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Volumn 11, Issue 3, 2015, Pages

Mutation in MRPS34 Compromises Protein Synthesis and Causes Mitochondrial Dysfunction

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; MITOCHONDRIAL PROTEIN; MITOCHONDRIAL RIBOSOMAL PROTEIN OF THE SMALL SUBUNIT 34; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RNA 12S; SUCCINATE DEHYDROGENASE (UBIQUINONE); UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG; MITOCHONDRIAL DNA; MRPS34 PROTEIN, HUMAN; MRPS34 PROTEIN, MOUSE; RIBOSOME PROTEIN; RIBOSOME RNA; RNA, RIBOSOMAL, 12S;

EID: 84926377210     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1005089     Document Type: Article
Times cited : (39)

References (42)
  • 1
    • 0019444843 scopus 로고
    • tRNA punctuation model of RNA processing in human mitochondria
    • Ojala D, Montoya J, Attardi G, (1981) tRNA punctuation model of RNA processing in human mitochondria. Nature 290: 470–474. 7219536
    • (1981) Nature , vol.290 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 2
    • 84869051280 scopus 로고    scopus 로고
    • Mitochondrial disorders as windows into an ancient organelle
    • Vafai SB, Mootha VK, (2012) Mitochondrial disorders as windows into an ancient organelle. Nature 491: 374–383. doi: 10.1038/nature11707 23151580
    • (2012) Nature , vol.491 , pp. 374-383
    • Vafai, S.B.1    Mootha, V.K.2
  • 3
    • 84892756479 scopus 로고    scopus 로고
    • Mitochondria: Impaired mitochondrial translation in human disease
    • Boczonadi V, Horvath R, (2014) Mitochondria: Impaired mitochondrial translation in human disease. Int J Biochem Cell Biol 48: 77–84. doi: 10.1016/j.biocel.2013.12.011 24412566
    • (2014) Int J Biochem Cell Biol , vol.48 , pp. 77-84
    • Boczonadi, V.1    Horvath, R.2
  • 4
    • 0141953259 scopus 로고    scopus 로고
    • Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins
    • Sharma M, Koc E, Datta P, Booth T, Spremulli L, et al. (2003) Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins. Cell 115: 97–108. 14532006
    • (2003) Cell , vol.115 , pp. 97-108
    • Sharma, M.1    Koc, E.2    Datta, P.3    Booth, T.4    Spremulli, L.5
  • 5
    • 0035980117 scopus 로고    scopus 로고
    • Proteomic Analysis of the Mammalian Mitochondrial Ribosome. Identification of protein components in the 28 S small subunit
    • Suzuki T, (2001) Proteomic Analysis of the Mammalian Mitochondrial Ribosome. Identification of protein components in the 28 S small subunit. J Biol Chem 276: 33181–33195. doi: 10.1074/jbc.M103236200 11402041
    • (2001) J Biol Chem , vol.276 , pp. 33181-33195
    • Suzuki, T.1
  • 7
    • 84892797558 scopus 로고    scopus 로고
    • Greber BJ, Boehringer D, Leitner A, Bieri P, Voigts-Hoffmann F, et al. (2013) Architecture of the large subunit of the mammalian mitochondrial ribosome. Nature: 1–17. doi: 10.1038/nature12890
  • 9
    • 0141953259 scopus 로고    scopus 로고
    • Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins
    • Sharma M, Koc E, Datta P, Booth T, Spremulli L, et al. (2003) Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins. Cell 115: 97–108. 14532006
    • (2003) Cell , vol.115 , pp. 97-108
    • Sharma, M.1    Koc, E.2    Datta, P.3    Booth, T.4    Spremulli, L.5
  • 10
    • 84909594483 scopus 로고    scopus 로고
    • Structure of the large ribosomal subunit from human mitochondria
    • Brown A, Amunts A, Bai X-C, Sugimoto Y, Edwards PC, et al. (2014) Structure of the large ribosomal subunit from human mitochondria. Science 346: 718–722. doi: 10.1126/science.1258026 25278503
    • (2014) Science , vol.346 , pp. 718-722
    • Brown, A.1    Amunts, A.2    Bai, X.-C.3    Sugimoto, Y.4    Edwards, P.C.5
  • 11
    • 0035877697 scopus 로고    scopus 로고
    • Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria
    • Suzuki T, Terasaki M, Takemoto-Hori C, Hanada T, Ueda T, et al. (2001) Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria. J Biol Chem 276: 21724–21736. doi: 10.1074/jbc.M100432200 M100432200 [pii]. 11279069
    • (2001) J Biol Chem , vol.276 , pp. 21724-21736
    • Suzuki, T.1    Terasaki, M.2    Takemoto-Hori, C.3    Hanada, T.4    Ueda, T.5
  • 12
    • 84870392446 scopus 로고    scopus 로고
    • Structural aspects of mitochondrial translational apparatus
    • Agrawal RK, Sharma MR, (2012) Structural aspects of mitochondrial translational apparatus. Curr Opin Struct Biol 22: 797–803. doi: 10.1016/j.sbi.2012.08.003 22959417
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 797-803
    • Agrawal, R.K.1    Sharma, M.R.2
  • 13
    • 33646138730 scopus 로고    scopus 로고
    • Mba1, a membrane-associated ribosome receptor in mitochondria
    • Ott MM, Prestele MM, Bauerschmitt HH, Funes SS, Bonnefoy NN, et al. (2006) Mba1, a membrane-associated ribosome receptor in mitochondria. EMBO J 25: 1603–1610. doi: 10.1038/sj.emboj.7601070 16601683
    • (2006) EMBO J , vol.25 , pp. 1603-1610
    • Ott, M.M.1    Prestele, M.M.2    Bauerschmitt, H.H.3    Funes, S.S.4    Bonnefoy, N.N.5
  • 14
    • 0035380711 scopus 로고    scopus 로고
    • The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present
    • Koc EC, Burkhart W, Blackburn K, Moseley A, Spremulli LL, (2001) The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present. J Biochem 276: 19363–19374. Available: http://www.jbc.org/cgi/doi/10.1074/jbc.M100727200. 11279123
    • (2001) J Biochem , vol.276 , pp. 19363-19374
    • Koc, E.C.1    Burkhart, W.2    Blackburn, K.3    Moseley, A.4    Spremulli, L.L.5
  • 15
    • 0037029122 scopus 로고    scopus 로고
    • Evolution of a protein-rich mitochondrial ribosome: implications for human genetic disease
    • O'brien TW, (2002) Evolution of a protein-rich mitochondrial ribosome: implications for human genetic disease. Gene 286: 73–79. doi: 10.1016/S0378-1119(01)00808-3 11943462
    • (2002) Gene , vol.286 , pp. 73-79
    • O'brien, T.W.1
  • 16
    • 0037449940 scopus 로고    scopus 로고
    • Binding of the human homolog of the Drosophila discs large tumor suppressor protein to the mitochondrial ribosomal protein MRP-S34
    • Ogawa F, Adachi S, Kohu K, Shige K, Akiyama T, (2003) Binding of the human homolog of the Drosophila discs large tumor suppressor protein to the mitochondrial ribosomal protein MRP-S34. Biochem Biophys Res Commun 300: 789–792. doi: 10.1016/S0006-291X(02)02887-5 12507520
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 789-792
    • Ogawa, F.1    Adachi, S.2    Kohu, K.3    Shige, K.4    Akiyama, T.5
  • 17
    • 84864232091 scopus 로고    scopus 로고
    • Massively parallel sequencing of the mouse exome to accurately identify rare, induced mutations: an immediate source for thousands of new mouse models
    • Andrews TD, Whittle B, Field MA, Balakishnan B, Zhang Y, et al. (2012) Massively parallel sequencing of the mouse exome to accurately identify rare, induced mutations: an immediate source for thousands of new mouse models. Open Biol 2: 120061. doi: 10.1098/rsob.120061 22724066
    • (2012) Open Biol , vol.2 , pp. 120061
    • Andrews, T.D.1    Whittle, B.2    Field, M.A.3    Balakishnan, B.4    Zhang, Y.5
  • 18
    • 84874934557 scopus 로고    scopus 로고
    • Whole-exome sequencing identifies a mutation in the mitochondrial ribosome protein MRPL44 to underlie mitochondrial infantile cardiomyopathy
    • Carroll CJ, Isohanni P, Poyhonen R, Euro L, Richter U, et al. (2013) Whole-exome sequencing identifies a mutation in the mitochondrial ribosome protein MRPL44 to underlie mitochondrial infantile cardiomyopathy. J Med Genet 50: 151–159. doi: 10.1136/jmedgenet-2012-101375 23315540
    • (2013) J Med Genet , vol.50 , pp. 151-159
    • Carroll, C.J.1    Isohanni, P.2    Poyhonen, R.3    Euro, L.4    Richter, U.5
  • 19
    • 37249071299 scopus 로고    scopus 로고
    • Antenatal mitochondrial disease caused by mitochondrial ribosomal protein (MRPS22) mutation
    • Saada A, Shaag A, Arnon S, Dolfin T, Miller C, et al. (2007) Antenatal mitochondrial disease caused by mitochondrial ribosomal protein (MRPS22) mutation. J Med Genet 44: 784–786. doi: 10.1136/jmg.2007.053116 17873122
    • (2007) J Med Genet , vol.44 , pp. 784-786
    • Saada, A.1    Shaag, A.2    Arnon, S.3    Dolfin, T.4    Miller, C.5
  • 20
    • 77957661299 scopus 로고    scopus 로고
    • Interleukin-6-deficient mice develop hepatic inflammation and systemic insulin resistance
    • Matthews VB, Allen TL, Risis S, Chan MHS, Henstridge DC, et al. (2010) Interleukin-6-deficient mice develop hepatic inflammation and systemic insulin resistance. Diabetologia 53: 2431–2441. doi: 10.1007/s00125-010-1865-y 20697689
    • (2010) Diabetologia , vol.53 , pp. 2431-2441
    • Matthews, V.B.1    Allen, T.L.2    Risis, S.3    Chan, M.H.S.4    Henstridge, D.C.5
  • 21
    • 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 LL, 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. doi: 10.1016/j.mito.2008.04.004 18539099
    • (2008) Mitochondrion , vol.8 , pp. 254-261
    • Emdadul, H.M.1    Grasso, D.2    Miller, C.3    Spremulli, L.L.4    Saada, A.5
  • 22
    • 67349234111 scopus 로고    scopus 로고
    • Pentatricopeptide repeat domain protein 3 associates with the mitochondrial small ribosomal subunit and regulates translation
    • Davies SMK, Rackham O, Shearwood A-MJ, Hamilton KL, Narsai R, et al. (2009) Pentatricopeptide repeat domain protein 3 associates with the mitochondrial small ribosomal subunit and regulates translation. FEBS Letts 583: 1853–1858. doi: 10.1016/j.febslet.2009.04.048 19427859
    • (2009) FEBS Letts , vol.583 , pp. 1853-1858
    • Davies, S.M.K.1    Rackham, O.2    Shearwood, A.-M.J.3    Hamilton, K.L.4    Narsai, R.5
  • 23
    • 84857192195 scopus 로고    scopus 로고
    • LRPPRC is necessary for polyadenylation and coordination of translation of mitochondrial mRNAs
    • Ruzzenente B, Metodiev MD, Wredenberg A, Bratic A, Park CB, et al. (2011) LRPPRC is necessary for polyadenylation and coordination of translation of mitochondrial mRNAs. EMBO J 31: 443–456. doi: 10.1038/emboj.2011.392 22045337
    • (2011) EMBO J , vol.31 , pp. 443-456
    • Ruzzenente, B.1    Metodiev, M.D.2    Wredenberg, A.3    Bratic, A.4    Park, C.B.5
  • 24
    • 84887624341 scopus 로고    scopus 로고
    • Organelle transcriptomes: products of a deconstructed genome
    • Small ID, Rackham O, Filipovska A, (2013) Organelle transcriptomes: products of a deconstructed genome. Curr Opin Microbiol 16: 652–658. doi: 10.1016/j.mib.2013.07.011 23932204
    • (2013) Curr Opin Microbiol , vol.16 , pp. 652-658
    • Small, I.D.1    Rackham, O.2    Filipovska, A.3
  • 25
    • 0034674626 scopus 로고    scopus 로고
    • Mammalian Mitochondrial Ribosomal Proteins (4). Amino acid sequencing, characterization, and identification of corresponding gene sequences
    • O'Brien TW, (2000) Mammalian Mitochondrial Ribosomal Proteins (4). Amino acid sequencing, characterization, and identification of corresponding gene sequences. J Biol Chem 275: 18153–18159. doi: 10.1074/jbc.M909762199 10751423
    • (2000) J Biol Chem , vol.275 , pp. 18153-18159
    • O'Brien, T.W.1
  • 26
    • 0016659588 scopus 로고
    • Regulation of ribosomal protein synthesis in Escherichia coli B/r
    • Dennis PP, Young RF, (1975) Regulation of ribosomal protein synthesis in Escherichia coli B/r. J Bacteriol 121: 994–999. 1090612
    • (1975) J Bacteriol , vol.121 , pp. 994-999
    • Dennis, P.P.1    Young, R.F.2
  • 27
    • 77955082781 scopus 로고    scopus 로고
    • Mutations in C12orf65 in patients with encephalomyopathy and a mitochondrial translation defect
    • Antonicka H, Ostergaard E, Sasarman F, Weraarpachai W, Wibrand F, et al. (2010) Mutations in C12orf65 in patients with encephalomyopathy and a mitochondrial translation defect. Am J Hum Genet 87: 115–122. S0002-9297(10)00307-1 [pii] doi: 10.1016/j.ajhg.2010.06.004 20598281
    • (2010) Am J Hum Genet , vol.87 , pp. 115-122
    • Antonicka, H.1    Ostergaard, E.2    Sasarman, F.3    Weraarpachai, W.4    Wibrand, F.5
  • 28
    • 84867252179 scopus 로고    scopus 로고
    • An RMND1 Mutation Causes Encephalopathy Associated with Multiple Oxidative Phosphorylation Complex Deficiencies and a Mitochondrial Translation Defect
    • Janer A, Antonicka H, Lalonde E, Nishimura T, Sasarman F, et al. (2012) An RMND1 Mutation Causes Encephalopathy Associated with Multiple Oxidative Phosphorylation Complex Deficiencies and a Mitochondrial Translation Defect. Am J Hum Genet 91: 737–743. doi: 10.1016/j.ajhg.2012.08.020 23022098
    • (2012) Am J Hum Genet , vol.91 , pp. 737-743
    • Janer, A.1    Antonicka, H.2    Lalonde, E.3    Nishimura, T.4    Sasarman, F.5
  • 29
    • 84895774463 scopus 로고    scopus 로고
    • Tissue-specific loss of DARS2 activates stress responses independently of respiratory chain deficiency in the heart
    • Dogan SA, Pujol C, Maiti P, Kukat A, Wang S, et al. (2014) Tissue-specific loss of DARS2 activates stress responses independently of respiratory chain deficiency in the heart. Cell Metab 19: 458–469. doi: 10.1016/j.cmet.2014.02.004 24606902
    • (2014) Cell Metab , vol.19 , pp. 458-469
    • Dogan, S.A.1    Pujol, C.2    Maiti, P.3    Kukat, A.4    Wang, S.5
  • 30
    • 80052007901 scopus 로고    scopus 로고
    • The Human Mitochondrial Transcriptome
    • Mercer TR, Neph S, Dinger ME, Crawford J, Smith MA, et al. (2011) The Human Mitochondrial Transcriptome. Cell 146: 645–658. doi: 10.1016/j.cell.2011.06.051 21854988
    • (2011) Cell , vol.146 , pp. 645-658
    • Mercer, T.R.1    Neph, S.2    Dinger, M.E.3    Crawford, J.4    Smith, M.A.5
  • 31
    • 21044441973 scopus 로고    scopus 로고
    • Mitochondrial myopathy, sideroblastic anemia, and lactic acidosis: an autosomal recessive syndrome in Persian Jews caused by a mutation in the PUS1 gene
    • Zeharia A, Fischel-Ghodsian N, Casas K, Bykhocskaya Y, Tamari H, et al. (2005) Mitochondrial myopathy, sideroblastic anemia, and lactic acidosis: an autosomal recessive syndrome in Persian Jews caused by a mutation in the PUS1 gene. J Child Neurol 20: 449–452. 15971356
    • (2005) J Child Neurol , vol.20 , pp. 449-452
    • Zeharia, A.1    Fischel-Ghodsian, N.2    Casas, K.3    Bykhocskaya, Y.4    Tamari, H.5
  • 32
    • 79955799806 scopus 로고    scopus 로고
    • Acute liver failure with subsequent cirrhosis as the primary manifestation of TRMU mutations
    • Schara U, Kleist-Retzow von J-C, Lainka E, Gerner P, Pyle A, et al. (2011) Acute liver failure with subsequent cirrhosis as the primary manifestation of TRMU mutations. J Inherit Metab Dis 34: 197–201. doi: 10.1007/s10545-010-9250-z 21153446
    • (2011) J Inherit Metab Dis , vol.34 , pp. 197-201
    • Schara, U.1    Kleist-Retzow von, J.-C.2    Lainka, E.3    Gerner, P.4    Pyle, A.5
  • 33
    • 81255169321 scopus 로고    scopus 로고
    • The 2-thiouridylase function of the human MTU1 (TRMU) enzyme is dispensable for mitochondrial translation
    • Sasarman F, Antonicka H, Horvath R, Shoubridge EA, (2011) The 2-thiouridylase function of the human MTU1 (TRMU) enzyme is dispensable for mitochondrial translation. Hum Mol Genet 20: 4634–4643. doi: 10.1093/hmg/ddr397 21890497
    • (2011) Hum Mol Genet , vol.20 , pp. 4634-4643
    • Sasarman, F.1    Antonicka, H.2    Horvath, R.3    Shoubridge, E.A.4
  • 34
    • 34250302680 scopus 로고    scopus 로고
    • Mitochondrial hepatopathies: advances in genetics and pathogenesis
    • Lee WS, Sokol RJ, (2007) Mitochondrial hepatopathies: advances in genetics and pathogenesis. Hepatology 45: 1555–1565. doi: 10.1002/hep.21710 17538929
    • (2007) Hepatology , vol.45 , pp. 1555-1565
    • Lee, W.S.1    Sokol, R.J.2
  • 35
    • 78650483039 scopus 로고    scopus 로고
    • Inventory control: cytochrome c oxidase assembly regulates mitochondrial translation
    • Mick DU, Fox TD, Rehling P, (2011) Inventory control: cytochrome c oxidase assembly regulates mitochondrial translation. Nat Rev Mol Cell Biol 12: 14–20. doi: 10.1038/nrm3029 21179059
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 14-20
    • Mick, D.U.1    Fox, T.D.2    Rehling, P.3
  • 36
    • 71749091518 scopus 로고    scopus 로고
    • Pentatricopeptide repeat domain protein 1 lowers the levels of mitochondrial leucine tRNAs in cells
    • Rackham O, Davies SMK, Shearwood A-MJ, Hamilton KL, Whelan J, et al. (2009) Pentatricopeptide repeat domain protein 1 lowers the levels of mitochondrial leucine tRNAs in cells. Nucleic Acids Res 37: 5859–5867. doi: 10.1093/nar/gkp627 19651879
    • (2009) Nucleic Acids Res , vol.37 , pp. 5859-5867
    • Rackham, O.1    Davies, S.M.K.2    Shearwood, A.-M.J.3    Hamilton, K.L.4    Whelan, J.5
  • 37
  • 38
    • 0035879703 scopus 로고    scopus 로고
    • Measurements of protein carbonyls, ortho- and meta-tyrosine and oxidative phosphorylation complex activity in mitochondria from young and old rats
    • Davies SMS, Poljak AA, Duncan MWM, Smythe GAG, Murphy MPM, (2001) Measurements of protein carbonyls, ortho- and meta-tyrosine and oxidative phosphorylation complex activity in mitochondria from young and old rats. Free Rad Biol Med 31: 181–190. doi: 10.1016/S0891-5849(01)00576-7 11440830
    • (2001) Free Rad Biol Med , vol.31 , pp. 181-190
    • Davies, S.M.S.1    Poljak, A.A.2    Duncan, M.W.M.3    Smythe, G.A.G.4    Murphy, M.P.M.5
  • 39
    • 84879336390 scopus 로고    scopus 로고
    • Imaging of neutral lipids by oil red O for analyzing the metabolic status in health and disease
    • Mehlem A, Hagberg CE, Muhl L, Eriksson U, Falkevall A, (2013) Imaging of neutral lipids by oil red O for analyzing the metabolic status in health and disease. Nat Protoc 8: 1149–1154. doi: 10.1038/nprot.2013.055 23702831
    • (2013) Nat Protoc , vol.8 , pp. 1149-1154
    • Mehlem, A.1    Hagberg, C.E.2    Muhl, L.3    Eriksson, U.4    Falkevall, A.5
  • 40
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros M, Vincens P, (1996) Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 241: 779–786. 8944766
    • (1996) Eur J Biochem , vol.241 , pp. 779-786
    • Claros, M.1    Vincens, P.2
  • 41
    • 84883577718 scopus 로고    scopus 로고
    • Analysis Tool Web Services from the EMBL-EBI
    • McWilliam H, Li W, Uludag M, Squizzato S, Park YM, et al. (2013) Analysis Tool Web Services from the EMBL-EBI. Nucleic Acids Res 41: W597–W600. Available: http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=23671338&retmode=ref&cmd=prlinks. doi: 10.1093/nar/gkt376 23671338
    • (2013) Nucleic Acids Res , vol.41 , pp. 597-600
    • McWilliam, H.1    Li, W.2    Uludag, M.3    Squizzato, S.4    Park, Y.M.5
  • 42
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT, (1999) Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292: 195–202. doi: 10.1006/jmbi.1999.3091 10493868
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1


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