Involvement of mitochondrial ribosomal proteins in ribosomal RNA-mediated protein folding

Anindita Das, Jaydip Ghosh, Arpita Bhattacharya, Dibyendu Samanta, Debasis Das, Chanchal Das Gupta

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


The peptidyl transferase center of the domain V of large ribosomal RNA in the prokaryotic and eukaryotic cytosolic ribosomes acts as general protein folding modulator. We showed earlier that one part of the domain V (RNA1 containing the peptidyl transferase loop) binds unfolded protein and directs it to a folding competent state (FCS) that is released by the other part (RNA2) to attain the folded native state by itself. Here we show that the peptidyl transferase loop of the mitochondrial ribosome releases unfolded proteins in FCS extremely slowly despite its lack of the rRNA segment analogous to RNA2. The release of FCS can be hastened by the equivalent activity of RNA2 or the large subunit proteins of the mitochondrial ribosome. The RNA2 or large subunit proteins probably introduce some allosteric change in the peptidyl transferase loop to enable it to release proteins in FCS.

Original languageEnglish (US)
Pages (from-to)43771-43781
Number of pages11
JournalJournal of Biological Chemistry
Issue number51
StatePublished - Dec 23 2011
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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