메뉴 건너뛰기




Volumn 38, Issue 16, 2010, Pages 5554-5568

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

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CARBAMOYL PHOSPHATE SYNTHASE; DEATH ASSOCIATED PROTEIN KINASE; ELONGATION FACTOR TU; ERAL1 PROTEIN; GLUTAMATE DEHYDROGENASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCINE HYDROXYMETHYLTRANSFERASE; GUANINE NUCLEOTIDE BINDING PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HYDROGEN PEROXIDE; INITIATION FACTOR 2; ISOLEUCINE TRANSFER RNA LIGASE; MALATE DEHYDROGENASE; PROHIBITIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PYRROLINE 5 CARBOXYLATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE; RIBOSOME PROTEIN; RNA 12S; RNA 28S; SMALL INTERFERING RNA; SUCCINATE DEHYDROGENASE; SUPEROXIDE; THREONINE TRANSFER RNA LIGASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR A; UNCLASSIFIED DRUG; VIMENTIN; CYTOCHROME C OXIDASE; ERAL1 PROTEIN, HUMAN; MITOCHONDRIAL PROTEIN; RNA; RNA BINDING PROTEIN; RNA, MITOCHONDRIAL;

EID: 77956539977     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq305     Document Type: Article
Times cited : (89)

References (47)
  • 1
    • 22044443172 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A in the maintenance of mitochondrial DNA: overview of its multiple roles
    • Kang,D. and Hamasaki,N. (2005) Mitochondrial transcription factor A in the maintenance of mitochondrial DNA: overview of its multiple roles. Ann. NY Acad. Sci., 1042, 101-108.
    • (2005) Ann. NY Acad. Sci. , vol.1042 , pp. 101-108
    • Kang, D.1    Hamasaki, N.2
  • 2
    • 33847792061 scopus 로고    scopus 로고
    • Mitochondrial transcription and its regulation in mammalian cells
    • Asin-Cayuela,J. and Gustafsson,C.M. (2007) Mitochondrial transcription and its regulation in mammalian cells. Trends Biochem. Sci., 32, 111-117.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 111-117
    • Asin-Cayuela, J.1    Gustafsson, C.M.2
  • 3
    • 34548627532 scopus 로고    scopus 로고
    • DNA replication and transcription in mammalian mitochondria
    • Falkenberg,M., Larsson,N.G. and Gustafsson,C.M. (2007) DNA replication and transcription in mammalian mitochondria. Annu. Rev. Biochem., 76, 679-699.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 679-699
    • Falkenberg, M.1    Larsson, N.G.2    Gustafsson, C.M.3
  • 4
    • 0028436180 scopus 로고
    • Protein synthesis in mitochondria
    • Pel,H.J. and Grivell,L.A. (1994) Protein synthesis in mitochondria. Mol. Biol. Rep., 19, 183-194.
    • (1994) Mol. Biol. Rep. , vol.19 , pp. 183-194
    • Pel, H.J.1    Grivell, L.A.2
  • 6
    • 0037029122 scopus 로고    scopus 로고
    • Evolution of a protein-rich mitochondrial ribosome: implications for human genetic disease
    • O'Brien,T.W. (2002) Evolution of a protein-rich mitochondrial ribosome: implications for human genetic disease. Gene, 286, 73-79.
    • (2002) Gene , vol.286 , pp. 73-79
    • O'Brien, T.W.1
  • 7
    • 0035416644 scopus 로고    scopus 로고
    • The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders
    • Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S., Watanabe,K. and Tanaka,T. (2001) The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders. Genomics, 77, 65-70.
    • (2001) Genomics , vol.77 , pp. 65-70
    • Kenmochi, N.1    Suzuki, T.2    Uechi, T.3    Magoori, M.4    Kuniba, M.5    Higa, S.6    Watanabe, K.7    Tanaka, T.8
  • 9
    • 33744752749 scopus 로고    scopus 로고
    • The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1
    • Antonicka,H., Sasarman,F., Kennaway,N.G. and Shoubridge,E.A. (2006) The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1. Hum. Mol. Genet., 15, 1835-1846.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1835-1846
    • Antonicka, H.1    Sasarman, F.2    Kennaway, N.G.3    Shoubridge, E.A.4
  • 11
    • 45449099046 scopus 로고    scopus 로고
    • The effect of mutated mitochondrial ribosomal proteins S16 and S22 on the assembly of the small and large ribosomal subunits in human mitochondria
    • Emdadul Haque,M., Grasso,D., Miller,C., Spremulli,L.L. and Saada,A. (2008) The effect of mutated mitochondrial ribosomal proteins S16 and S22 on the assembly of the small and large ribosomal subunits in human mitochondria. Mitochondrion, 8, 254-261.
    • (2008) Mitochondrion , vol.8 , pp. 254-261
    • Emdadul Haque, M.1    Grasso, D.2    Miller, C.3    Spremulli, L.L.4    Saada, A.5
  • 12
    • 33644674439 scopus 로고    scopus 로고
    • The organization and inheritance of the mitochondrial genome
    • Chen,X.J. and Butow,R.A. (2005) The organization and inheritance of the mitochondrial genome. Nat. Rev. Genet., 6, 815-825.
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 815-825
    • Chen, X.J.1    Butow, R.A.2
  • 13
    • 36248997738 scopus 로고    scopus 로고
    • Evolutionary tinkering with mitochondrial nucleoids
    • Kucej,M. and Butow,R.A. (2007) Evolutionary tinkering with mitochondrial nucleoids. Trends Cell Biol., 17, 586-592.
    • (2007) Trends Cell Biol. , vol.17 , pp. 586-592
    • Kucej, M.1    Butow, R.A.2
  • 14
    • 0025829045 scopus 로고
    • Similarity of human mitochondrial transcription factor 1 to high mobility group proteins
    • Parisi,M.A. and Clayton,D.A. (1991) Similarity of human mitochondrial transcription factor 1 to high mobility group proteins. Science, 252, 965-969.
    • (1991) Science , vol.252 , pp. 965-969
    • Parisi, M.A.1    Clayton, D.A.2
  • 15
    • 0034630725 scopus 로고    scopus 로고
    • Binding of human mitochondrial transcription factor A, an HMG box protein, to a four-way DNA junction
    • Ohno,T., Umeda,S., Hamasaki,N. and Kang,D. (2000) Binding of human mitochondrial transcription factor A, an HMG box protein, to a four-way DNA junction. Biochem. Biophys. Res. Commun., 271, 492-498.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 492-498
    • Ohno, T.1    Umeda, S.2    Hamasaki, N.3    Kang, D.4
  • 16
    • 44849128599 scopus 로고    scopus 로고
    • Expression and maintenance of mitochondrial DNA: new insights into human disease pathology
    • Shadel,G.S. (2008) Expression and maintenance of mitochondrial DNA: new insights into human disease pathology. Am. J. Pathol., 172, 1445-1456.
    • (2008) Am. J. Pathol. , vol.172 , pp. 1445-1456
    • Shadel, G.S.1
  • 18
    • 0034043879 scopus 로고    scopus 로고
    • Analysis of guanine nucleotide binding and exchange kinetics of the Escherichia coli GTPase Era
    • Sullivan,S.M., Mishra,R., Neubig,R.R. and Maddock,J.R. (2000) Analysis of guanine nucleotide binding and exchange kinetics of the Escherichia coli GTPase Era. J. Bacteriol., 182, 3460-3466.
    • (2000) J. Bacteriol. , vol.182 , pp. 3460-3466
    • Sullivan, S.M.1    Mishra, R.2    Neubig, R.R.3    Maddock, J.R.4
  • 19
    • 0034067634 scopus 로고    scopus 로고
    • Era GTPase of Escherichia coli: binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates
    • Meier,T.I., Peery,R.B., McAllister,K.A. and Zhao,G. (2000) Era GTPase of Escherichia coli: binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates. Microbiology, 146, 1071-1083.
    • (2000) Microbiology , vol.146 , pp. 1071-1083
    • Meier, T.I.1    Peery, R.B.2    McAllister, K.A.3    Zhao, G.4
  • 21
    • 0037422192 scopus 로고    scopus 로고
    • Elimination of the vertebrate Escherichia coli Ras-like protein homologue leads to cell cycle arrest at G1 phase and apoptosis
    • Gohda,J., Nomura,Y., Suzuki,H., Arai,H., Akiyama,T. and Inoue,J. (2003) Elimination of the vertebrate Escherichia coli Ras-like protein homologue leads to cell cycle arrest at G1 phase and apoptosis. Oncogene, 22, 1340-1348.
    • (2003) Oncogene , vol.22 , pp. 1340-1348
    • Gohda, J.1    Nomura, Y.2    Suzuki, H.3    Arai, H.4    Akiyama, T.5    Inoue, J.6
  • 23
    • 11144354662 scopus 로고    scopus 로고
    • Targeted disruption of one allele of the Y-box binding protein-1 (YB-1) gene in mouse embryonic stem cells and increased sensitivity to cisplatin and mitomycin C
    • Shibahara,K., Uchiumi,T., Fukuda,T., Kura,S., Tominaga,Y., Maehara,Y., Kohno,K., Nakabeppu,Y., Tsuzuki,T. and Kuwano,M. (2004) Targeted disruption of one allele of the Y-box binding protein-1 (YB-1) gene in mouse embryonic stem cells and increased sensitivity to cisplatin and mitomycin C. Cancer Sci., 95, 348-353.
    • (2004) Cancer Sci. , vol.95 , pp. 348-353
    • Shibahara, K.1    Uchiumi, T.2    Fukuda, T.3    Kura, S.4    Tominaga, Y.5    Maehara, Y.6    Kohno, K.7    Nakabeppu, Y.8    Tsuzuki, T.9    Kuwano, M.10
  • 25
    • 34248632009 scopus 로고    scopus 로고
    • The C-terminal tail of mitochondrial transcription factor a markedly strengthens its general binding to DNA
    • Ohgaki,K., Kanki,T., Fukuoh,A., Kurisaki,H., Aoki,Y., Ikeuchi,M., Kim,S.H., Hamasaki,N. and Kang,D. (2007) The C-terminal tail of mitochondrial transcription factor a markedly strengthens its general binding to DNA. J. Biochem., 141, 201-211.
    • (2007) J. Biochem. , vol.141 , pp. 201-211
    • Ohgaki, K.1    Kanki, T.2    Fukuoh, A.3    Kurisaki, H.4    Aoki, Y.5    Ikeuchi, M.6    Kim, S.H.7    Hamasaki, N.8    Kang, D.9
  • 26
    • 0035896652 scopus 로고    scopus 로고
    • Nam1p, a protein involved in RNA processing and translation, is coupled to transcription through an interaction with yeast mitochondrial RNA polymerase
    • Rodeheffer,M.S., Boone,B.E., Bryan,A.C. and Shadel,G.S. (2001) Nam1p, a protein involved in RNA processing and translation, is coupled to transcription through an interaction with yeast mitochondrial RNA polymerase. J. Biol. Chem., 276, 8616-8622.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8616-8622
    • Rodeheffer, M.S.1    Boone, B.E.2    Bryan, A.C.3    Shadel, G.S.4
  • 27
    • 0033529190 scopus 로고    scopus 로고
    • Stability of the mitochondrial genome requires an amino-terminal domain of yeast mitochondrial RNA polymerase
    • Wang,Y. and Shadel,G.S. (1999) Stability of the mitochondrial genome requires an amino-terminal domain of yeast mitochondrial RNA polymerase. Proc. Natl Acad. Sci. USA, 96, 8046-8051.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8046-8051
    • Wang, Y.1    Shadel, G.S.2
  • 28
    • 34250376484 scopus 로고    scopus 로고
    • Human mitochondrial ribosomal protein MRPL12 interacts directly with mitochondrial RNA polymerase to modulate mitochondrial gene expression
    • Wang,Z., Cotney,J. and Shadel,G.S. (2007) Human mitochondrial ribosomal protein MRPL12 interacts directly with mitochondrial RNA polymerase to modulate mitochondrial gene expression. J. Biol. Chem., 282, 12610-12618.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12610-12618
    • Wang, Z.1    Cotney, J.2    Shadel, G.S.3
  • 29
    • 41249098355 scopus 로고    scopus 로고
    • The layered structure of human mitochondrial DNA nucleoids
    • Bogenhagen,D.F., Rousseau,D. and Burke,S. (2008) The layered structure of human mitochondrial DNA nucleoids. J. Biol. Chem., 283, 3665-3675.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3665-3675
    • Bogenhagen, D.F.1    Rousseau, D.2    Burke, S.3
  • 31
    • 33748746678 scopus 로고    scopus 로고
    • Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane
    • Wang,Y. and Bogenhagen,D.F. (2006) Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane. J. Biol. Chem., 281, 25791-25802.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25791-25802
    • Wang, Y.1    Bogenhagen, D.F.2
  • 32
    • 33745757322 scopus 로고    scopus 로고
    • Era and RbfA have overlapping function in ribosome biogenesis in Escherichia coli
    • Inoue,K., Chen,J., Tan,Q. and Inouye,M. (2006) Era and RbfA have overlapping function in ribosome biogenesis in Escherichia coli. J. Mol. Microbiol. Biotechnol., 11, 41-52.
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 41-52
    • Inoue, K.1    Chen, J.2    Tan, Q.3    Inouye, M.4
  • 34
    • 56049087303 scopus 로고    scopus 로고
    • The A3243G tRNALeu(UUR) MELAS mutation causes amino acid misincorporation and a combined respiratory chain assembly defect partially suppressed by overexpression of EFTu and EFG2
    • Sasarman,F., Antonicka,H. and Shoubridge,E.A. (2008) The A3243G tRNALeu(UUR) MELAS mutation causes amino acid misincorporation and a combined respiratory chain assembly defect partially suppressed by overexpression of EFTu and EFG2. Hum. Mol. Genet., 17, 3697-3707.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3697-3707
    • Sasarman, F.1    Antonicka, H.2    Shoubridge, E.A.3
  • 36
    • 33845970551 scopus 로고    scopus 로고
    • Mammalian dap3 is an essential gene required for mitochondrial homeostasis in vivo and contributing to the extrinsic pathway for apoptosis
    • Kim,H.R., Chae,H.J., Thomas,M., Miyazaki,T., Monosov,A., Monosov,E., Krajewska,M., Krajewski,S. and Reed,J.C. (2007) Mammalian dap3 is an essential gene required for mitochondrial homeostasis in vivo and contributing to the extrinsic pathway for apoptosis. FASEB J., 21, 188-196.
    • (2007) FASEB J. , vol.21 , pp. 188-196
    • Kim, H.R.1    Chae, H.J.2    Thomas, M.3    Miyazaki, T.4    Monosov, A.5    Monosov, E.6    Krajewska, M.7    Krajewski, S.8    Reed, J.C.9
  • 38
    • 4344716374 scopus 로고    scopus 로고
    • Death-associated protein 3 localizes to the mitochondria and is involved in the process of mitochondrial fragmentation during cell death
    • Mukamel,Z. and Kimchi,A. (2004) Death-associated protein 3 localizes to the mitochondria and is involved in the process of mitochondrial fragmentation during cell death. J. Biol. Chem., 279, 36732-36738.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36732-36738
    • Mukamel, Z.1    Kimchi, A.2
  • 39
    • 64149088232 scopus 로고    scopus 로고
    • hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis
    • Tang,T., Zheng,B., Chen,S.H., Murphy,A.N., Kudlicka,K., Zhou,H. and Farquhar,M.G. (2009) hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis. J. Biol. Chem., 284, 5414-5424.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5414-5424
    • Tang, T.1    Zheng, B.2    Chen, S.H.3    Murphy, A.N.4    Kudlicka, K.5    Zhou, H.6    Farquhar, M.G.7
  • 41
    • 23644454808 scopus 로고    scopus 로고
    • Nuclear MRP genes and mitochondrial disease
    • O'Brien,T.W., O'Brien,B.J. and Norman,R.A. (2005) Nuclear MRP genes and mitochondrial disease. Gene, 354, 147-151.
    • (2005) Gene , vol.354 , pp. 147-151
    • O'Brien, T.W.1    O'Brien, B.J.2    Norman, R.A.3
  • 43
    • 0032125744 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Pet309 protein is embedded in the mitochondrial inner membrane
    • Manthey,G.M., Przybyla-Zawislak,B.D. and McEwen,J.E. (1998) The Saccharomyces cerevisiae Pet309 protein is embedded in the mitochondrial inner membrane. Eur. J. Biochem., 255, 156-161.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 156-161
    • Manthey, G.M.1    Przybyla-Zawislak, B.D.2    McEwen, J.E.3
  • 45
    • 37749036789 scopus 로고    scopus 로고
    • Pentatricopeptide repeat (PPR) proteins as sequence-specificity factors in post-transcriptional processes in organelles
    • Delannoy,E., Stanley,W.A., Bond,C.S. and Small,I.D. (2007) Pentatricopeptide repeat (PPR) proteins as sequence-specificity factors in post-transcriptional processes in organelles. Biochem. Soc. Trans., 35, 1643-1647.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1643-1647
    • Delannoy, E.1    Stanley, W.A.2    Bond, C.S.3    Small, I.D.4
  • 47
    • 4344595430 scopus 로고    scopus 로고
    • The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene in cytochrome oxidase assembly: mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA
    • Xu,F., Morin,C., Mitchell,G., Ackerley,C. and Robinson,B.H. (2004) The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene in cytochrome oxidase assembly: mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA. Biochem. J., 382, 331-336.
    • (2004) Biochem. J. , vol.382 , pp. 331-336
    • Xu, F.1    Morin, C.2    Mitchell, G.3    Ackerley, C.4    Robinson, B.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.