Nucleic acid actions on abnormal protein aggregation, phase transitions and phase separation

Jerson L Silva; Tuane C Vieira; Yraima Cordeiro; Guilherme A P de Oliveira

doi:10.1016/j.sbi.2022.102346

Nucleic acid actions on abnormal protein aggregation, phase transitions and phase separation

Curr Opin Struct Biol. 2022 Apr:73:102346. doi: 10.1016/j.sbi.2022.102346. Epub 2022 Mar 2.

Authors

Jerson L Silva¹, Tuane C Vieira², Yraima Cordeiro³, Guilherme A P de Oliveira⁴

Affiliations

¹ Institute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ, 21941-901, Brazil. Electronic address: [email protected].
² Institute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ, 21941-901, Brazil.
³ Faculty of Pharmacy, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
⁴ Institute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ, 21941-901, Brazil. Electronic address: [email protected].

PMID: 35247749
DOI: 10.1016/j.sbi.2022.102346

Abstract

Liquid-liquid phase separation (LLPS) and phase transitions (PT) of proteins, which include the formation of gel- and solid-like species, have been characterized as physical processes related to the pathology of conformational diseases. Nucleic acid (NA)-binding proteins related to neurodegenerative disorders and cancer were shown by us and others to experience PT modulated by different NAs. Herein, we discuss recent work on phase separation and phase transitions of two amyloidogenic proteins, i.e. the prion protein (PrP) and p53, which undergo conformational changes and aggregate upon NA interaction. The role of different NAs in these processes is discussed to shed light on the relevance of PSs and PTs for both the functional and pathological roles of these mammalian proteins.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Amyloidogenic Proteins
Animals
Mammals / metabolism
Nucleic Acids*
Prion Proteins / chemistry
Prion Proteins / metabolism
Prions* / chemistry
Prions* / metabolism
Protein Aggregates
Protein Aggregation, Pathological / metabolism

Substances

Amyloidogenic Proteins
Nucleic Acids
Prion Proteins
Prions
Protein Aggregates