In vitro protein folding by E. coli ribosome: Unfolded protein splitting 70S to interact with 50S subunit

Arunima Basu, Dibyendu Samanta, Debasis Das, Saheli Chowdhury, Arpita Bhattacharya, Jaydip Ghosh, Anindita Das, Chanchal DasGupta

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

Folding of unfolded protein on Escherichia coli 70S ribosome is accompanied by rapid dissociation of the ribosome into 50S and 30S subunits. The dissociation rate of 70S ribosome with unfolded protein is much faster than that caused by combined effect of translation and polypeptide release factors known to be involved in the dissociation of ribosome into subunits. The protein then reaches a "folding competent" state on 50S and is released to take up native conformation by itself. Release before attaining the folding competent state or prevention of release by cross-linking it with ribosome, would not allow the protein to get back to its native conformation.

Original languageEnglish (US)
Pages (from-to)598-603
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume366
Issue number2
DOIs
StatePublished - Feb 8 2008

Keywords

  • 50S subunit
  • Protein folding
  • Ribosomal subunit dissociation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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