ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1 leads to mitochondrial dysfunction and growth retardation

Takeshi Uchiumi, Kippei Ohgaki, Mikako Yagi, Yoshimasa Aoki, Aya Sakai, Shinya Matsumoto, Dongchon Kang

Research output: Contribution to journalArticlepeer-review

64 Citations (Scopus)

Abstract

ERAL1, a homologue of Era protein in Escherichia coli, is a member of conserved GTP-binding proteins with RNA-binding activity. Depletion of prokaryotic Era inhibits cell division without affecting chromosome segregation. Previously, we isolated ERAL1 protein as one of proteins which were associated with mitochondrial transcription factor A by using immunoprecipitation. In this study, we analysed the localization and function of ERAL1 in mammalian cells. ERAL1 was localized in mitochondrial matrix and associated with mitoribosomal proteins including the 12S rRNA. siRNA knockdown of ERAL1 decreased mitochondrial translation, caused redistribution of ribosomal small subunits and reduced 12S rRNA. The knockdown of ERAL1 in human HeLa cells elevated mitochondrial superoxide production and slightly decreased mitochondrial membrane potential. The knockdown inhibited the growth of HeLa cells with an accumulation of apoptotic cells. These results suggest that ERAL1 is localized in a small subunit of the mitochondrial ribosome, plays an important role in the small ribosomal constitution, and is also involved in cell viability.

Original languageEnglish
Article numbergkq305
Pages (from-to)5554-5568
Number of pages15
JournalNucleic acids research
Volume38
Issue number16
DOIs
Publication statusPublished - Apr 29 2010
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics

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