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Volumn 8, Issue 10, 2013, Pages

Mitochondrial Aminopeptidase Deletion Increases Chronological Lifespan and Oxidative Stress Resistance while Decreasing Respiratory Metabolism in S. cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; GLUCOSE; MITOCHONDRIAL PROTEIN; PROTEIN ICP55; PROTEIN MDL1; PROTEIN TOR1; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE; TARGET OF RAPAMYCIN KINASE; UNCLASSIFIED DRUG;

EID: 84885139764     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0077234     Document Type: Article
Times cited : (10)

References (33)
  • 1
    • 77949865316 scopus 로고    scopus 로고
    • Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy
    • O'Toole JF, Liu Y, Davis EE, Westlake CJ, Attanasio M, et al, (2010) Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy. J Clin Invest 120: 791-802.
    • (2010) J Clin Invest , vol.120 , pp. 791-802
    • O'Toole, J.F.1    Liu, Y.2    Davis, E.E.3    Westlake, C.J.4    Attanasio, M.5
  • 2
    • 0023777507 scopus 로고
    • Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme
    • Yoshimoto T, Murayama N, Honda T, Tone H, Tsuru D, (1988) Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme. J Biochem 104: 93-97.
    • (1988) J Biochem , vol.104 , pp. 93-97
    • Yoshimoto, T.1    Murayama, N.2    Honda, T.3    Tone, H.4    Tsuru, D.5
  • 3
    • 71049136017 scopus 로고    scopus 로고
    • Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55
    • Naamati A, Regev-Rudzki N, Galperin S, Lill R, (2009) Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. J Biol Chem 284: 30200-30208.
    • (2009) J Biol Chem , vol.284 , pp. 30200-30208
    • Naamati, A.1    Regev-Rudzki, N.2    Galperin, S.3    Lill, R.4
  • 4
    • 70349840621 scopus 로고    scopus 로고
    • Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability
    • Vogtle FN, Wortelkamp S, Zahedi RP, Becker D, Leidhold C, et al, (2009) Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability. Cell 139: 428-439.
    • (2009) Cell , vol.139 , pp. 428-439
    • Vogtle, F.N.1    Wortelkamp, S.2    Zahedi, R.P.3    Becker, D.4    Leidhold, C.5
  • 5
  • 6
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics
    • Reinders J, Zahedi RP, Pfanner N, Meisinger C, Sickmann A, (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5: 1543-1554.
    • (2006) J Proteome Res , vol.5 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 8
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A, Finley D, Varshavsky A, (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 9
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky A (2011) The N-end rule pathway and regulation by proteolysis. Protein Sci 10.
    • (2011) Protein Sci , vol.10
    • Varshavsky, A.1
  • 10
    • 0035896360 scopus 로고    scopus 로고
    • Role of the ABC transporter Mdl1 in peptide export from mitochondria
    • Young L, Leonhard K, Tatsuta T, Trowsdale J, Langer T, (2001) Role of the ABC transporter Mdl1 in peptide export from mitochondria. Science 291: 2135-2138.
    • (2001) Science , vol.291 , pp. 2135-2138
    • Young, L.1    Leonhard, K.2    Tatsuta, T.3    Trowsdale, J.4    Langer, T.5
  • 11
    • 0031894922 scopus 로고    scopus 로고
    • Mitochondrial disorders and the kidney
    • Niaudet P, (1998) Mitochondrial disorders and the kidney. Arch Dis Child 78: 387-390.
    • (1998) Arch Dis Child , vol.78 , pp. 387-390
    • Niaudet, P.1
  • 12
    • 84866076360 scopus 로고    scopus 로고
    • Nutritional control of growth and development in yeast
    • Broach JR, (2012) Nutritional control of growth and development in yeast. Genetics 192: 73-105.
    • (2012) Genetics , vol.192 , pp. 73-105
    • Broach, J.R.1
  • 13
    • 78349294528 scopus 로고    scopus 로고
    • Simple is good: yeast models of neurodegeneration
    • Tenreiro S, Outeiro TF, (2010) Simple is good: yeast models of neurodegeneration. FEMS Yeast Res 10: 970-979.
    • (2010) FEMS Yeast Res , vol.10 , pp. 970-979
    • Tenreiro, S.1    Outeiro, T.F.2
  • 14
    • 4444271170 scopus 로고    scopus 로고
    • A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
    • Janke C, Magiera MM, Rathfelder N, Taxis C, Reber S, et al, (2004) A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast 21: 947-962.
    • (2004) Yeast , vol.21 , pp. 947-962
    • Janke, C.1    Magiera, M.M.2    Rathfelder, N.3    Taxis, C.4    Reber, S.5
  • 17
    • 0036024975 scopus 로고    scopus 로고
    • Blue Native electrophoresis to study mitochondrial and other protein complexes
    • Nijtmans LG, Henderson NS, Holt IJ, (2002) Blue Native electrophoresis to study mitochondrial and other protein complexes. Methods 26: 327-334.
    • (2002) Methods , vol.26 , pp. 327-334
    • Nijtmans, L.G.1    Henderson, N.S.2    Holt, I.J.3
  • 18
    • 33745473351 scopus 로고    scopus 로고
    • Defective mitochondrial gene expression results in reactive oxygen species-mediated inhibition of respiration and reduction of yeast life span
    • Bonawitz ND, Rodeheffer MS, Shadel GS, (2006) Defective mitochondrial gene expression results in reactive oxygen species-mediated inhibition of respiration and reduction of yeast life span. Mol Cell Biol 26: 4818-4829.
    • (2006) Mol Cell Biol , vol.26 , pp. 4818-4829
    • Bonawitz, N.D.1    Rodeheffer, M.S.2    Shadel, G.S.3
  • 19
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schagger H, Pfeiffer K, (2000) Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J 19: 1777-1783.
    • (2000) EMBO J , vol.19 , pp. 1777-1783
    • Schagger, H.1    Pfeiffer, K.2
  • 20
    • 33947574775 scopus 로고    scopus 로고
    • Reduced TOR signaling extends chronological life span via increased respiration and upregulation of mitochondrial gene expression
    • Bonawitz ND, Chatenay-Lapointe M, Pan Y, Shadel GS, (2007) Reduced TOR signaling extends chronological life span via increased respiration and upregulation of mitochondrial gene expression. Cell Metab 5: 265-277.
    • (2007) Cell Metab , vol.5 , pp. 265-277
    • Bonawitz, N.D.1    Chatenay-Lapointe, M.2    Pan, Y.3    Shadel, G.S.4
  • 21
    • 68049109688 scopus 로고    scopus 로고
    • Extension of chronological life span by reduced TOR signaling requires down-regulation of Sch9p and involves increased mitochondrial OXPHOS complex density
    • Pan Y, Shadel GS, (2009) Extension of chronological life span by reduced TOR signaling requires down-regulation of Sch9p and involves increased mitochondrial OXPHOS complex density. Aging (Albany NY) 1: 131-145.
    • (2009) Aging (Albany NY) , vol.1 , pp. 131-145
    • Pan, Y.1    Shadel, G.S.2
  • 22
    • 84868561251 scopus 로고    scopus 로고
    • Metabolic regulation, mitochondria and the life-prolonging effect of rapamycin: a mini-review
    • Pan Y, Nishida Y, Wang M, Verdin E, (2012) Metabolic regulation, mitochondria and the life-prolonging effect of rapamycin: a mini-review. Gerontology 58: 524-530.
    • (2012) Gerontology , vol.58 , pp. 524-530
    • Pan, Y.1    Nishida, Y.2    Wang, M.3    Verdin, E.4
  • 23
    • 34249813098 scopus 로고    scopus 로고
    • Sch9 is a major target of TORC1 in Saccharomyces cerevisiae
    • Urban J, Soulard A, Huber A, Lippman S, Mukhopadhyay D, et al, (2007) Sch9 is a major target of TORC1 in Saccharomyces cerevisiae. Mol Cell 26: 663-674.
    • (2007) Mol Cell , vol.26 , pp. 663-674
    • Urban, J.1    Soulard, A.2    Huber, A.3    Lippman, S.4    Mukhopadhyay, D.5
  • 24
    • 33845958976 scopus 로고    scopus 로고
    • A systems biology approach to study glucose repression in the yeast Saccharomyces cerevisiae
    • Westergaard SL, Oliveira AP, Bro C, Olsson L, Nielsen J, (2007) A systems biology approach to study glucose repression in the yeast Saccharomyces cerevisiae. Biotechnol Bioeng 96: 134-145.
    • (2007) Biotechnol Bioeng , vol.96 , pp. 134-145
    • Westergaard, S.L.1    Oliveira, A.P.2    Bro, C.3    Olsson, L.4    Nielsen, J.5
  • 25
    • 33748752151 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity
    • Schieke SM, Phillips D, McCoy JP Jr, Aponte AM, Shen RF, et al, (2006) The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity. J Biol Chem 281: 27643-27652.
    • (2006) J Biol Chem , vol.281 , pp. 27643-27652
    • Schieke, S.M.1    Phillips, D.2    McCoy Jr., J.P.3    Aponte, A.M.4    Shen, R.F.5
  • 26
    • 76049099052 scopus 로고    scopus 로고
    • Direct control of mitochondrial function by mTOR
    • Ramanathan A, Schreiber SL, (2009) Direct control of mitochondrial function by mTOR. Proc Natl Acad Sci U S A 106: 22229-22232.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 22229-22232
    • Ramanathan, A.1    Schreiber, S.L.2
  • 27
    • 36749081539 scopus 로고    scopus 로고
    • mTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex
    • Cunningham JT, Rodgers JT, Arlow DH, Vazquez F, Mootha VK, et al, (2007) mTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex. Nature 450: 736-740.
    • (2007) Nature , vol.450 , pp. 736-740
    • Cunningham, J.T.1    Rodgers, J.T.2    Arlow, D.H.3    Vazquez, F.4    Mootha, V.K.5
  • 28
    • 84863937859 scopus 로고    scopus 로고
    • Mammalian target of rapamycin and the kidney. II. Pathophysiology and therapeutic implications
    • Lieberthal W, Levine JS, (2012) Mammalian target of rapamycin and the kidney. II. Pathophysiology and therapeutic implications. Am J Physiol Renal Physiol 303: F180-F191.
    • (2012) Am J Physiol Renal Physiol , vol.303
    • Lieberthal, W.1    Levine, J.S.2
  • 29
    • 79959409830 scopus 로고    scopus 로고
    • Amino acid signaling in TOR activation
    • Kim J, Guan KL, (2011) Amino acid signaling in TOR activation. Annu Rev Biochem 80: 1001-32 -.
    • (2011) Annu Rev Biochem , vol.80 , pp. 1001-1032
    • Kim, J.1    Guan, K.L.2
  • 30
    • 84863323742 scopus 로고    scopus 로고
    • Mammalian target of rapamycin and the kidney. I. The signaling pathway
    • Lieberthal W, Levine JS, (2012) Mammalian target of rapamycin and the kidney. I. The signaling pathway. Am J Physiol Renal Physiol 303: F1-10.
    • (2012) Am J Physiol Renal Physiol , vol.303 , pp. 1-10
    • Lieberthal, W.1    Levine, J.S.2
  • 31
    • 78649728763 scopus 로고    scopus 로고
    • The mitochondrial UPR - protecting organelle protein homeostasis
    • Haynes CM, Ron D, (2010) The mitochondrial UPR- protecting organelle protein homeostasis. J Cell Sci 123: 3849-3855.
    • (2010) J Cell Sci , vol.123 , pp. 3849-3855
    • Haynes, C.M.1    Ron, D.2
  • 32
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund AM, Pellegrino MW, Fiorese CJ, Baker BM, Haynes CM, (2012) Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337: 587-590.
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 33
    • 84878138385 scopus 로고    scopus 로고
    • Mitonuclear protein imbalance as a conserved longevity mechanism
    • Houtkooper RH, Mouchiroud L, Ryu D, Moullan N, Katsyuba E, et al, (2013) Mitonuclear protein imbalance as a conserved longevity mechanism. Nature 497: 451-457.
    • (2013) Nature , vol.497 , pp. 451-457
    • Houtkooper, R.H.1    Mouchiroud, L.2    Ryu, D.3    Moullan, N.4    Katsyuba, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.