Another function for the mitochondrial ribosomal RNA: Protein folding

I. Sulijoadikusumo, N. Horikoshi, A. Usheva*

*Corresponding author for this work

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

Specialized proteins known as molecular chaperones bind transiently to non-native conformational states of proteins and protein complexes to promote transition to a biologically active conformation. Recently, it was demonstrated in vitro that proteins do not uniquely possess this activity. We show that mitochondrial 12S and 16S ribosomal RNA can fold chemically denatured proteins and reactivate heat-induced aggregated proteins in vitro. This chaperone action is ATP-independent. The specific secondary structure of the mitochondrial rRNA is critical to its folding activity. Furthermore, mutant mitochondrial 16S rRNA from aged cardiac muscle cells lacked this activity. We propose that mitochondrial 12S and 16S ribosomal RNA may play an important role in protein folding in mitochondria.

Original languageEnglish (US)
Pages (from-to)11559-11564
Number of pages6
JournalBiochemistry
Volume40
Issue number38
DOIs
StatePublished - Sep 25 2001

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Another function for the mitochondrial ribosomal RNA: Protein folding'. Together they form a unique fingerprint.

  • Cite this

    Sulijoadikusumo, I., Horikoshi, N., & Usheva, A. (2001). Another function for the mitochondrial ribosomal RNA: Protein folding. Biochemistry, 40(38), 11559-11564. https://doi.org/10.1021/bi015526q