cite this

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title = "Characterization of hnRNPK protein structural transitions and interactions",

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AB - This thesis demonstrates the structural properties and RNA-binding functions of the human protein heterogeneous nuclear ribonucleoprotein K (hnRNPK) in four distinct states; aggregate, monomer, fibrillar hydrogel, and phase-separated state; using structural and biophysical analysis methods. A variety of experiments have successfully identified factors driving hnRNPK protein to transition into four aforementioned states. Additionally, the use of stabilizing additives enables reversible transitions of hnRNPK between monomeric and aggregate states. The insights provided by this thesis unravel an exciting prospect of state transitions in the cell, allowing biological materials to transform between physical states, and coordinating cellular mechanisms under stress.

KW - hnRNPK

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KW - multiple physical states

KW - additives

KW - reversible transitions

KW - RNA-binding

KW - structural translations

KW - gelation

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DO - 10.26182/7tj7-s311

M3 - Doctoral Thesis

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Characterization of hnRNPK protein structural transitions and interactions

Abstract

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