The aggregation properties of Escherichia coli proteins associated with their cellular abundance

Virginia Castillo, Ricardo Graña-Montes, Salvador Ventura

Research output: Contribution to journalArticleResearchpeer-review

26 Citations (Scopus)

Abstract

Proteins are key players in most cellular processes. Therefore, their abundances are thought to be tightly regulated at the gene-expression level. Recent studies indicate, however, that steady-state cellular-protein concentrations correlate better across species than the levels of the corresponding mRNAs; this supports the existence of selective forces to maintain precise cellular-protein concentrations and homeostasis, even if gene-expression levels diverge. One of these forces might be the avoidance of protein aggregation because, in the cell, the folding of proteins into functional conformations might be in competition with anomalous aggregation into non-functional and usually toxic structures in a concentration-dependent manner. The data in the present work provide support for this hypothesis because, in E. coli, the experimental solubility of proteins correlates better with the cellular abundance than with the gene-expression levels. We found that the divergence between protein and mRNAs levels is low for high-abundance proteins. This suggests that because abundant proteins are at higher risk of aggregation, cellular concentrations need to be stringently regulated by gene expression. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish
Pages (from-to)752-760
JournalBiotechnology Journal
Volume6
DOIs
Publication statusPublished - 1 Jun 2011

Keywords

  • Escherichia coli
  • Protein aggregation
  • Protein evolution
  • Protein expression
  • Protein folding

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