메뉴 건너뛰기




Volumn 123, Issue 2, 2005, Pages 277-289

The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

ISOENZYME; MITOCHONDRIAL PROTEIN; PARAPLEGIN; PROTEINASE; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

EID: 26844484821     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.08.003     Document Type: Article
Times cited : (324)

References (41)
  • 1
    • 0030008581 scopus 로고    scopus 로고
    • The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
    • H. Arlt, R. Tauer, H. Feldmann, W. Neupert, and T. Langer The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria Cell 85 1996 875 885
    • (1996) Cell , vol.85 , pp. 875-885
    • Arlt, H.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 2
    • 0032541406 scopus 로고    scopus 로고
    • The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease
    • H. Arlt, G. Steglich, R. Perryman, B. Guiard, W. Neupert, and T. Langer The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease EMBO J. 17 1998 4837 4847
    • (1998) EMBO J. , vol.17 , pp. 4837-4847
    • Arlt, H.1    Steglich, G.2    Perryman, R.3    Guiard, B.4    Neupert, W.5    Langer, T.6
  • 3
    • 0344736798 scopus 로고    scopus 로고
    • Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia
    • L. Atorino, L. Silvestri, M. Koppen, L. Cassina, A. Ballabio, R. Marconi, T. Langer, and G. Casari Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia J. Cell Biol. 163 2003 777 787
    • (2003) J. Cell Biol. , vol.163 , pp. 777-787
    • Atorino, L.1    Silvestri, L.2    Koppen, M.3    Cassina, L.4    Ballabio, A.5    Marconi, R.6    Langer, T.7    Casari, G.8
  • 4
    • 0027979074 scopus 로고
    • Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue
    • C.L. Campbell, N. Tanaka, K.H. White, and P.E. Thorsness Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue Mol. Biol. Cell 5 1994 899 905
    • (1994) Mol. Biol. Cell , vol.5 , pp. 899-905
    • Campbell, C.L.1    Tanaka, N.2    White, K.H.3    Thorsness, P.E.4
  • 6
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • A. Ciechanover Proteolysis: from the lysosome to ubiquitin and the proteasome Nat. Rev. Mol. Cell Biol. 6 2005 79 87
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 7
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • S. DiMauro, and E.A. Schon Mitochondrial respiratory-chain diseases N. Engl. J. Med. 348 2003 2656 2668
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2656-2668
    • Dimauro, S.1    Schon, E.A.2
  • 9
    • 0038819972 scopus 로고    scopus 로고
    • Evidence that synthesis of the Saccharomyces cerevisiae mitochondrially encoded ribosomal protein Var1p may be membrane localized
    • A. Fiori, T.L. Mason, and T.D. Fox Evidence that synthesis of the Saccharomyces cerevisiae mitochondrially encoded ribosomal protein Var1p may be membrane localized Eukaryot. Cell 2 2003 651 653
    • (2003) Eukaryot. Cell , vol.2 , pp. 651-653
    • Fiori, A.1    Mason, T.L.2    Fox, T.D.3
  • 10
    • 4644283533 scopus 로고    scopus 로고
    • O-ATP synthase in mitochondria
    • O-ATP synthase in mitochondria J. Biol. Chem. 279 2004 38338 38345
    • (2004) J. Biol. Chem. , vol.279 , pp. 38338-38345
    • Galluhn, D.1    Langer, T.2
  • 11
    • 0025762363 scopus 로고
    • Extended N-terminal sequencing of proteins of the large ribosomal subunit from yeast mitochondria
    • L. Grohmann, H.R. Graack, V. Kruft, T. Choli, S. Goldschmidt-Reisin, and M. Kitakawa Extended N-terminal sequencing of proteins of the large ribosomal subunit from yeast mitochondria FEBS Lett. 284 1991 51 56
    • (1991) FEBS Lett. , vol.284 , pp. 51-56
    • Grohmann, L.1    Graack, H.R.2    Kruft, V.3    Choli, T.4    Goldschmidt-Reisin, S.5    Kitakawa, M.6
  • 12
    • 0028072194 scopus 로고
    • Sequence of the AFG3 gene encoding a new member of the FtsH/Yme1/Tma subfamily of the AAA-protein family
    • E. Guélin, M. Rep, and L.A. Grivell Sequence of the AFG3 gene encoding a new member of the FtsH/Yme1/Tma subfamily of the AAA-protein family Yeast 10 1994 1389 1394
    • (1994) Yeast , vol.10 , pp. 1389-1394
    • Guélin, E.1    Rep, M.2    Grivell, L.A.3
  • 14
    • 19444380425 scopus 로고    scopus 로고
    • Nuclear genes and mitochondrial translation: A new class of genetic disease
    • H.T. Jacobs, and D.M. Turnbull Nuclear genes and mitochondrial translation: a new class of genetic disease Trends Genet. 21 2005 312 314
    • (2005) Trends Genet. , vol.21 , pp. 312-314
    • Jacobs, H.T.1    Turnbull, D.M.2
  • 15
    • 0024199388 scopus 로고
    • Import of proteins into yeast mitochondria: The nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit
    • R.E. Jensen, and M.P. Yaffe Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit EMBO J. 7 1988 3863 3871
    • (1988) EMBO J. , vol.7 , pp. 3863-3871
    • Jensen, R.E.1    Yaffe, M.P.2
  • 16
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: The importance of the C-terminal region of Oxa1
    • L. Jia, M. Dienhart, M. Schramp, M. McCauley, K. Hell, and R.A. Stuart Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1 EMBO J. 22 2003 6438 6447
    • (2003) EMBO J. , vol.22 , pp. 6438-6447
    • Jia, L.1    Dienhart, M.2    Schramp, M.3    McCauley, M.4    Hell, K.5    Stuart, R.A.6
  • 17
    • 21244505013 scopus 로고    scopus 로고
    • Role of the novel metallopeptidase MOP112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria
    • M. Kambacheld, S. Augustin, T. Tatsuta, S. Müller, and T. Langer Role of the novel metallopeptidase MOP112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria J. Biol. Chem. 280 2005 20132 20139
    • (2005) J. Biol. Chem. , vol.280 , pp. 20132-20139
    • Kambacheld, M.1    Augustin, S.2    Tatsuta, T.3    Müller, S.4    Langer, T.5
  • 18
    • 0032400955 scopus 로고    scopus 로고
    • MHC class I molecules compete in the endoplasmic reticulum for access to transporter associated with antigen processing
    • M.R. Knittler, K. Gulow, A. Seelig, and J.C. Howard MHC class I molecules compete in the endoplasmic reticulum for access to transporter associated with antigen processing J. Immunol. 161 1998 5967 5977
    • (1998) J. Immunol. , vol.161 , pp. 5967-5977
    • Knittler, M.R.1    Gulow, K.2    Seelig, A.3    Howard, J.C.4
  • 19
    • 4043071992 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae translational activator Cbs2p is associated with mitochondrial ribosomes
    • U. Krause-Buchholz, K. Barth, C. Dombrowski, and G. Rodel Saccharomyces cerevisiae translational activator Cbs2p is associated with mitochondrial ribosomes Curr. Genet. 46 2004 20 28
    • (2004) Curr. Genet. , vol.46 , pp. 20-28
    • Krause-Buchholz, U.1    Barth, K.2    Dombrowski, C.3    Rodel, G.4
  • 20
    • 0029775087 scopus 로고    scopus 로고
    • AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria
    • K. Leonhard, J.M. Herrmann, R.A. Stuart, G. Mannhaupt, W. Neupert, and T. Langer AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria EMBO J. 15 1996 4218 4229
    • (1996) EMBO J. , vol.15 , pp. 4218-4229
    • Leonhard, K.1    Herrmann, J.M.2    Stuart, R.A.3    Mannhaupt, G.4    Neupert, W.5    Langer, T.6
  • 21
    • 0034703062 scopus 로고    scopus 로고
    • Interaction of mammalian mitochondrial ribosomes with the inner membrane
    • M. Liu, and L. Spremulli Interaction of mammalian mitochondrial ribosomes with the inner membrane J. Biol. Chem. 275 2000 29400 29406
    • (2000) J. Biol. Chem. , vol.275 , pp. 29400-29406
    • Liu, M.1    Spremulli, L.2
  • 23
    • 0027241016 scopus 로고
    • COX3 mRNA-specific translational activator proteins are associated with the inner mitochondrial membrane in Saccharomyces cerevisiae
    • T.W. McMullin, and T.D. Fox COX3 mRNA-specific translational activator proteins are associated with the inner mitochondrial membrane in Saccharomyces cerevisiae J. Biol. Chem. 268 1993 11737 11741
    • (1993) J. Biol. Chem. , vol.268 , pp. 11737-11741
    • McMullin, T.W.1    Fox, T.D.2
  • 24
    • 0025934599 scopus 로고
    • Association of cytochrome b translational activator proteins with the mitochondrial membrane: Implications for cytochrome b expression in yeast
    • U. Michaelis, A. Korte, and G. Rodel Association of cytochrome b translational activator proteins with the mitochondrial membrane: implications for cytochrome b expression in yeast Mol. Gen. Genet. 230 1991 177 185
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 177-185
    • Michaelis, U.1    Korte, A.2    Rodel, G.3
  • 25
    • 0022110054 scopus 로고
    • Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae
    • A.M. Myers, L.K. Pape, and A. Tzagoloff Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae EMBO J. 4 1985 2087 2092
    • (1985) EMBO J. , vol.4 , pp. 2087-2092
    • Myers, A.M.1    Pape, L.K.2    Tzagoloff, A.3
  • 26
    • 0037238395 scopus 로고    scopus 로고
    • Interactions among COX1, COX2, and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae
    • S. Naithani, S.A. Saracco, C.A. Butler, and T.D. Fox Interactions among COX1, COX2, and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae Mol. Biol. Cell 14 2003 324 333
    • (2003) Mol. Biol. Cell , vol.14 , pp. 324-333
    • Naithani, S.1    Saracco, S.A.2    Butler, C.A.3    Fox, T.D.4
  • 28
    • 9644302406 scopus 로고    scopus 로고
    • Productive RUPture: Activation of transcription factors by proteasomal processing
    • M. Rape, and S. Jentsch Productive RUPture: activation of transcription factors by proteasomal processing Biochim. Biophys. Acta 1695 2004 209 213
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 209-213
    • Rape, M.1    Jentsch, S.2
  • 29
    • 0029837817 scopus 로고    scopus 로고
    • Three genes for mitochondrial proteins suppress null-mutations in both AFG3 and RCA1 when overexpressed
    • M. Rep, J. Nooy, E. Guélin, and L.A. Grivell Three genes for mitochondrial proteins suppress null-mutations in both AFG3 and RCA1 when overexpressed Curr. Genet. 30 1996 206 211
    • (1996) Curr. Genet. , vol.30 , pp. 206-211
    • Rep, M.1    Nooy, J.2    Guélin, E.3    Grivell, L.A.4
  • 31
    • 0017865122 scopus 로고
    • Mutations of the mitochondrial DNA of Saccharomyces cerevisiae which affect the interaction between mitochondrial ribosomes and the inner mitochondrial membrane
    • T.W. Spithill, M.K. Trembath, H.B. Lukins, and A.W. Linnane Mutations of the mitochondrial DNA of Saccharomyces cerevisiae which affect the interaction between mitochondrial ribosomes and the inner mitochondrial membrane Mol. Gen. Genet. 164 1978 155 162
    • (1978) Mol. Gen. Genet. , vol.164 , pp. 155-162
    • Spithill, T.W.1    Trembath, M.K.2    Lukins, H.B.3    Linnane, A.W.4
  • 32
    • 0032954927 scopus 로고    scopus 로고
    • Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria
    • G. Steglich, W. Neupert, and T. Langer Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria Mol. Cell. Biol. 19 1999 3435 3442
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3435-3442
    • Steglich, G.1    Neupert, W.2    Langer, T.3
  • 33
    • 0028771996 scopus 로고
    • Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration
    • C.K. Suzuki, K. Suda, N. Wang, and G. Schatz Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration Science 264 1994 273 276
    • (1994) Science , vol.264 , pp. 273-276
    • Suzuki, C.K.1    Suda, K.2    Wang, N.3    Schatz, G.4
  • 34
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria
    • G. Szyrach, M. Ott, N. Bonnefoy, W. Neupert, and J.M. Herrmann Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria EMBO J. 22 2003 6448 6457
    • (2003) EMBO J. , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5
  • 35
    • 33748306502 scopus 로고    scopus 로고
    • Studying proteolysis within mitochondria
    • in press.
    • Tatsuta, T., and Langer, T. (2005). Studying proteolysis within mitochondria. Curr. Topics Gen., in press.
    • (2005) Curr. Topics Gen.
    • Tatsuta, T.1    Langer, T.2
  • 36
    • 17744393686 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in human disease
    • R.W. Taylor, and D.M. Turnbull Mitochondrial DNA mutations in human disease Nat. Rev. Genet. 6 2005 389 402
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 389-402
    • Taylor, R.W.1    Turnbull, D.M.2
  • 37
    • 0027304446 scopus 로고
    • Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae
    • P.E. Thorsness, K.H. White, and T.D. Fox Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae Mol. Cell. Biol. 13 1993 5418 5426
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5418-5426
    • Thorsness, P.E.1    White, K.H.2    Fox, T.D.3
  • 38
    • 0028117097 scopus 로고
    • The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
    • C. Ungermann, W. Neupert, and D.M. Cyr The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria Science 266 1994 1250 1253
    • (1994) Science , vol.266 , pp. 1250-1253
    • Ungermann, C.1    Neupert, W.2    Cyr, D.M.3
  • 39
    • 0028325509 scopus 로고
    • A morphological view on mitochondrial protein targeting
    • I. Van der Klei, M. Veenhuis, and W. Neupert A morphological view on mitochondrial protein targeting Microsc. Res. Tech. 27 1994 284 293
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 284-293
    • Van Der Klei, I.1    Veenhuis, M.2    Neupert, W.3
  • 40
    • 0032698023 scopus 로고    scopus 로고
    • ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae
    • L. Van Dyck, and T. Langer ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae Cell. Mol. Life Sci. 55 1999 825 842
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 825-842
    • Van Dyck, L.1    Langer, T.2
  • 41
    • 0028049082 scopus 로고
    • PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae
    • L. Van Dyck, D.A. Pearce, and F. Sherman PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae J. Biol. Chem. 269 1994 238 242
    • (1994) J. Biol. Chem. , vol.269 , pp. 238-242
    • Van Dyck, L.1    Pearce, D.A.2    Sherman, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.