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Volumn 5, Issue APR, 2014, Pages

Evolution and significance of the Lon gene family in Arabidopsis organelle biogenesis and energy metabolism

Author keywords

Chloroplasts; Energy metabolism; Gene evolution; Gene expression; Lon; Mitochondria; Molecular modeling; Protein dual targeting

Indexed keywords


EID: 84901056356     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2014.00145     Document Type: Review
Times cited : (22)

References (56)
  • 1
    • 0035027728 scopus 로고    scopus 로고
    • Chloroplast and mitochondrial proteases in Arabidopsis. A proposed nomenclature
    • doi: 10.1104/pp.125.4.1912
    • Adam, Z., Adamska, I., Nakabayashi, K., Ostersetzer, O., Haussuhl, K., Manuell, A., et al. (2001). Chloroplast and mitochondrial proteases in Arabidopsis. A proposed nomenclature. Plant Physiol. 125, 1912-1918. doi: 10.1104/pp.125.4.1912
    • (2001) Plant Physiol. , vol.125 , pp. 1912-1918
    • Adam, Z.1    Adamska, I.2    Nakabayashi, K.3    Ostersetzer, O.4    Haussuhl, K.5    Manuell, A.6
  • 2
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: Metabolism, oxidative stress and signal transduction
    • doi: 10.1146/annurev.arplant.55.031903.141701
    • Apel, K., and Hirt, H. (2004). Reactive oxygen species: metabolism, oxidative stress and signal transduction. Annu. Rev. Plant Biol. 55, 373-399. doi: 10.1146/annurev.arplant.55.031903.141701
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 3
    • 84888291402 scopus 로고    scopus 로고
    • The exception proves the rule? Dual targeting of nuclear-encoded proteins into endosymbiotic organelles
    • doi: 10.1111/nph.12482
    • Baudisch, B., Langner, U., Garz, I., and Klösgen, R. B. (2014). The exception proves the rule? Dual targeting of nuclear-encoded proteins into endosymbiotic organelles. New Phytol. 201, 80-90. doi: 10.1111/nph.12482
    • (2014) New Phytol. , vol.201 , pp. 80-90
    • Baudisch, B.1    Langner, U.2    Garz, I.3    Klösgen, R.B.4
  • 4
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman, K. B., and Ames, B. N. (1998). The free radical theory of aging matures. Physiol. Rev. 78, 547-581.
    • (1998) Physiol. Rev. , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 5
    • 70349804290 scopus 로고    scopus 로고
    • Defining the determinants for dual targeting of amino acyl-tRNA synthetases to mitochondria and chloroplasts
    • doi: 10.1016/j.jmb.2009.08.072
    • Berglund, A. K., Pujol, C., Duchene, A. M., and Glaser, E. (2009a). Defining the determinants for dual targeting of amino acyl-tRNA synthetases to mitochondria and chloroplasts. J. Mol. Biol. 393, 803-814. doi: 10.1016/j.jmb.2009.08.072
    • (2009) J. Mol. Biol. , vol.393 , pp. 803-814
    • Berglund, A.K.1    Pujol, C.2    Duchene, A.M.3    Glaser, E.4
  • 6
    • 71249108997 scopus 로고    scopus 로고
    • Dual targeting to mitochondria and chloroplasts: Characterization of Thr-tRNA synthetase targeting peptide
    • doi: 10.1093/mp/ssp048
    • Berglund, A. K., Spånning, E., Biverståhl, H., Maddalo, G., Tellgren-Roth, C., Mäler, L., et al. (2009b). Dual targeting to mitochondria and chloroplasts: characterization of Thr-tRNA synthetase targeting peptide. Mol. Plant 2, 1298-1309. doi: 10.1093/mp/ssp048
    • (2009) Mol. Plant , vol.2 , pp. 1298-1309
    • Berglund, A.K.1    Spånning, E.2    Biverståhl, H.3    Maddalo, G.4    Tellgren-Roth, C.5    Mäler, L.6
  • 7
    • 15744384860 scopus 로고    scopus 로고
    • Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death
    • doi: 10.1016/j.freeradbiomed.2004.11.017
    • Bota, D. A., Ngo, J. K., and Davies, K. J. (2005). Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death. Free Radic. Biol. Med. 38, 665-677. doi: 10.1016/j.freeradbiomed.2004.11.017
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 665-677
    • Bota, D.A.1    Ngo, J.K.2    Davies, K.J.3
  • 8
    • 10744225162 scopus 로고    scopus 로고
    • The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
    • doi: 10.1074/jbc.M312243200
    • Botos, I., Melnikov, E. E., Cherry, S., Tropea, J. E., Khalatova, A. G., Rasulova, F., et al. (2004). The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site. J. Biol. Chem. 279, 8140-8148. doi: 10.1074/jbc.M312243200
    • (2004) J. Biol. Chem. , vol.279 , pp. 8140-8148
    • Botos, I.1    Melnikov, E.E.2    Cherry, S.3    Tropea, J.E.4    Khalatova, A.G.5    Rasulova, F.6
  • 9
    • 60349127044 scopus 로고    scopus 로고
    • Protein transport in organelles: Dual targeting of proteins to mitochondria and chloroplasts
    • doi: 10.1111/j.1742-4658.2009.06876.x
    • Carrie, C., Giraud, E., and Whelan, J. (2009). Protein transport in organelles: dual targeting of proteins to mitochondria and chloroplasts. FEBS J. 276, 1187-1195. doi: 10.1111/j.1742-4658.2009.06876.x
    • (2009) FEBS J. , vol.276 , pp. 1187-1195
    • Carrie, C.1    Giraud, E.2    Whelan, J.3
  • 10
    • 84871779194 scopus 로고    scopus 로고
    • A reevaluation of dual-targeting of proteins to mitochondria and chloroplasts
    • doi: 10.1016/j.bbamcr.2012.05.029
    • Carrie, C., and Small, I. (2013). A reevaluation of dual-targeting of proteins to mitochondria and chloroplasts. Biochim. Biophys. Acta 1833, 253-259. doi: 10.1016/j.bbamcr.2012.05.029
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 253-259
    • Carrie, C.1    Small, I.2
  • 11
    • 77958477536 scopus 로고    scopus 로고
    • Crystal structure of Lon protease: Molecular architecture of gated entry to a sequestered degradation chamber
    • doi: 10.1038/emboj.2010.226
    • Cha, S. S., An, Y. J., Lee, C. R., Lee, H. S., Kim, Y. G., Kim, S. J., et al. (2010). Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber. EMBO J. 29, 3520-3530. doi: 10.1038/emboj.2010.226
    • (2010) EMBO J. , vol.29 , pp. 3520-3530
    • Cha, S.S.1    An, Y.J.2    Lee, C.R.3    Lee, H.S.4    Kim, Y.G.5    Kim, S.J.6
  • 12
    • 0013533949 scopus 로고
    • The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La
    • doi: 10.1073/pnas.78.8.4931
    • Chung, C. H., and Goldberg, A. L. (1981). The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc. Natl. Acad. Sci. U.S.A. 78, 4931-4935. doi: 10.1073/pnas.78.8.4931
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4931-4935
    • Chung, C.H.1    Goldberg, A.L.2
  • 13
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • doi: 10.1146/annurev.bi.65.070196.004101
    • Coux, O., Tanaka, K., and Goldberg, A. L. (1996). Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847. doi: 10.1146/annurev.bi.65.070196.004101
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 14
    • 0029015912 scopus 로고
    • How can the products of a single gene be localized to more than one intracellular compartment?
    • doi: 10.1016/S0962-8924(00)89016-9
    • Danpure, C. J. (1995). How can the products of a single gene be localized to more than one intracellular compartment? Trends Cell Biol. 5, 230-238. doi: 10.1016/S0962-8924(00)89016-9
    • (1995) Trends Cell Biol. , vol.5 , pp. 230-238
    • Danpure, C.J.1
  • 15
    • 84901017612 scopus 로고    scopus 로고
    • Alternative transcription initiation and the AUG context configuration control dual organellar targeting and functional competence of Arabidopsis Lon1 protease
    • doi: 10.1093/mp/ssu030 [Epub ahead of print]
    • Daras, G., Rigas, S., Tsitsekian, D., Zur, H., Tuller, T., and Hatzopoulos, P. (2014). Alternative transcription initiation and the AUG context configuration control dual organellar targeting and functional competence of Arabidopsis Lon1 protease. Mol. Plant doi: 10.1093/mp/ssu030 [Epub ahead of print].
    • (2014) Mol. Plant
    • Daras, G.1    Rigas, S.2    Tsitsekian, D.3    Zur, H.4    Tuller, T.5    Hatzopoulos, P.6
  • 16
    • 0029439509 scopus 로고
    • Oxidative stress: The paradox of aerobic life
    • Davies, K. J. (1995). Oxidative stress: the paradox of aerobic life. Biochem. Soc. Symp. 61, 1-31.
    • (1995) Biochem. Soc. Symp. , vol.61 , pp. 1-31
    • Davies, K.J.1
  • 17
    • 0034705167 scopus 로고    scopus 로고
    • Protein oxidation in response to increased transcriptional or translational errors
    • doi: 10.1073/pnas.100422497
    • Dukan, S., Farewell, A., Ballesteros, M., Taddei, F., Radman, M., and Nyström, T. (2000). Protein oxidation in response to increased transcriptional or translational errors. Proc. Natl. Acad. Sci. U.S.A. 97, 5746-5749. doi: 10.1073/pnas.100422497
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5746-5749
    • Dukan, S.1    Farewell, A.2    Ballesteros, M.3    Taddei, F.4    Radman, M.5    Nyström, T.6
  • 18
    • 1842429937 scopus 로고    scopus 로고
    • Ancient invasions: From endosymbionts to organelles
    • doi: 10.1126/science.1094884
    • Dyall, S. D., Brown, M. T., and Johnson, P. J. (2004). Ancient invasions: from endosymbionts to organelles. Science 304, 253-257. doi: 10.1126/science.1094884
    • (2004) Science , vol.304 , pp. 253-257
    • Dyall, S.D.1    Brown, M.T.2    Johnson, P.J.3
  • 19
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • doi: 10.1038/35041687
    • Finkel, T., and Holbrook, N. J. (2000). Oxidants, oxidative stress and the biology of ageing. Nature 408, 239-247. doi: 10.1038/35041687
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 20
    • 48949119155 scopus 로고    scopus 로고
    • Mitochondrial protein quality control: Implications in ageing
    • doi: 10.1002/biot.200800041
    • Friguet, B., Bulteau, A. L., and Petropoulos, I. (2008). Mitochondrial protein quality control: implications in ageing. Biotechnol. J. 3, 757-764. doi: 10.1002/biot.200800041
    • (2008) Biotechnol. J. , vol.3 , pp. 757-764
    • Friguet, B.1    Bulteau, A.L.2    Petropoulos, I.3
  • 21
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • doi: 10.1016/j.cell.2007.01.047
    • Fukuda, R., Zhang, H., Kim, J. W., Shimoda, L., Dang, C. V., and Semenza, G. L. (2007). HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. Cell 129, 111-122. doi: 10.1016/j.cell.2007.01.047
    • (2007) Cell , vol.129 , pp. 111-122
    • Fukuda, R.1    Zhang, H.2    Kim, J.W.3    Shimoda, L.4    Dang, C.V.5    Semenza, G.L.6
  • 22
    • 84891758047 scopus 로고    scopus 로고
    • Import determinants of organelle-specific and dual targeting peptides of mitochondria and chloroplasts in Arabidopsis thaliana
    • doi: 10.1093/mp/sst148
    • Ge, C., Spånning, E., Glaser, E., and Wieslander, A. (2014). Import determinants of organelle-specific and dual targeting peptides of mitochondria and chloroplasts in Arabidopsis thaliana. Mol. Plant 7, 121-136. doi: 10.1093/mp/sst148
    • (2014) Mol. Plant , vol.7 , pp. 121-136
    • Ge, C.1    Spånning, E.2    Glaser, E.3    Wieslander, A.4
  • 23
    • 50049083221 scopus 로고    scopus 로고
    • Recognition of misfolded proteins by Lon, a AAA+ protease
    • doi: 10.1101/gad.1670908
    • Gur, E., and Sauer, R. T. (2008). Recognition of misfolded proteins by Lon, a AAA+ protease. Genes Dev. 22, 2267-2277. doi: 10.1101/gad.1670908
    • (2008) Genes Dev. , vol.22 , pp. 2267-2277
    • Gur, E.1    Sauer, R.T.2
  • 24
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • doi: 10.1093/geronj/11.3.298
    • Harman, D. (1956). Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 11, 298-300. doi: 10.1093/geronj/11.3.298
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 25
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • doi: 10.1146/annurev.biochem.67.1.425
    • Hershko, A., and Ciechanover, A. (1998). The ubiquitin system. Annu. Rev. Biochem. 67, 425-479. doi: 10.1146/annurev.biochem.67.1.425
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 26
    • 18444390287 scopus 로고    scopus 로고
    • Transmission of cell stress from endoplasmic reticulum to mitochondria: Enhanced expression of Lon protease
    • doi: 10.1083/jcb.200108103
    • Hori, O., Ichinoda, F., Tamatani, T., Yamaguchi, A., Sato, N., Ozawa, K., et al. (2002). Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease. J. Cell Biol. 157, 1151-1160. doi: 10.1083/jcb.200108103
    • (2002) J. Cell Biol. , vol.157 , pp. 1151-1160
    • Hori, O.1    Ichinoda, F.2    Tamatani, T.3    Yamaguchi, A.4    Sato, N.5    Ozawa, K.6
  • 27
    • 58749109023 scopus 로고    scopus 로고
    • Genevestigator V3: A reference expression database for the meta-analysis of transcriptomes
    • doi: 10.1155/2008/420747
    • Hruz, T., Laule, O., Szabo, G., Wessendorp, F., Bleuler, S., Oertle, L., et al. (2008). Genevestigator V3: a reference expression database for the meta-analysis of transcriptomes. Adv. Bioinformatics 2008;420747. doi: 10.1155/2008/420747
    • (2008) Adv. Bioinformatics 2008 , pp. 420747
    • Hruz, T.1    Laule, O.2    Szabo, G.3    Wessendorp, F.4    Bleuler, S.5    Oertle, L.6
  • 28
    • 84871729535 scopus 로고    scopus 로고
    • Protein quality control in organelles-AAA/FtsH story
    • doi: 10.1016/j.bbamcr.2012.03.016
    • Janska, H., Kwasniak, M., and Szczepanowska, J. (2013). Protein quality control in organelles-AAA/FtsH story. Biochim. Biophys. Acta 1833, 381-387. doi: 10.1016/j.bbamcr.2012.03.016
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 381-387
    • Janska, H.1    Kwasniak, M.2    Szczepanowska, J.3
  • 29
    • 77953743324 scopus 로고    scopus 로고
    • ATP-dependent proteases in biogenesis and maintenance of plant mitochondria
    • doi: 10.1016/j.bbabio.2010.02.027
    • Janska, H., Piechota, J., and Kwasniak, M. (2010). ATP-dependent proteases in biogenesis and maintenance of plant mitochondria. Biochim. Biophys. Acta 1797, 1071-1075. doi: 10.1016/j.bbabio.2010.02.027
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1071-1075
    • Janska, H.1    Piechota, J.2    Kwasniak, M.3
  • 30
    • 70350633819 scopus 로고    scopus 로고
    • Arabidopsis LON2 is necessary for peroxisomal function and sustained matrix protein import
    • doi: 10.1104/pp.109.142505
    • Lingard, M. J., and Bartel, B. (2009). Arabidopsis LON2 is necessary for peroxisomal function and sustained matrix protein import. Plant Physiol. 151, 1354-1365. doi: 10.1104/pp.109.142505
    • (2009) Plant Physiol. , vol.151 , pp. 1354-1365
    • Lingard, M.J.1    Bartel, B.2
  • 31
    • 0034634395 scopus 로고    scopus 로고
    • The evolutionary fate and consequences of duplicate genes
    • doi: 10.1126/science.290.5494.1151
    • Lynch, M., and Conery, J. S. (2000). The evolutionary fate and consequences of duplicate genes. Science 290, 1151-1155. doi: 10.1126/science.290.5494.1151
    • (2000) Science , vol.290 , pp. 1151-1155
    • Lynch, M.1    Conery, J.S.2
  • 32
    • 25844434373 scopus 로고    scopus 로고
    • Plant organellar protein targeting: A traffic plan still under construction
    • doi: 10.1016/j.tcb.2005.08.007
    • Mackenzie, S. A. (2005). Plant organellar protein targeting: a traffic plan still under construction. Trends Cell Biol. 15, 548-554. doi: 10.1016/j.tcb.2005.08.007
    • (2005) Trends Cell Biol. , vol.15 , pp. 548-554
    • McKenzie, S.A.1
  • 33
    • 33749624260 scopus 로고    scopus 로고
    • Recent surprises in protein targeting to mitochondria and plastids
    • doi: 10.1016/j.pbi.2006.09.002
    • Millar, A. H., Whelan, J., and Small, I. (2006). Recent surprises in protein targeting to mitochondria and plastids. Curr. Opin. Plant Biol. 9, 610-615. doi: 10.1016/j.pbi.2006.09.002
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 610-615
    • Millar, A.H.1    Whelan, J.2    Small, I.3
  • 34
    • 34250849635 scopus 로고    scopus 로고
    • Oxidative modifications to cellular components in plants
    • doi: 10.1146/annurev.arplant.58.032806.103946
    • Møller, I. M., Jensen, P. E., and Hansson, A. (2007). Oxidative modifications to cellular components in plants. Annu. Rev. Plant Biol. 58, 459-481. doi: 10.1146/annurev.arplant.58.032806.103946
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 459-481
    • Møller, I.M.1    Jensen, P.E.2    Hansson, A.3
  • 35
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • doi: 10.1126/science.1223560
    • Nargund, A. M., Pellegrino, M. W., Fiorese, C. J., Baker, B. M., and Haynes, C. M. (2012). Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337, 587-590. doi: 10.1126/science.1223560
    • (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
  • 36
    • 21644454699 scopus 로고    scopus 로고
    • Cleavage site selection within a folded substrate by the ATP-dependent lon protease
    • doi: 10.1074/jbc.M502796200
    • Ondrovicová, G., Liu, T., Singh, K., Tian, B., Li, H., Gakh, O., et al. (2005). Cleavage site selection within a folded substrate by the ATP-dependent lon protease. J. Biol. Chem. 280, 25103-25110. doi: 10.1074/jbc.M502796200
    • (2005) J. Biol. Chem. , vol.280 , pp. 25103-25110
    • Ondrovicová, G.1    Liu, T.2    Singh, K.3    Tian, B.4    Li, H.5    Gakh, O.6
  • 37
    • 34548417715 scopus 로고    scopus 로고
    • Multiple intracellular locations of Lon protease in Arabidopsis: Evidence for the localization of AtLon4 to chloroplasts
    • doi: 10.1093/pcp/pcm052
    • Ostersetzer, O., Kato, Y., Adam, Z., and Sakamoto, W. (2007). Multiple intracellular locations of Lon protease in Arabidopsis: evidence for the localization of AtLon4 to chloroplasts. Plant Cell Physiol. 48, 881-885. doi: 10.1093/pcp/pcm052
    • (2007) Plant Cell Physiol. , vol.48 , pp. 881-885
    • Ostersetzer, O.1    Kato, Y.2    Adam, Z.3    Sakamoto, W.4
  • 38
    • 0035852247 scopus 로고    scopus 로고
    • Dual targeting to mitochondria and chloroplasts
    • doi: 10.1016/S0167-4889(01)00146-X
    • Peeters, N., and Small, I. (2001). Dual targeting to mitochondria and chloroplasts. Biochim. Biophys. Acta 1541, 54-63. doi: 10.1016/S0167-4889(01)00146-X
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 54-63
    • Peeters, N.1    Small, I.2
  • 39
    • 33750719563 scopus 로고    scopus 로고
    • Maintenance of proteins and aging: The role of oxidized protein repair
    • doi: 10.1080/10715760600917144
    • Petropoulos, I., and Friguet, B. (2006). Maintenance of proteins and aging: the role of oxidized protein repair. Free Radic. Res. 40, 1269-1276. doi: 10.1080/10715760600917144
    • (2006) Free Radic. Res. , vol.40 , pp. 1269-1276
    • Petropoulos, I.1    Friguet, B.2
  • 40
    • 58249113926 scopus 로고    scopus 로고
    • The role of Lon1 protease in post-germinative growth and maintenance of mitochondrial function in Arabidopsis thaliana
    • doi: 10.1111/j.1469-8137.2008.02701.x
    • Rigas, S., Daras, G., Laxa, M., Marathias, N., Fasseas, C., Sweetlove, L. J., et al. (2009a). The role of Lon1 protease in post-germinative growth and maintenance of mitochondrial function in Arabidopsis thaliana. New Phytol. 181, 588-600. doi: 10.1111/j.1469-8137.2008.02701.x
    • (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
  • 41
    • 62549130681 scopus 로고    scopus 로고
    • Mitochondria biogenesis via Lon1 selective proteolysis: Who dares to live for ever?
    • doi: 10.4161/psb.4.3.7863
    • Rigas, S., Daras, G., Sweetlove, L. J., and Hatzopoulos, P. (2009b). Mitochondria biogenesis via Lon1 selective proteolysis: who dares to live for ever? Plant Signal. Behav. 4, 221-224. doi: 10.4161/psb.4.3.7863
    • (2009) Plant Signal. Behav. , vol.4 , pp. 221-224
    • Rigas, S.1    Daras, G.2    Sweetlove, L.J.3    Hatzopoulos, P.4
  • 42
    • 84859875666 scopus 로고    scopus 로고
    • The multifaceted role of Lon proteolysis in seedling establishment and maintenance of plant organelle function: Living from protein destruction
    • doi: 10.1111/j.1399-3054.2011.01537.x
    • Rigas, S., Daras, G., Tsitsekian, D., and Hatzopoulos, P. (2012). The multifaceted role of Lon proteolysis in seedling establishment and maintenance of plant organelle function: living from protein destruction. Physiol. Plant. 145, 215-223. doi: 10.1111/j.1399-3054.2011.01537.x
    • (2012) Physiol. Plant. , vol.145 , pp. 215-223
    • Rigas, S.1    Daras, G.2    Tsitsekian, D.3    Hatzopoulos, P.4
  • 43
    • 33746578414 scopus 로고    scopus 로고
    • Slicing a protease: Structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains
    • doi: 10.1110/ps.052069306
    • Rotanova, T. V., Botos, I., Melnikov, E. E., Rasulova, F., Gustchina, A., Maurizi, M. R., et al. (2006). Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains. Protein Sci. 15, 1815-1828. doi: 10.1110/ps.052069306
    • (2006) Protein Sci. , vol.15 , pp. 1815-1828
    • Rotanova, T.V.1    Botos, I.2    Melnikov, E.E.3    Rasulova, F.4    Gustchina, A.5    Maurizi, M.R.6
  • 44
    • 33745645551 scopus 로고    scopus 로고
    • Protein degradation machineries in plastids
    • doi: 10.1146/annurev.arplant.57.032905.105401
    • Sakamoto, W. (2006). Protein degradation machineries in plastids. Annu. Rev. Plant Biol. 57, 599-621. doi: 10.1146/annurev.arplant.57.032905.105401
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 599-621
    • Sakamoto, W.1
  • 45
    • 0344962439 scopus 로고    scopus 로고
    • One ticket for multiple destinations: Dual targeting of proteins to distinct subcellular locations
    • doi: 10.1016/j.pbi.2003.09.008
    • Silva-Filho, M. C. (2003). One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations. Curr. Opin. Plant Biol. 6, 589-595. doi: 10.1016/j.pbi.2003.09.008
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 589-595
    • Silva-Filho, M.C.1
  • 46
    • 3543046184 scopus 로고    scopus 로고
    • Expression in multigene families. Analysis of chloroplast and mitochondrial proteases
    • doi: 10.1104/pp.104.043299
    • Sinvany-Villalobo, G., Davydov, O., Ben-Ari, G., Zaltsman, A., Raskind, A., and Adam, Z. (2004). Expression in multigene families. Analysis of chloroplast and mitochondrial proteases. Plant Physiol. 135, 1336-1345. doi: 10.1104/pp.104.043299
    • (2004) Plant Physiol. , vol.135 , pp. 1336-1345
    • Sinvany-Villalobo, G.1    Davydov, O.2    Ben-Ari, G.3    Zaltsman, A.4    Raskind, A.5    Adam, Z.6
  • 47
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26S proteasome proteolytic pathway
    • doi: 10.1146/annurev.arplant.55.031903.141801
    • Smalle, J., and Vierstra, R. D. (2004). The ubiquitin 26S proteasome proteolytic pathway. Annu. Rev. Plant Biol. 55, 555-590. doi: 10.1146/annurev.arplant.55.031903.141801
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 555-590
    • Smalle, J.1    Vierstra, R.D.2
  • 48
    • 84868316157 scopus 로고    scopus 로고
    • Loss of Lon1 in Arabidopsis changes the mitochondrial proteome leading to altered metabolite profiles and growth retardation without an accumulation of oxidative damage
    • doi: 10.1104/pp.112.203711
    • Solheim, C., Li, L., Hatzopoulos, P., and Millar, A. H. (2012). Loss of Lon1 in Arabidopsis changes the mitochondrial proteome leading to altered metabolite profiles and growth retardation without an accumulation of oxidative damage. Plant Physiol. 160, 1187-1203. doi: 10.1104/pp.112.203711
    • (2012) Plant Physiol. , vol.160 , pp. 1187-1203
    • Solheim, C.1    Li, L.2    Hatzopoulos, P.3    Millar, A.H.4
  • 49
    • 0033536010 scopus 로고    scopus 로고
    • Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits
    • doi: 10.1073/pnas.96.12.6787
    • Stahlberg, H., Kutejová, E., Suda, K., Wolpensinger, B., Lustig, A., Schatz, G., et al. (1999). Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits. Proc. Natl. Acad. Sci. U.S.A. 96, 6787-6790. doi: 10.1073/pnas.96.12.6787
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6787-6790
    • Stahlberg, H.1    Kutejová, E.2    Suda, K.3    Wolpensinger, B.4    Lustig, A.5    Schatz, G.6
  • 50
    • 0028362456 scopus 로고
    • Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration
    • doi: 10.1126/science.8146662
    • Suzuki, C. K., Suda, K., Wang, N., and Schatz, G. (1994). Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration. Science 264, 273-276. doi: 10.1126/science.8146662
    • (1994) Science , vol.264 , pp. 273-276
    • Suzuki, C.K.1    Suda, K.2    Wang, N.3    Schatz, G.4
  • 51
    • 0019862897 scopus 로고
    • E. coli contains eight soluble proteolytic activities, one being ATP dependent
    • doi: 10.1038/292652a0
    • Swamy, K. H., and Goldberg, A. L. (1981). E. coli contains eight soluble proteolytic activities, one being ATP dependent. Nature 292, 652-654. doi: 10.1038/292652a0
    • (1981) Nature , vol.292 , pp. 652-654
    • Swamy, K.H.1    Goldberg, A.L.2
  • 52
    • 84855225838 scopus 로고    scopus 로고
    • Multitasking in the mitochondrion by the ATP-dependent Lon protease
    • doi: 10.1016/j.bbamcr.2011.11.003
    • Venkatesh, S., Lee, J., Singh, K., Lee, I., and Suzuki, C. K. (2012). Multitasking in the mitochondrion by the ATP-dependent Lon protease. Biochim. Biophys. Acta 1823, 56-66. doi: 10.1016/j.bbamcr.2011.11.003
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 56-66
    • Venkatesh, S.1    Lee, J.2    Singh, K.3    Lee, I.4    Suzuki, C.K.5
  • 53
    • 84878450345 scopus 로고    scopus 로고
    • Distinct quaternary structures of the AAA+ Lon protease control substrate degradation
    • doi: 10.1073/pnas.1307066110
    • Vieux, E. F., Wohlever, M. L., Chen, J. Z., Sauer, R. T., and Baker, T. A. (2013). Distinct quaternary structures of the AAA+ Lon protease control substrate degradation. Proc. Natl. Acad. Sci. U.S.A. 110, E2002-E2008. doi: 10.1073/pnas.1307066110
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110
    • Vieux, E.F.1    Wohlever, M.L.2    Chen, J.Z.3    Sauer, R.T.4    Baker, T.A.5
  • 54
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • doi: 10.1146/annurev.biochem.68.1.1015
    • Voges, D., Zwickl, P., and Baumeister, W. (1999). The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015-1068. doi: 10.1146/annurev.biochem.68.1.1015
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 55
    • 29044432842 scopus 로고    scopus 로고
    • Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1
    • doi: 10.1515/BC.2005.149
    • von Janowsky, B., Knapp, K., Major, T., Krayl, M., Guiard, B., and Voos, W. (2005). Structural properties of substrate proteins determine their proteolysis by the mitochondrial AAA+ protease Pim1. Biol. Chem. 386, 1307-1317. doi: 10.1515/BC.2005.149
    • (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
  • 56
    • 84871793725 scopus 로고    scopus 로고
    • Chaperone-protease networks in mitochondrial protein homeostasis
    • doi: 10.1016/j.bbamcr.2012.06.005
    • Voos, W. (2013). Chaperone-protease networks in mitochondrial protein homeostasis. Biochim. Biophys. Acta 1833, 388-399. doi: 10.1016/j.bbamcr.2012.06.005
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 388-399
    • Voos, W.1


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