메뉴 건너뛰기




Volumn 18, Issue 2, 2013, Pages 129-138

BOLA1 is an aerobic protein that prevents mitochondrial morphology changes induced by glutathione depletion

Author keywords

[No Author keywords available]

Indexed keywords

BOLA1 PROTEIN; BUTHIONINE SULFOXIMINE; GLUTAREDOXIN; GLUTAREDOXIN GLRX5; GLUTATHIONE; MITOCHONDRIAL PROTEIN; S NITROSOCYSTEINE; THIOL; UNCLASSIFIED DRUG;

EID: 84870520180     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4253     Document Type: Article
Times cited : (44)

References (43)
  • 1
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • Abascal F, Zardoya R, and Posada D. ProtTest: selection of best-fit models of protein evolution. Bioinformatics 21: 2104-2105, 2005.
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 2
    • 0024110635 scopus 로고
    • Identification, cloning, and expression of bolA, an ftsZ-dependent morphogene of Escherichia coli
    • Aldea M, Hernandez-Chico C, de la Campa AG, Kushner SR, and Vicente M. Identification, cloning, and expression of bolA, an ftsZ-dependent morphogene of Escherichia coli. J Bacteriol 170: 5169-5176, 1988.
    • (1988) J Bacteriol , vol.170 , pp. 5169-5176
    • Aldea, M.1    Hernandez-Chico, C.2    De La Campa, A.G.3    Kushner, S.R.4    Vicente, M.5
  • 3
    • 0032829681 scopus 로고    scopus 로고
    • Influence of nitric oxide on the intracellular reduced gluta-thione pool: Different cellular capacities and strategies to encounter nitric oxide-mediated stress
    • Berendji D, Kolb-Bachofen V, Meyer KL, and Kroncke KD. Influence of nitric oxide on the intracellular reduced gluta-thione pool: different cellular capacities and strategies to encounter nitric oxide-mediated stress. Free Radic Biol Med 27: 773-780, 1999.
    • (1999) Free Radic Biol Med , vol.27 , pp. 773-780
    • Berendji, D.1    Kolb-Bachofen, V.2    Meyer, K.L.3    Kroncke, K.D.4
  • 4
    • 67149128101 scopus 로고    scopus 로고
    • Gene expression in peripheral blood leukocytes in monozygotic twins discordant for chronic fatigue: No evidence of a biomarker
    • Byrnes A, Jacks A, Dahlman-Wright K, Evengard B, Wright FA, Pedersen NL, and Sullivan PF. Gene expression in peripheral blood leukocytes in monozygotic twins discordant for chronic fatigue: no evidence of a biomarker. PLoS One 4: e5805, 2009.
    • (2009) PLoS One , vol.4
    • Byrnes, A.1    Jacks, A.2    Dahlman-Wright, K.3    Evengard, B.4    Wright, F.A.5    Pedersen, N.L.6    Sullivan, P.F.7
  • 6
    • 80053898097 scopus 로고    scopus 로고
    • Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes
    • Cameron JM, Janer A, Levandovskiy V, Mackay N, Rouault TA, Tong WH, Ogilvie I, Shoubridge EA, and Robinson BH. Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes. Am J Hum Genet 89: 486-495, 2011.
    • (2011) Am J Hum Genet , vol.89 , pp. 486-495
    • Cameron, J.M.1    Janer, A.2    Levandovskiy, V.3    MacKay, N.4    Rouault, T.A.5    Tong, W.H.6    Ogilvie, I.7    Shoubridge, E.A.8    Robinson, B.H.9
  • 7
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho DH, Nakamura T, Fang J, Cieplak P, Godzik A, Gu Z, and Lipton SA. S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 324: 102-105, 2009.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 8
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros MG and Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 241: 779-786, 1996.
    • (1996) Eur J Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 9
    • 67650999518 scopus 로고    scopus 로고
    • Evolution and diversity of glutaredoxins in photosynthetic organisms
    • Couturier J, Jacquot JP, and Rouhier N. Evolution and diversity of glutaredoxins in photosynthetic organisms. Cell Mol Life Sci 66: 2539-2557, 2009.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2539-2557
    • Couturier, J.1    Jacquot, J.P.2    Rouhier, N.3
  • 10
    • 0042266921 scopus 로고    scopus 로고
    • Reconstruction of the proto-mitochondrial metabolism
    • Gabaldon T and Huynen MA. Reconstruction of the proto-mitochondrial metabolism. Science 301: 609, 2003.
    • (2003) Science , vol.301 , pp. 609
    • Gabaldon, T.1    Huynen, M.A.2
  • 11
    • 0345600247 scopus 로고    scopus 로고
    • A protein interaction map of Drosophila mela-nogaster
    • Giot L, et al. A protein interaction map of Drosophila mela-nogaster. Science 302: 1727-1736, 2003.
    • (2003) Science , vol.302 , pp. 1727-1736
    • Giot, L.1
  • 12
    • 25444456661 scopus 로고    scopus 로고
    • Gene expression profiling in the chronic fatigue syndrome
    • Grans H, Nilsson P, and Evengard B. Gene expression profiling in the chronic fatigue syndrome. J Intern Med 258: 388-390, 2005.
    • (2005) J Intern Med , vol.258 , pp. 388-390
    • Grans, H.1    Nilsson, P.2    Evengard, B.3
  • 14
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y, et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415: 180-183, 2002.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1
  • 15
    • 44449163314 scopus 로고    scopus 로고
    • NDUFA2 complex i mutation leads to Leigh disease
    • Hoefs SJ, et al. NDUFA2 complex I mutation leads to Leigh disease. Am J Hum Genet 82: 1306-1315, 2008.
    • (2008) Am J Hum Genet , vol.82 , pp. 1306-1315
    • Hoefs, S.J.1
  • 16
    • 12744251555 scopus 로고    scopus 로고
    • Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin
    • Huynen MA, Spronk CA, Gabaldon T, and Snel B. Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin. FEBS Lett 579: 591-596, 2005.
    • (2005) FEBS Lett , vol.579 , pp. 591-596
    • Huynen, M.A.1    Spronk, C.A.2    Gabaldon, T.3    Snel, B.4
  • 17
    • 0033974688 scopus 로고    scopus 로고
    • Toward a protein-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins
    • Ito T, Tashiro K, Muta S, Ozawa R, Chiba T, Nishi-zawa M, Yamamoto K, Kuhara S, and Sakaki Y. Toward a protein-protein interaction map of the budding yeast: a comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins. Proc Natl Acad Sci USA 97: 1143-1147, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1143-1147
    • Ito, T.1    Tashiro, K.2    Muta, S.3    Ozawa, R.4    Chiba, T.5    Nishi-Zawa, M.6    Yamamoto, K.7    Kuhara, S.8    Sakaki, Y.9
  • 18
    • 78651265091 scopus 로고    scopus 로고
    • The crystal structure of human GLRX5: Iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity
    • Johansson C, et al. The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity. Biochem J 433: 303-311, 2010.
    • (2010) Biochem J , vol.433 , pp. 303-311
    • Johansson, C.1
  • 19
    • 76349122676 scopus 로고    scopus 로고
    • Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast
    • Kim KD, Chung WH, Kim HJ, Lee KC, and Roe JH. Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast. Biochem Biophys Res Commun 392: 467-472, 2010.
    • (2010) Biochem Biophys Res Commun , vol.392 , pp. 467-472
    • Kim, K.D.1    Chung, W.H.2    Kim, H.J.3    Lee, K.C.4    Roe, J.H.5
  • 20
    • 56249140087 scopus 로고    scopus 로고
    • Computer-assisted live cell analysis of mito-chondrial membrane potential, morphology and calcium handling
    • Koopman WJ, Distelmaier F, Esseling JJ, Smeitink JA, and Willems PH. Computer-assisted live cell analysis of mito-chondrial membrane potential, morphology and calcium handling. Methods 46: 304-311, 2008.
    • (2008) Methods , vol.46 , pp. 304-311
    • Koopman, W.J.1    Distelmaier, F.2    Esseling, J.J.3    Smeitink, J.A.4    Willems, P.H.5
  • 22
    • 25444446126 scopus 로고    scopus 로고
    • Mitochondrial network complexity and pathological decrease in complex i activity are tightly correlated in isolated human complex i deficiency
    • Koopman WJ, Visch HJ, Verkaart S, van den Heuvel LW, Smeitink JA, and Willems PH. Mitochondrial network complexity and pathological decrease in complex I activity are tightly correlated in isolated human complex I deficiency. Am J Physiol Cell Physiol 289: C881-C890, 2005.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Koopman, W.J.1    Visch, H.J.2    Verkaart, S.3    Van Den Heuvel, L.W.4    Smeitink, J.A.5    Willems, P.H.6
  • 23
    • 44849098197 scopus 로고    scopus 로고
    • Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis
    • Kumanovics A, et al. Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis. J Biol Chem 283: 10276-10286, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 10276-10286
    • Kumanovics, A.1
  • 24
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • Larkin MA, et al. Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947-2948, 2007.
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 25
    • 78650949287 scopus 로고    scopus 로고
    • Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast
    • Li H, Mapolelo DT, Dingra NN, Keller G, Riggs-Gelasco PJ, Winge DR, Johnson MK, and Outten CE. Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast. J Biol Chem 286: 867-876, 2010.
    • (2010) J Biol Chem , vol.286 , pp. 867-876
    • Li, H.1    Mapolelo, D.T.2    Dingra, N.N.3    Keller, G.4    Riggs-Gelasco, P.J.5    Winge, D.R.6    Johnson, M.K.7    Outten, C.E.8
  • 26
    • 63449137389 scopus 로고    scopus 로고
    • Glutaredoxin 5 regulates osteoblast apoptosis by protecting against oxidative stress
    • Linares GR, Xing W, Govoni KE, Chen ST, and Mohan S. Glutaredoxin 5 regulates osteoblast apoptosis by protecting against oxidative stress. Bone 44: 795-804, 2009.
    • (2009) Bone , vol.44 , pp. 795-804
    • Linares, G.R.1    Xing, W.2    Govoni, K.E.3    Chen, S.T.4    Mohan, S.5
  • 27
    • 36349007756 scopus 로고    scopus 로고
    • Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer
    • Meyer AJ, Brach T, Marty L, Kreye S, Rouhier N, Jacquot JP, and Hell R Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer. Plant J 52: 973-986, 2007.
    • (2007) Plant J , vol.52 , pp. 973-986
    • Meyer, A.J.1    Brach, T.2    Marty, L.3    Kreye, S.4    Rouhier, N.5    Jacquot, J.P.6    Hell, R.7
  • 29
    • 46349103594 scopus 로고    scopus 로고
    • A mitochondrial protein compendium elucidates complex i disease biology
    • Pagliarini DJ, et al. A mitochondrial protein compendium elucidates complex I disease biology. Cell 134: 112-123,2008.
    • (2008) Cell , vol.134 , pp. 112-123
    • Pagliarini, D.J.1
  • 30
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque MT, Tamarit J, Belli G, Ros J, and Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell 13: 1109-1121, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 31
    • 0033009562 scopus 로고    scopus 로고
    • The stationary-phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth
    • Santos JM, Freire P, Vicente M, and Arraiano CM. The stationary-phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth. Mol Microbiol 32: 789-798, 1999.
    • (1999) Mol Microbiol , vol.32 , pp. 789-798
    • Santos, J.M.1    Freire, P.2    Vicente, M.3    Arraiano, C.M.4
  • 32
    • 0036033601 scopus 로고    scopus 로고
    • The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli
    • Santos JM, Lobo M, Matos AP, De Pedro MA, and Arraiano CM. The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli. Mol Microbiol 45: 1729-1740, 2002.
    • (2002) Mol Microbiol , vol.45 , pp. 1729-1740
    • Santos, J.M.1    Lobo, M.2    Matos, A.P.3    De Pedro, M.A.4    Arraiano, C.M.5
  • 33
    • 11144358198 scopus 로고    scopus 로고
    • A gene atlas of the mouse and human protein-encoding transcriptomes
    • Su AI, et al. A gene atlas of the mouse and human protein-encoding transcriptomes. Proc Natl Acad SciUSA 101: 6062-6067, 2004.
    • (2004) Proc Natl Acad SciUSA , vol.101 , pp. 6062-6067
    • Su, A.I.1
  • 34
    • 0038491193 scopus 로고    scopus 로고
    • Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin
    • Tamarit J, Belli G, Cabiscol E, Herrero E, and Ros J. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J Biol Chem 278: 25745-25751, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 25745-25751
    • Tamarit, J.1    Belli, G.2    Cabiscol, E.3    Herrero, E.4    Ros, J.5
  • 37
    • 33947129099 scopus 로고    scopus 로고
    • Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex i assembly
    • Vogel RO, et al. Cytosolic signaling protein Ecsit also localizes to mitochondria where it interacts with chaperone NDUFAF1 and functions in complex I assembly. Genes Dev 21: 615-624, 2007.
    • (2007) Genes Dev , vol.21 , pp. 615-624
    • Vogel, R.O.1
  • 39
    • 23944500052 scopus 로고    scopus 로고
    • Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis
    • Wingert RA, et al. Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis. Nature 436: 1035-1039, 2005.
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1
  • 40
    • 33646822978 scopus 로고    scopus 로고
    • CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation
    • Ye H, Abdel-Ghany SE, Anderson TD, Pilon-Smits EA, and Pilon M. CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation. J Biol Chem 281: 8958-8969, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 8958-8969
    • Ye, H.1    Abdel-Ghany, S.E.2    Anderson, T.D.3    Pilon-Smits, E.A.4    Pilon, M.5
  • 41
    • 77951843593 scopus 로고    scopus 로고
    • Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythoblasts
    • Ye H, et al. Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythoblasts. J Clin Invest 120: 1749-1761, 2010.
    • (2010) J Clin Invest , vol.120 , pp. 1749-1761
    • Ye, H.1
  • 42
    • 3242890471 scopus 로고    scopus 로고
    • SiRNA Selection Server: An automated siRNA oligonucleo-tide prediction server
    • Yuan B, Latek R, Hossbach M, Tuschl T, and Lewitter F. siRNA Selection Server: an automated siRNA oligonucleo-tide prediction server. Nucleic Acids Res 32: W130-W134, 2004.
    • (2004) Nucleic Acids Res , vol.32
    • Yuan, B.1    Latek, R.2    Hossbach, M.3    Tuschl, T.4    Lewitter, F.5
  • 43
    • 53149105514 scopus 로고    scopus 로고
    • HBolA, novel non-classical secreted proteins, belonging to different BolA family with functional divergence
    • Zhou YB, et al. hBolA, novel non-classical secreted proteins, belonging to different BolA family with functional divergence. Mol Cell Biochem 317: 61-68, 2008.
    • (2008) Mol Cell Biochem , vol.317 , pp. 61-68
    • Zhou, Y.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.