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 journalArticle

50 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

Fingerprint

HeLa Cells
Growth
Small Ribosome Subunits
Chromosome Segregation
Proteins
Mitochondrial Membrane Potential
Escherichia coli Proteins
Constitution and Bylaws
GTP-Binding Proteins
Immunoprecipitation
Superoxides
Cell Division
Small Interfering RNA
Cell Survival
RNA
Mitochondrial Ribosomes
ribosomal RNA 12S
mitochondrial transcription factor A

All Science Journal Classification (ASJC) codes

  • Genetics

Cite this

ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1 leads to mitochondrial dysfunction and growth retardation. / Uchiumi, Takeshi; Ohgaki, Kippei; Yagi, Mikako; Aoki, Yoshimasa; Sakai, Aya; Matsumoto, Shinya; Kang, Dongchon.

In: Nucleic acids research, Vol. 38, No. 16, gkq305, 29.04.2010, p. 5554-5568.

Research output: Contribution to journalArticle

Uchiumi, Takeshi ; Ohgaki, Kippei ; Yagi, Mikako ; Aoki, Yoshimasa ; Sakai, Aya ; Matsumoto, Shinya ; Kang, Dongchon. / ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1 leads to mitochondrial dysfunction and growth retardation. In: Nucleic acids research. 2010 ; Vol. 38, No. 16. pp. 5554-5568.
@article{f88ae354590a430c959929be3102cea5,
title = "ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1 leads to mitochondrial dysfunction and growth retardation",
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.",
author = "Takeshi Uchiumi and Kippei Ohgaki and Mikako Yagi and Yoshimasa Aoki and Aya Sakai and Shinya Matsumoto and Dongchon Kang",
year = "2010",
month = "4",
day = "29",
doi = "10.1093/nar/gkq305",
language = "English",
volume = "38",
pages = "5554--5568",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "16",

}

TY - JOUR

T1 - ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1 leads to mitochondrial dysfunction and growth retardation

AU - Uchiumi, Takeshi

AU - Ohgaki, Kippei

AU - Yagi, Mikako

AU - Aoki, Yoshimasa

AU - Sakai, Aya

AU - Matsumoto, Shinya

AU - Kang, Dongchon

PY - 2010/4/29

Y1 - 2010/4/29

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=77956539977&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77956539977&partnerID=8YFLogxK

U2 - 10.1093/nar/gkq305

DO - 10.1093/nar/gkq305

M3 - Article

C2 - 20430825

AN - SCOPUS:77956539977

VL - 38

SP - 5554

EP - 5568

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 16

M1 - gkq305

ER -