Document Type

Poster

Publication Date

Summer 7-26-2024

Program/Event

Undergraduate Arts and Research Showcase

Abstract

Liquid-Liquid Phase Separation (LLPS) is a process when a polypeptide condenses into a dense and dilute phase in aqueous solutions. Within cells, this process is believed to relate to stress regulation and various cellular processes. Several stress-related proteins found only during the embryonic developmental stage of diapause in the brine shrimp, A. franciscana, have been observed to undergo LLPS in vitro. Our results show that the small heat shock protein (sHSP) p26 has a greater propensity to LLPS under varying salt concentrations compared to LEA6, a late embryogenesis abundant protein (LEA). At a protein concentration of 1.31 mg/ml in a buffer that mimics the cellular environment of diapaused cysts, LLPS of LEA6 occurred at pH 6.4, but not at pH 7.8. These results are significant since a pH drop occurs in the organism during anoxic quiescence, which is a prolonged state of environmentally regulated metabolic arrest. These observations suggest a possible function of LLPS proteins which is dependent on pH levels.

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