메뉴 건너뛰기




Volumn 1797, Issue 6-7, 2010, Pages 1071-1075

ATP-dependent proteases in biogenesis and maintenance of plant mitochondria

Author keywords

AAA protease; Arabidopsis thaliana; ATP dependent protease; Clp; FtsH; Lon; Oxidative phosphorylation; Plant mitochondria

Indexed keywords

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; ARABIDOPSIS PROTEIN; ENDOPEPTIDASE CLP; ENDOPEPTIDASE LA; PROTEIN FTSH10; PROTEIN FTSH11; PROTEIN FTSH3; PROTEIN FTSH4; PROTEIN LON 1; PROTEIN LON 4; UNCLASSIFIED DRUG;

EID: 77953743324     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.02.027     Document Type: Review
Times cited : (53)

References (47)
  • 1
    • 0036165070 scopus 로고    scopus 로고
    • Changes in chloroplast FtsH-like gene during cold acclimation in alfalfa (Medigo sativa)
    • Ivashuta S., Imai R., Uchiyama K., Gau M., Shimamoto Y. Changes in chloroplast FtsH-like gene during cold acclimation in alfalfa (Medigo sativa). J. Plant Physiol. 2001, 159:85-90.
    • (2001) J. Plant Physiol. , vol.159 , pp. 85-90
    • Ivashuta, S.1    Imai, R.2    Uchiyama, K.3    Gau, M.4    Shimamoto, Y.5
  • 2
    • 77953803050 scopus 로고    scopus 로고
    • Mitochondrial protease AtFtsH4 protects ageing Arabidopsis rosettes against oxidative damage under short-day photoperiod
    • Kicia M., Gola E.M., Janska H. Mitochondrial protease AtFtsH4 protects ageing Arabidopsis rosettes against oxidative damage under short-day photoperiod. Plant Signal. Behav. 2010, 5:126-128.
    • (2010) Plant Signal. Behav. , vol.5 , pp. 126-128
    • Kicia, M.1    Gola, E.M.2    Janska, H.3
  • 3
    • 0032124755 scopus 로고    scopus 로고
    • A cytoplasmic male sterility-associated mitochondrial peptide in common bean is post-translationally regulated
    • Sarria R., Lyznik A., Vallejos C.E., Mackenzie S.A. A cytoplasmic male sterility-associated mitochondrial peptide in common bean is post-translationally regulated. Plant Cell 1998, 10:1217-1228.
    • (1998) Plant Cell , vol.10 , pp. 1217-1228
    • Sarria, R.1    Lyznik, A.2    Vallejos, C.E.3    Mackenzie, S.A.4
  • 4
    • 0034505937 scopus 로고    scopus 로고
    • Protein degradation in mitochondria
    • Kaser M., Langer T. Protein degradation in mitochondria. Semin. Cell Dev. Biol. 2000, 11:181-190.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 181-190
    • Kaser, M.1    Langer, T.2
  • 5
    • 34250369119 scopus 로고    scopus 로고
    • Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases
    • Koppen M., Langer T. Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases. Crit. Rev. Biochem. Mol. Biol. 2007, 42:221-242.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 221-242
    • Koppen, M.1    Langer, T.2
  • 6
    • 0032698023 scopus 로고    scopus 로고
    • ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae
    • Van Dyck L., Langer T. ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae. Cell. Mol. Life Sci. 1999, 56:825-842.
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 825-842
    • Van Dyck, L.1    Langer, T.2
  • 7
    • 17444420141 scopus 로고    scopus 로고
    • ATP-dependent proteases in plant mitochondria: what do we know about them today?
    • Janska H. ATP-dependent proteases in plant mitochondria: what do we know about them today?. Physiol. Plant. 2005, 123:399-405.
    • (2005) Physiol. Plant. , vol.123 , pp. 399-405
    • Janska, H.1
  • 8
    • 0037010120 scopus 로고    scopus 로고
    • AAA+ proteins and substrate recognition, it all depends on their partner in crime
    • Dougan D.A., Mogk A., Zeth K., Turgay K., Bukau B. AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett. 2002, 529:6-10.
    • (2002) FEBS Lett. , vol.529 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 9
    • 39149135202 scopus 로고    scopus 로고
    • Protein targeting to ATP-dependent proteases
    • Inobe T., Matouschek A. Protein targeting to ATP-dependent proteases. Curr. Opin. Struct. Biol. 2008, 18:43-51.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 43-51
    • Inobe, T.1    Matouschek, A.2
  • 10
    • 39449097830 scopus 로고    scopus 로고
    • Common and specific mechanisms of AAA+ proteins involved in protein quality control
    • Mogk A., Haslberger T., Tessarz P., Bukau B. Common and specific mechanisms of AAA+ proteins involved in protein quality control. Biochem. Soc. Trans. 2008, 36:120-125.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 120-125
    • Mogk, A.1    Haslberger, T.2    Tessarz, P.3    Bukau, B.4
  • 11
    • 64549106859 scopus 로고    scopus 로고
    • Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes
    • Striebel F., Kress W., Weber-Ban E. Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes. Curr. Opin. Struct. Biol. 2009, 19:209-217.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 209-217
    • Striebel, F.1    Kress, W.2    Weber-Ban, E.3
  • 12
    • 0344211512 scopus 로고    scopus 로고
    • Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH
    • Herman C., Prakash S., Lu C.Z., Matouschek A., Gross C.A. Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Mol. Cell 2003, 11:659-669.
    • (2003) Mol. Cell , vol.11 , pp. 659-669
    • Herman, C.1    Prakash, S.2    Lu, C.Z.3    Matouschek, A.4    Gross, C.A.5
  • 13
    • 77953736348 scopus 로고    scopus 로고
    • Prohibitins and m-AAA proteases form a 2 MDa supercomplex in plant mitochondria
    • PP3-64
    • Piechota J., Kolodziejczak M., Janska H. Prohibitins and m-AAA proteases form a 2 MDa supercomplex in plant mitochondria. FEBS J. 2008, 275:227-227. PP3-64.
    • (2008) FEBS J. , vol.275 , pp. 227-227
    • Piechota, J.1    Kolodziejczak, M.2    Janska, H.3
  • 15
    • 34548417715 scopus 로고    scopus 로고
    • Multiple intracellular locations of Lon protease in Arabidopsis: evidence for the localization of AtLon4 to chloroplasts
    • Ostersetzer O., Kato Y., Adam Z., Sakamoto W. Multiple intracellular locations of Lon protease in Arabidopsis: evidence for the localization of AtLon4 to chloroplasts. Plant Cell Physiol. 2007, 48:881-885.
    • (2007) Plant Cell Physiol. , vol.48 , pp. 881-885
    • Ostersetzer, O.1    Kato, Y.2    Adam, Z.3    Sakamoto, W.4
  • 16
    • 58249113926 scopus 로고    scopus 로고
    • Role of Lon1 protease in post-germinative growth and maintenance of mitochondrial function in Arabidopsis thaliana
    • Rigas S., Daras G., Laxa M., Marathias N., Fasseas C., Sweetlove L.J., Hatzopoulos P. Role of Lon1 protease in post-germinative growth and maintenance of mitochondrial function in Arabidopsis thaliana. New Phytol. 2009, 181:588-600.
    • (2009) New Phytol. , vol.181 , pp. 588-600
    • Rigas, S.1    Daras, G.2    Laxa, M.3    Marathias, N.4    Fasseas, C.5    Sweetlove, L.J.6    Hatzopoulos, P.7
  • 17
    • 0035039711 scopus 로고    scopus 로고
    • Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease
    • Halperin T., Zheng B., Itzhaki H., Clarke A.K., Adam Z. Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease. Plant Mol. Biol. 2001, 45:461-468.
    • (2001) Plant Mol. Biol. , vol.45 , pp. 461-468
    • Halperin, T.1    Zheng, B.2    Itzhaki, H.3    Clarke, A.K.4    Adam, Z.5
  • 18
    • 33745645551 scopus 로고    scopus 로고
    • Protein degradation machineries in plastids
    • Sakamoto W. Protein degradation machineries in plastids. Annu. Rev. Plant Biol. 2006, 57:599-621.
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 599-621
    • Sakamoto, W.1
  • 19
    • 0037113870 scopus 로고    scopus 로고
    • A higher plant mitochondrial homologue of the yeast m-AAA protease. Molecular clonning, localization, and putative function
    • Kolodziejczak M., Kolaczkowska A., Szczesny B., Urantowka A., Knorpp C., Kieleczawa J., Janska H. A higher plant mitochondrial homologue of the yeast m-AAA protease. Molecular clonning, localization, and putative function. J. Biol. Chem. 2002, 277:43792-43798.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43792-43798
    • Kolodziejczak, M.1    Kolaczkowska, A.2    Szczesny, B.3    Urantowka, A.4    Knorpp, C.5    Kieleczawa, J.6    Janska, H.7
  • 20
    • 0033012642 scopus 로고    scopus 로고
    • Two nuclear-directed means of suppressing a dominant mitochondrial mutation in common bean
    • Sarria R., Janska H., Arrieta-Montiel M., Lyznik A., Mackenzie S.A. Two nuclear-directed means of suppressing a dominant mitochondrial mutation in common bean. J. Hered. 1999, 90:357-361.
    • (1999) J. Hered. , vol.90 , pp. 357-361
    • Sarria, R.1    Janska, H.2    Arrieta-Montiel, M.3    Lyznik, A.4    Mackenzie, S.A.5
  • 21
    • 0033036242 scopus 로고    scopus 로고
    • Enhanced mitochondrial biogenesis is associated with increased expression of the mitochondrial ATP-dependent Lon protease
    • Luciakova K., Sokolikova B., Chloupkova M., Nelson B.D. Enhanced mitochondrial biogenesis is associated with increased expression of the mitochondrial ATP-dependent Lon protease. FEBS Lett. 1999, 444:186-188.
    • (1999) FEBS Lett. , vol.444 , pp. 186-188
    • Luciakova, K.1    Sokolikova, B.2    Chloupkova, M.3    Nelson, B.D.4
  • 22
    • 0028049082 scopus 로고
    • PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae
    • Van Dyck L., Pearce D.A., Sherman F. PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 1994, 269:238-242.
    • (1994) J. Biol. Chem. , vol.269 , pp. 238-242
    • Van Dyck, L.1    Pearce, D.A.2    Sherman, F.3
  • 23
    • 1042289735 scopus 로고    scopus 로고
    • Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications
    • Peltier J.B., Ripoll D.R., Friso G., Rudella A., Cai Y., Ytterberg J., Giacomelli L., Pillardy J., van Wijk K.J. Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications. J. Biol. Chem. 2004, 279:4768-4781.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4768-4781
    • Peltier, J.B.1    Ripoll, D.R.2    Friso, G.3    Rudella, A.4    Cai, Y.5    Ytterberg, J.6    Giacomelli, L.7    Pillardy, J.8    van Wijk, K.J.9
  • 26
    • 13444264729 scopus 로고    scopus 로고
    • Arabidopsis microarray database and analysis toolbox
    • G.E.N.E.V.E.S.T.I.G.A.T.O.R.
    • Zimmermann P., Hirsch-Hoffmann M., Hennig L., Gruissem W. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 2004, 136:2621-2632. G.E.N.E.V.E.S.T.I.G.A.T.O.R.
    • (2004) Plant Physiol. , vol.136 , pp. 2621-2632
    • Zimmermann, P.1    Hirsch-Hoffmann, M.2    Hennig, L.3    Gruissem, W.4
  • 27
    • 33748632913 scopus 로고    scopus 로고
    • FtsH11 protease plays a critical role in Arabidopsis thermotolerance
    • Chen J., Burke J.J., Velten J., Xin Z. FtsH11 protease plays a critical role in Arabidopsis thermotolerance. Plant J. 2006, 48:73-84.
    • (2006) Plant J. , vol.48 , pp. 73-84
    • Chen, J.1    Burke, J.J.2    Velten, J.3    Xin, Z.4
  • 28
    • 70350534258 scopus 로고    scopus 로고
    • Stress responses in Prochlorococcus MIT9313 vs. SS120 involve differential expression of genes encoding proteases ClpP, FtsH and Lon
    • Gomez-Baena G., Rangel O.A., Lopez-Lozano A., Garcia-Fernandez J.M., Diez J. Stress responses in Prochlorococcus MIT9313 vs. SS120 involve differential expression of genes encoding proteases ClpP, FtsH and Lon. Res. Microbiol. 2009, 160:567-575.
    • (2009) Res. Microbiol. , vol.160 , pp. 567-575
    • Gomez-Baena, G.1    Rangel, O.A.2    Lopez-Lozano, A.3    Garcia-Fernandez, J.M.4    Diez, J.5
  • 29
    • 0141789762 scopus 로고    scopus 로고
    • Proteolysis in prokaryotes: protein quality control and regulatory principles
    • Hengge R., Bukau B. Proteolysis in prokaryotes: protein quality control and regulatory principles. Mol. Microbiol. 2003, 49:1451-1462.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1451-1462
    • Hengge, R.1    Bukau, B.2
  • 30
    • 77953802639 scopus 로고    scopus 로고
    • Identification and characterization of a heat-inducible ftsH gene from tomato (Lycopersicon esculentum Mill.)star, open
    • Sun A., Yi S., Yang Y., Zhao C., Liu J. Identification and characterization of a heat-inducible ftsH gene from tomato (Lycopersicon esculentum Mill.)star, open. Plant Sci. 2005, 170:551:562-551:562.
    • (2005) Plant Sci. , vol.170
    • Sun, A.1    Yi, S.2    Yang, Y.3    Zhao, C.4    Liu, J.5
  • 31
    • 0033639076 scopus 로고    scopus 로고
    • Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface
    • Leonhard K., Guiard B., Pellecchia G., Tzagoloff A., Neupert W., Langer T. Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface. Mol. Cell 2000, 5:629-638.
    • (2000) Mol. Cell , vol.5 , pp. 629-638
    • Leonhard, K.1    Guiard, B.2    Pellecchia, G.3    Tzagoloff, A.4    Neupert, W.5    Langer, T.6
  • 32
    • 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
    • Leonhard K., Herrmann J.M., Stuart R.A., Mannhaupt G., Neupert W., Langer T. 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. 1996, 15:4218-4229.
    • (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
  • 33
    • 29044432842 scopus 로고    scopus 로고
    • Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1
    • von Janowsky B., Knapp K., Major T., Krayl M., Guiard B., Voos W. Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1. Biol. Chem. 2005, 386:1307-1317.
    • (2005) Biol. Chem. , vol.386 , pp. 1307-1317
    • von Janowsky, B.1    Knapp, K.2    Major, T.3    Krayl, M.4    Guiard, B.5    Voos, W.6
  • 34
    • 68949215025 scopus 로고    scopus 로고
    • Translocation and assembly of mitochondrially coded Saccharomyces cerevisiae cytochrome c oxidase subunit Cox2 by Oxa1 and Yme1 in the absence of Cox18
    • Fiumera H.L., Dunham M.J., Saracco S.A., Butler C.A., Kelly J.A., Fox T.D. Translocation and assembly of mitochondrially coded Saccharomyces cerevisiae cytochrome c oxidase subunit Cox2 by Oxa1 and Yme1 in the absence of Cox18. Genetics 2009, 182:519-528.
    • (2009) Genetics , vol.182 , pp. 519-528
    • Fiumera, H.L.1    Dunham, M.J.2    Saracco, S.A.3    Butler, C.A.4    Kelly, J.A.5    Fox, T.D.6
  • 35
    • 33750986200 scopus 로고    scopus 로고
    • A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space
    • Rainey R.N., Glavin J.D., Chen H.W., French S.W., Teitell M.A., Koehler C.M. A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space. Mol. Cell. Biol. 2006, 26:8488-8497.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8488-8497
    • Rainey, R.N.1    Glavin, J.D.2    Chen, H.W.3    French, S.W.4    Teitell, M.A.5    Koehler, C.M.6
  • 36
    • 33846490396 scopus 로고    scopus 로고
    • M-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria
    • Tatsuta T., Augustin S., Nolden M., Friedrichs B., Langer T. m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J. 2007, 26:325-335.
    • (2007) EMBO J. , vol.26 , pp. 325-335
    • Tatsuta, T.1    Augustin, S.2    Nolden, M.3    Friedrichs, B.4    Langer, T.5
  • 37
    • 0036424840 scopus 로고    scopus 로고
    • A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1
    • Esser K., Tursun B., Ingenhoven M., Michaelis G., Pratje E. A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1. J. Mol. Biol. 2002, 323:835-843.
    • (2002) J. Mol. Biol. , vol.323 , pp. 835-843
    • Esser, K.1    Tursun, B.2    Ingenhoven, M.3    Michaelis, G.4    Pratje, E.5
  • 38
    • 26844484821 scopus 로고    scopus 로고
    • The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria
    • Nolden M., Ehses S., Koppen M., Bernacchia A., Rugarli E.I., Langer T. The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 2005, 123:277-289.
    • (2005) Cell , vol.123 , pp. 277-289
    • Nolden, M.1    Ehses, S.2    Koppen, M.3    Bernacchia, A.4    Rugarli, E.I.5    Langer, T.6
  • 39
    • 61949403154 scopus 로고    scopus 로고
    • The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria
    • Suppanz I.E., Wurm C.A., Wenzel D., Jakobs S. The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol. Biol. Cell 2009, 20:572-580.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 572-580
    • Suppanz, I.E.1    Wurm, C.A.2    Wenzel, D.3    Jakobs, S.4
  • 40
    • 0028362456 scopus 로고
    • Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration
    • Suzuki C.K., Suda K., Wang N., Schatz G. Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration. Science 1994, 264:891.
    • (1994) Science , vol.264 , pp. 891
    • Suzuki, C.K.1    Suda, K.2    Wang, N.3    Schatz, G.4
  • 41
    • 69249129473 scopus 로고    scopus 로고
    • The lack of mitochondrial AtFtsH4 protease alters Arabidopsis leaf morphology at the late stage of rosette development under short-day photoperiod
    • Gibala M., Kicia M., Sakamoto W., Gola E.M., Kubrakiewicz J., Smakowska E., Janska H. The lack of mitochondrial AtFtsH4 protease alters Arabidopsis leaf morphology at the late stage of rosette development under short-day photoperiod. Plant J. 2009, 59:685-699.
    • (2009) Plant J. , vol.59 , pp. 685-699
    • Gibala, M.1    Kicia, M.2    Sakamoto, W.3    Gola, E.M.4    Kubrakiewicz, J.5    Smakowska, E.6    Janska, H.7
  • 42
    • 0032493810 scopus 로고    scopus 로고
    • ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system
    • Savel'ev A.S., Novikova L.A., Kovaleva I.E., Luzikov V.N., Neupert W., Langer T. ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system. J. Biol. Chem. 1998, 273:20596-20602.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20596-20602
    • Savel'ev, A.S.1    Novikova, L.A.2    Kovaleva, I.E.3    Luzikov, V.N.4    Neupert, W.5    Langer, T.6
  • 43
    • 1642278051 scopus 로고    scopus 로고
    • The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes
    • Yu F., Park S., Rodermel S.R. The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes. Plant J. 2004, 37:864-876.
    • (2004) Plant J. , vol.37 , pp. 864-876
    • Yu, F.1    Park, S.2    Rodermel, S.R.3
  • 44
    • 33644874521 scopus 로고    scopus 로고
    • Two types of FtsH protease subunits are required for chloroplast biogenesis and Photosystem II repair in Arabidopsis
    • Zaltsman A., Ori N., Adam Z. Two types of FtsH protease subunits are required for chloroplast biogenesis and Photosystem II repair in Arabidopsis. Plant Cell 2005, 17:2782-2790.
    • (2005) Plant Cell , vol.17 , pp. 2782-2790
    • Zaltsman, A.1    Ori, N.2    Adam, Z.3
  • 45
    • 33845642214 scopus 로고    scopus 로고
    • The significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes
    • Kolodziejczak M., Gibala M., Urantowka A., Janska H. The significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes. Physiol. Plantarum 2007, 129:135-142.
    • (2007) Physiol. Plantarum , vol.129 , pp. 135-142
    • Kolodziejczak, M.1    Gibala, M.2    Urantowka, A.3    Janska, H.4
  • 46
    • 2542431031 scopus 로고    scopus 로고
    • Progression and specificity of protein oxidation in the life cycle of Arabidopsis thaliana
    • Johansson E., Olsson O., Nystrom T. Progression and specificity of protein oxidation in the life cycle of Arabidopsis thaliana. J. Biol. Chem. 2004, 279:22204-22208.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22204-22208
    • Johansson, E.1    Olsson, O.2    Nystrom, T.3
  • 47
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota D.A., Davies K.J. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 2002, 4:674-680.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.