Identification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach

Tatsuya Niwa, Kei Fujiwara, Hideki Taguchi

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Chaperones are essential to maintain the proper folding of various proteins in vivo. The Escherichia coli chaperonin GroEL/GroES (GroE) is one of the best-studied chaperones, and its in vivo substrates have been identified, mainly by mass spectrometry-based proteomic studies. Here, we newly identified 20 in vivo obligate GroE substrates with the aid of data from an in vitro comprehensive analysis. The newly identified substrates have similar physicochemical properties to the known substrates, but their expression levels in vivo were significantly lower. Information from the in vitro comprehensive analysis has the potential to compensate for limitations of the MS-based proteomic approaches.

Original languageEnglish
Pages (from-to)251-257
Number of pages7
JournalFEBS Letters
Volume590
Issue number2
DOIs
Publication statusPublished - 2016 Jan 1

Keywords

  • chaperone
  • chaperonin
  • GroEL
  • protein aggregation
  • protein folding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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