16 49

Cited 0 times in

RNA-dependent proteome solubility maintenance in Escherichia coli lysates analysed by quantitative mass spectrometry: Proteomic characterization in terms of isoelectric point, structural disorder, functional hub, and chaperone network

Authors
 Chan Park  ;  Bitnara Han  ;  Yura Choi  ;  Yoontae Jin  ;  Kwang Pyo Kim  ;  Seong Il Choi  ;  Baik L Seong 
Citation
 RNA BIOLOGY, Vol.21(1) : 1-18, 2024-01 
Journal Title
RNA BIOLOGY
ISSN
 1547-6286 
Issue Date
2024-01
MeSH
Escherichia coli Proteins* / metabolism ; Escherichia coli* / genetics ; Escherichia coli* / metabolism ; Isoelectric Point ; Mass Spectrometry ; Molecular Chaperones / genetics ; Molecular Chaperones / metabolism ; Protein Aggregates ; Protein Folding ; Proteome / metabolism ; Proteomics ; RNA / metabolism ; Solubility
Keywords
Aggregation ; RNA ; RNA-binding proteins ; intrinsically disordered regions (IDRs) ; molecular chaperones ; proteostasis
Abstract
Protein aggregation, a consequence of misfolding and impaired proteostasis, can lead to cellular malfunctions such as various proteinopathies. The mechanisms protecting proteins from aggregation in complex cellular environments have long been investigated, often from a protein-centric viewpoint. However, our study provides insights into a crucial, yet overlooked actor: RNA. We found that depleting RNAs from Escherichia coli lysates induces global protein aggregation. Our quantitative mass spectrometry analysis identified over 900 statistically significant proteins from the Escherichia coli proteome whose solubility depends on RNAs. Proteome-wide characterization showed that the RNA dependency is particularly enriched among acidic proteins, intrinsically disordered proteins, and structural hub proteins. Moreover, we observed distinct differences in RNA-binding mode and Gene Ontology categories between RNA-dependent acidic and basic proteins. Notably, the solubility of key molecular chaperones [Trigger factor, DnaJ, and GroES] is largely dependent on RNAs, suggesting a yet-to-be-explored hierarchical relationship between RNA-based chaperone (termed as chaperna) and protein-based chaperones, both of which constitute the whole chaperone network. These findings provide new insights into the RNA-centric role in maintaining healthy proteome solubility in vivo, where proteins associate with a variety of RNAs, either stably or transiently. © 2024 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.
Files in This Item:
T202402433.pdf Download
DOI
10.1080/15476286.2024.2315383
Appears in Collections:
1. College of Medicine (의과대학) > Research Institute (부설연구소) > 1. Journal Papers
Yonsei Authors
Choi, Seong Il(최성일)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/199147
사서에게 알리기
  feedback

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse

Links