메뉴 건너뛰기




Volumn 145, Issue 1, 2012, Pages 180-186

A novel mitochondrial and chloroplast peptidasome, PreP

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; CHLOROPLAST PROTEIN; MITOCHONDRIAL PROTEIN; PEPTIDE HYDROLASE; PRESEQUENCE PROTEASE PREP, ARABIDOPSIS;

EID: 84859844774     PISSN: 00319317     EISSN: 13993054     Source Type: Journal    
DOI: 10.1111/j.1399-3054.2011.01531.x     Document Type: Review
Times cited : (26)

References (46)
  • 2
    • 80155167229 scopus 로고    scopus 로고
    • Decreased proteolytic activity of the mitochondrial Aβ degrading enzyme, PreP peptidasome, in Alzheimer's Disease brain mitochondria.
    • Alikhani N, Lan G, Yan S, Du H, Pinho CM, Chen IX, Glaser E, Yan SD (2011b) Decreased proteolytic activity of the mitochondrial Aβ degrading enzyme, PreP peptidasome, in Alzheimer's Disease brain mitochondria. J Alzheimers Dis 27: 75-87
    • (2011) J Alzheimers Dis , vol.27 , pp. 75-87
    • Alikhani, N.1    Lan, G.2    Yan, S.3    Du, H.4    Pinho, C.M.5    Chen, I.X.6    Glaser, E.7    Yan, S.D.8
  • 3
    • 69249218858 scopus 로고    scopus 로고
    • Binding of divalent cations is essential for the activity of the organellar peptidasome in Arabidopsis thaliana, AtPreP.
    • Backman HG, Pessoa J, Eneqvist T, Glaser E (2009) Binding of divalent cations is essential for the activity of the organellar peptidasome in Arabidopsis thaliana, AtPreP. FEBS Lett 583: 2727-2733
    • (2009) FEBS Lett , vol.583 , pp. 2727-2733
    • Backman, H.G.1    Pessoa, J.2    Eneqvist, T.3    Glaser, E.4
  • 4
    • 2942530586 scopus 로고    scopus 로고
    • Chloroplast proteomics: potentials and challenges.
    • Baginsky S, Gruissem W (2004) Chloroplast proteomics: potentials and challenges. J Exp Bot 55: 1213-1220
    • (2004) J Exp Bot , vol.55 , pp. 1213-1220
    • Baginsky, S.1    Gruissem, W.2
  • 5
    • 70349804290 scopus 로고    scopus 로고
    • Defining the determinants for dual targeting of amino acyl-tRNA synthetases to mitochondria and chloroplasts.
    • Berglund AK, Pujol C, Duchene AM, Glaser E (2009) Defining the determinants for dual targeting of amino acyl-tRNA synthetases to mitochondria and chloroplasts. J Mol Biol 393: 803-814
    • (2009) J Mol Biol , vol.393 , pp. 803-814
    • Berglund, A.K.1    Pujol, C.2    Duchene, A.M.3    Glaser, E.4
  • 6
    • 0348133604 scopus 로고    scopus 로고
    • Dual targeting and function of a protease in mitochondria and chloroplasts.
    • Bhushan S, Lefebvre B, Stahl A, Boutry M, Glaser E (2003) Dual targeting and function of a protease in mitochondria and chloroplasts. EMBO Rep 4: 1073-1078
    • (2003) EMBO Rep , vol.4 , pp. 1073-1078
    • Bhushan, S.1    Lefebvre, B.2    Stahl, A.3    Boutry, M.4    Glaser, E.5
  • 8
    • 33745411089 scopus 로고    scopus 로고
    • The role of the N-terminal domain of chloroplast targeting peptides in organellar protein import and miss-sorting.
    • Bhushan S, Kuhn C, Berglund AK, Roth C, Glaser E (2006) The role of the N-terminal domain of chloroplast targeting peptides in organellar protein import and miss-sorting. FEBS Lett 580: 3966-3972
    • (2006) FEBS Lett , vol.580 , pp. 3966-3972
    • Bhushan, S.1    Kuhn, C.2    Berglund, A.K.3    Roth, C.4    Glaser, E.5
  • 9
    • 77956913411 scopus 로고    scopus 로고
    • Chloroplast import signals: the length requirement for translocation in vitro and in vivo.
    • Bionda T, Tillmann B, Simm S, Beilstein K, Ruprecht M, Schleiff E (2010) Chloroplast import signals: the length requirement for translocation in vitro and in vivo. J Mol Biol 402: 510-523
    • (2010) J Mol Biol , vol.402 , pp. 510-523
    • Bionda, T.1    Tillmann, B.2    Simm, S.3    Beilstein, K.4    Ruprecht, M.5    Schleiff, E.6
  • 10
    • 0026709336 scopus 로고
    • The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain.
    • Braun HP, Emmermann M, Kruft V, Schmitz UK (1992) The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J 11: 3219-3227
    • (1992) EMBO J , vol.11 , pp. 3219-3227
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 11
    • 60349127044 scopus 로고    scopus 로고
    • Protein transport in organelles: dual targeting of proteins to mitochondria and chloroplasts.
    • Carrie C, Giraud E, Whelan J (2009) Protein transport in organelles: dual targeting of proteins to mitochondria and chloroplasts. FEBS J 276: 1187-1195
    • (2009) FEBS J , vol.276 , pp. 1187-1195
    • Carrie, C.1    Giraud, E.2    Whelan, J.3
  • 12
    • 33644876148 scopus 로고    scopus 로고
    • Dual-domain, dual-targeting organellar protein presequences in Arabidopsis can use non-AUG start codons.
    • Christensen AC, Lyznik A, Mohammed S, Elowsky CG, Elo A, Yule R, Mackenzie SA (2005) Dual-domain, dual-targeting organellar protein presequences in Arabidopsis can use non-AUG start codons. Plant Cell 17: 2805-2816
    • (2005) Plant Cell , vol.17 , pp. 2805-2816
    • Christensen, A.C.1    Lyznik, A.2    Mohammed, S.3    Elowsky, C.G.4    Elo, A.5    Yule, R.6    Mackenzie, S.A.7
  • 17
    • 0028177426 scopus 로고
    • Bifunctional role of the bc1 complex in plants. Mitochondrial bc1 complex catalyses both electron transport and protein processing.
    • Glaser E, Eriksson A, Sjöling S (1994) Bifunctional role of the bc1 complex in plants. Mitochondrial bc1 complex catalyses both electron transport and protein processing. FEBS Lett 346: 83-87
    • (1994) FEBS Lett , vol.346 , pp. 83-87
    • Glaser, E.1    Eriksson, A.2    Sjöling, S.3
  • 19
    • 0024276898 scopus 로고
    • Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein.
    • Hawlitschek G, Schneider H, Schmidt B, Tropschug M, Hartl FU, Neupert W (1988) Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein. Cell 53: 795-806
    • (1988) Cell , vol.53 , pp. 795-806
    • Hawlitschek, G.1    Schneider, H.2    Schmidt, B.3    Tropschug, M.4    Hartl, F.U.5    Neupert, W.6
  • 20
    • 0034330546 scopus 로고    scopus 로고
    • One RNA polymerase serving two genomes.
    • Hedtke B, Borner T, Weihe A (2000) One RNA polymerase serving two genomes. EMBO Rep 1: 435-440
    • (2000) EMBO Rep , vol.1 , pp. 435-440
    • Hedtke, B.1    Borner, T.2    Weihe, A.3
  • 22
    • 67650156863 scopus 로고    scopus 로고
    • Refining the definition of plant mitochondrial presequences through analysis of sorting signals, N-terminal modifications, and cleavage motifs.
    • Huang S, Taylor NL, Whelan J, Millar AH (2009) Refining the definition of plant mitochondrial presequences through analysis of sorting signals, N-terminal modifications, and cleavage motifs. Plant Physiol 150: 1272-1285
    • (2009) Plant Physiol , vol.150 , pp. 1272-1285
    • Huang, S.1    Taylor, N.L.2    Whelan, J.3    Millar, A.H.4
  • 23
    • 0027978980 scopus 로고
    • Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import.
    • Hugosson M, Andreu D, Boman HG, Glaser E (1994) Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import. Eur J Biochem 223: 1027-1033
    • (1994) Eur J Biochem , vol.223 , pp. 1027-1033
    • Hugosson, M.1    Andreu, D.2    Boman, H.G.3    Glaser, E.4
  • 25
    • 11244334104 scopus 로고    scopus 로고
    • Enhanced peptide secretion by gene disruption of CYM1, a novel protease in Saccharomyces cerevisiae.
    • Jonson L, Rehfeld JF, Johnsen AH (2004) Enhanced peptide secretion by gene disruption of CYM1, a novel protease in Saccharomyces cerevisiae. Eur J Biochem 271: 4788-4797
    • (2004) Eur J Biochem , vol.271 , pp. 4788-4797
    • Jonson, L.1    Rehfeld, J.F.2    Johnsen, A.H.3
  • 26
    • 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.
    • Kambacheld M, Augustin S, Tatsuta T, Müller S, Langer T (2005) Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. J Biol Chem 280: 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
  • 27
    • 0027287709 scopus 로고
    • Import of a mitochondrial presequence into protein-free phospholipid vesicles.
    • Maduke M, Roise D (1993) Import of a mitochondrial presequence into protein-free phospholipid vesicles. Science 260: 364-367
    • (1993) Science , vol.260 , pp. 364-367
    • Maduke, M.1    Roise, D.2
  • 29
    • 0344668824 scopus 로고    scopus 로고
    • Characterization of a novel zinc metalloprotease involved in degrading signal peptides in mitochondria and chloroplasts.
    • Moberg P, Stahl A, Bhushan S, Wright SJ, Eriksson AC, Bruce BD, Glaser E ( 2003) Characterization of a novel zinc metalloprotease involved in degrading signal peptides in mitochondria and chloroplasts. Plant J 36:616-628
    • (2003) Plant J , vol.36 , pp. 616-628
    • Moberg, P.1    Stahl, A.2    Bhushan, S.3    Wright, S.J.4    Eriksson, A.C.5    Bruce, B.D.6    Glaser, E.7
  • 30
    • 1242317038 scopus 로고    scopus 로고
    • NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia.
    • Moberg P, Nilsson S, Stahl A, Eriksson AC, Glaser E, Maler L (2004) NMR solution structure of the mitochondrial F1beta presequence from Nicotiana plumbaginifolia. J Mol Biol 336: 1129-1140
    • (2004) J Mol Biol , vol.336 , pp. 1129-1140
    • Moberg, P.1    Nilsson, S.2    Stahl, A.3    Eriksson, A.C.4    Glaser, E.5    Maler, L.6
  • 31
    • 0028238446 scopus 로고
    • Effects of amphipathic peptides, including presequences, on the functional integrity of rat liver mitochondrial membranes.
    • Nicolay K, Laterveer FD, van Heerde WL (1994) Effects of amphipathic peptides, including presequences, on the functional integrity of rat liver mitochondrial membranes. J Bioenerg Biomembr 26: 327-334
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 327-334
    • Nicolay, K.1    Laterveer, F.D.2    van Heerde, W.L.3
  • 32
    • 70350242932 scopus 로고    scopus 로고
    • Deletion of an organellar peptidasome PreP affects early development in Arabidopsis thaliana.
    • Nilsson Cederholm S, Backman HG, Pesaresi P, Leister D, Glaser E (2009) Deletion of an organellar peptidasome PreP affects early development in Arabidopsis thaliana. Plant Mol Biol 71: 497-508
    • (2009) Plant Mol Biol , vol.71 , pp. 497-508
    • Nilsson Cederholm, S.1    Backman, H.G.2    Pesaresi, P.3    Leister, D.4    Glaser, E.5
  • 33
    • 31944448611 scopus 로고    scopus 로고
    • Convergent evolution of receptors for protein import into mitochondria.
    • Perry AJ, Hulett JM, Likić VA, Lithgow T, Gooley PR (2006) Convergent evolution of receptors for protein import into mitochondria. Curr Biol 16: 221-229
    • (2006) Curr Biol , vol.16 , pp. 221-229
    • Perry, A.J.1    Hulett, J.M.2    Likić, V.A.3    Lithgow, T.4    Gooley, P.R.5
  • 35
    • 0032560485 scopus 로고    scopus 로고
    • A chloroplast processing enzyme functions as the general stromal processing peptidase.
    • Richter S, Lamppa GK (1998) A chloroplast processing enzyme functions as the general stromal processing peptidase. Proc Natl Acad Sci USA 95: 7463-7468
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7463-7468
    • Richter, S.1    Lamppa, G.K.2
  • 36
    • 0022725788 scopus 로고
    • A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers.
    • Roise D, Horvath SJ, Tomich JM, Richards JH, Schatz G (1986) A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. EMBO J 5: 1327-1334
    • (1986) EMBO J , vol.5 , pp. 1327-1334
    • Roise, D.1    Horvath, S.J.2    Tomich, J.M.3    Richards, J.H.4    Schatz, G.5
  • 37
    • 0036926941 scopus 로고    scopus 로고
    • N-terminal domain of the dual-targeted pea glutathione reductase signal peptide controls organellar targeting efficiency.
    • Rudhe C, Clifton R, Whelan J, Glaser E (2002) N-terminal domain of the dual-targeted pea glutathione reductase signal peptide controls organellar targeting efficiency. J Mol Biol 324: 577-585
    • (2002) J Mol Biol , vol.324 , pp. 577-585
    • Rudhe, C.1    Clifton, R.2    Whelan, J.3    Glaser, E.4
  • 38
    • 0344962439 scopus 로고    scopus 로고
    • One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations.
    • Silva-Filho MC (2003) One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations. Curr Opin Plant Biol 6: 589-595
    • (2003) Curr Opin Plant Biol , vol.6 , pp. 589-595
    • Silva-Filho, M.C.1
  • 41
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices.
    • von Heijne G (1986) Mitochondrial targeting sequences may form amphiphilic helices. EMBO J 5: 1335-1342
    • (1986) EMBO J , vol.5 , pp. 1335-1342
    • von Heijne, G.1
  • 42
    • 0034687710 scopus 로고    scopus 로고
    • Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation.
    • Wieprecht T, Apostolov O, Beyermann M, Seelig J (2000) Interaction of a mitochondrial presequence with lipid membranes: role of helix formation for membrane binding and perturbation. Biochemistry 39: 15297-15305
    • (2000) Biochemistry , vol.39 , pp. 15297-15305
    • Wieprecht, T.1    Apostolov, O.2    Beyermann, M.3    Seelig, J.4
  • 44
    • 0026487057 scopus 로고
    • Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequence.
    • Zardeneta G, Horowitz PM (1992) Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequence. J Biol Chem 267: 24193-24198
    • (1992) J Biol Chem , vol.267 , pp. 24193-24198
    • Zardeneta, G.1    Horowitz, P.M.2
  • 45
    • 0036007390 scopus 로고    scopus 로고
    • Interaction of plant mitochondrial and chloroplast signal peptides with Hsp70 molecular chaperone.
    • Zhang X-P, Glaser E (2002) Interaction of plant mitochondrial and chloroplast signal peptides with Hsp70 molecular chaperone. Trends Plant Sci 7: 14-21
    • (2002) Trends Plant Sci , vol.7 , pp. 14-21
    • Zhang, X.-P.1    Glaser, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.