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

Tatsuya Niwa, Kei Fujiwara, Hideki Taguchi

研究成果: Article

2 引用 (Scopus)

抄録

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.

元の言語English
ページ(範囲)251-257
ページ数7
ジャーナルFEBS Letters
590
発行部数2
DOI
出版物ステータスPublished - 2016 1 1

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Proteomics
Chaperonins
Protein Folding
Substrates
Mass Spectrometry
Escherichia coli
Mass spectrometry
In Vitro Techniques
Proteins

ASJC Scopus subject areas

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

これを引用

Identification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach. / Niwa, Tatsuya; Fujiwara, Kei; Taguchi, Hideki.

:: FEBS Letters, 巻 590, 番号 2, 01.01.2016, p. 251-257.

研究成果: Article

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