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Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL

Academic Article
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Overview

authors

  • Chapman, Eli
  • Farr, G. W.
  • Usaite, R.
  • Furtak, K.
  • Fenton, W. A.
  • Chaudhuri, T. K.
  • Hondorp, E. R.
  • Matthews, R. G.
  • Wolf, S. G.
  • Yates III, John
  • Pypaert, M.
  • Horwich, A. L.

publication date

  • October 2006

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • In a newly isolated temperature-sensitive lethal Escherichia coli mutant affecting the chaperonin GroEL, we observed wholesale aggregation of newly translated proteins. After temperature shift, transcription, translation, and growth slowed over two to three generations, accompanied by filamentation and accretion (in approximately 2% of cells) of paracrystalline arrays containing mutant chaperonin complex. A biochemically isolated inclusion body fraction contained the collective of abundant proteins of the bacterial cytoplasm as determined by SDS/PAGE and proteolysis/MS analyses. Pulse-chase experiments revealed that newly made proteins, but not preexistent ones, were recruited to this insoluble fraction. Although aggregation of "stringent" GroEL/GroES-dependent substrates may secondarily produce an "avalanche" of aggregation, the observations raise the possibility, supported by in vitro refolding experiments, that the widespread aggregation reflects that GroEL function supports the proper folding of a majority of newly translated polypeptides, not just the limited number indicated by interaction studies and in vitro experiments.

subject areas

  • Chaperonin 60
  • Escherichia coli
  • Escherichia coli Proteins
  • Inclusion Bodies
  • Methyltransferases
  • Mutation
  • Phenotype
  • Protein Biosynthesis
  • Proteomics
  • Solubility
  • Substrate Specificity
  • Temperature
  • Time Factors
  • Transcription, Genetic
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Research

keywords

  • chaperone
  • misfolding
  • protein folding
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Identity

PubMed Central ID

  • PMC1613232

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0607534103

PubMed ID

  • 17043235
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Additional Document Info

start page

  • 15800

end page

  • 15805

volume

  • 103

issue

  • 43

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