title: Identification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach.
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.
authors.affiliation: Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan.
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Niwa
authors.affiliation: Department of Biosciences & Informatics, Faculty of Science and Technology, Keio University, Kohokuku, Yokohama, Japan.
authors.forename: Kei
authors.initials: K
authors.lastname: Fujiwara
authors.affiliation: Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan.
authors.forename: Hideki
authors.initials: H
authors.lastname: Taguchi
mesh_terms: D002474:Cell-Free System; D018835:Chaperonin 10 / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism*; D011485:Protein Binding; D040901:Proteomics
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60
keywords: GroEL; chaperone; chaperonin; protein aggregation; protein folding