메뉴 건너뛰기




Volumn 24, Issue 12, 2013, Pages 5037-5057

Mitochondrial targeting of the Arabidopsis F1-ATPase γ-subunit via multiple compensatory and synergistic presequence motifs

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84873052925     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.112.105361     Document Type: Article
Times cited : (24)

References (57)
  • 1
    • 0034598904 scopus 로고    scopus 로고
    • Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
    • Abe, Y., Shodai, T., Muto, T., Mihara, K., Torii, H., Nishikawa, S., Endo, T., and Kohda, D. (2000). Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell 100: 551-560.
    • (2000) Cell , vol.100 , pp. 551-560
    • Abe, Y.1    Shodai, T.2    Muto, T.3    Mihara, K.4    Torii, H.5    Nishikawa, S.6    Endo, T.7    Kohda, D.8
  • 2
    • 0242437931 scopus 로고    scopus 로고
    • Discrete mutations in the presequence of potato formate dehydrogenase inhibit the in vivo targeting of GFP fusions into mitochondria
    • Ambard-Bretteville, F., Small, I., Grandjean, O., and Colas des Francs-Small, C. (2003). Discrete mutations in the presequence of potato formate dehydrogenase inhibit the in vivo targeting of GFP fusions into mitochondria. Biochem. Biophys. Res. Commun. 311: 966-971.
    • (2003) Biochem. Biophys. Res. Commun , vol.311 , pp. 966-971
    • Ambard-Bretteville, F.1    Small, I.2    Grandjean, O.3    Colas des Francs-Small, C.4
  • 3
    • 38849157710 scopus 로고    scopus 로고
    • AKR2A-mediated import of chloroplast outer membrane proteins is essential for chloroplast biogenesis
    • Bae, W., Lee, Y.J., Kim, D.H., Lee, J., Kim, S., Sohn, E.J., and Hwang, I. (2008). AKR2A-mediated import of chloroplast outer membrane proteins is essential for chloroplast biogenesis. Nat. Cell Biol. 10: 220-227.
    • (2008) Nat. Cell Biol , vol.10 , pp. 220-227
    • Bae, W.1    Lee, Y.J.2    Kim, D.H.3    Lee, J.4    Kim, S.5    Sohn, E.J.6    Hwang, I.7
  • 4
    • 70349331195 scopus 로고    scopus 로고
    • Protein import machineries in endosymbiotic organelles
    • Balsera, M., Soll, J., and Bölter, B. (2009). Protein import machineries in endosymbiotic organelles. Cell. Mol. Life Sci. 66: 1903-1923.
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 1903-1923
    • Balsera, M.1    Soll, J.2    Bölter, B.3
  • 5
    • 0001777212 scopus 로고    scopus 로고
    • Protein translocation into mitochondria: The role of TIM complexes
    • Bauer, M.F., Hofmann, S., Neupert, W., and Brunner, M. (2000). Protein translocation into mitochondria: The role of TIM complexes. Trends Cell Biol. 10: 25-31.
    • (2000) Trends Cell Biol , vol.10 , pp. 25-31
    • Bauer, M.F.1    Hofmann, S.2    Neupert, W.3    Brunner, M.4
  • 6
    • 0040610676 scopus 로고    scopus 로고
    • Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein
    • Brix, J., Rüdiger, S., Bukau, B., Schneider-Mergener, J., and Pfanner, N. (1999). Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. J. Biol. Chem. 274: 16522-16530.
    • (1999) J. Biol. Chem , vol.274 , pp. 16522-16530
    • Brix, J.1    Rüdiger, S.2    Bukau, B.3    Schneider-Mergener, J.4    Pfanner, N.5
  • 7
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska, A., Koehler, C.M., Milenkovic, D., Lithgow, T., and Pfanner, N. (2009). Importing mitochondrial proteins: Machineries and mechanisms. Cell 138: 628-644.
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 8
    • 0038575101 scopus 로고    scopus 로고
    • Investigations on the in vitro import ability of mitochondrial precursor proteins synthesized in wheat germ transcription-translation extract
    • Dessi, P., Pavlov, P.F., Wållberg, F., Rudhe, C., Brack, S., Whelan, J., and Glaser, E. (2003). Investigations on the in vitro import ability of mitochondrial precursor proteins synthesized in wheat germ transcription-translation extract. Plant Mol. Biol. 52: 259-271.
    • (2003) Plant Mol. Biol , vol.52 , pp. 259-271
    • Dessi, P.1    Pavlov, P.F.2    Wållberg, F.3    Rudhe, C.4    Brack, S.5    Whelan, J.6    Glaser, E.7
  • 9
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal, P., Likic, V., Tachezy, J., and Lithgow, T. (2006). Evolution of the molecular machines for protein import into mitochondria. Science 313: 314-318.
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 10
    • 0034796437 scopus 로고    scopus 로고
    • Hydrophobic residues within the predicted N-terminal amphiphilic a-helix of a plant mitochondrial targeting presequence play a major role in in vivo import
    • Duby, G., Oufattole, M., and Boutry, M. (2001). Hydrophobic residues within the predicted N-terminal amphiphilic a-helix of a plant mitochondrial targeting presequence play a major role in in vivo import. Plant J. 27: 539-549.
    • (2001) Plant J , vol.27 , pp. 539-549
    • Duby, G.1    Oufattole, M.2    Boutry, M.3
  • 12
    • 70349451660 scopus 로고    scopus 로고
    • Multiple pathways for mitochondrial protein traffic
    • Endo, T., and Yamano, K. (2009). Multiple pathways for mitochondrial protein traffic. Biol. Chem. 390: 723-730.
    • (2009) Biol. Chem , vol.390 , pp. 723-730
    • Endo, T.1    Yamano, K.2
  • 13
    • 79851512985 scopus 로고    scopus 로고
    • Structural insight into the mitochondrial protein import system
    • Endo, T., Yamano, K., and Kawano, S. (2011). Structural insight into the mitochondrial protein import system. Biochim. Biophys. Acta 1808: 955-970.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 955-970
    • Endo, T.1    Yamano, K.2    Kawano, S.3
  • 14
    • 8544225067 scopus 로고    scopus 로고
    • Mitochondrial protein import. Requirement of presequence elements and tom components for precursor binding to the TOM complex
    • Esaki, M., Shimizu, H., Ono, T., Yamamoto, H., Kanamori, T., Nishikawa, S., and Endo, T. (2004). Mitochondrial protein import. Requirement of presequence elements and tom components for precursor binding to the TOM complex. J. Biol. Chem. 279: 45701-45707.
    • (2004) J. Biol. Chem , vol.279 , pp. 45701-45707
    • Esaki, M.1    Shimizu, H.2    Ono, T.3    Yamamoto, H.4    Kanamori, T.5    Nishikawa, S.6    Endo, T.7
  • 15
    • 0141692862 scopus 로고    scopus 로고
    • Fatty acid biosynthesis in mitochondria of grasses: Malonyl-coenzyme A is generated by a mitochondriallocalized acetyl-coenzyme A carboxylase
    • Focke, M., Gieringer, E., Schwan, S., Jänsch, L., Binder, S., and Braun, H.P. (2003). Fatty acid biosynthesis in mitochondria of grasses: Malonyl-coenzyme A is generated by a mitochondriallocalized acetyl-coenzyme A carboxylase. Plant Physiol. 133: 875-884.
    • (2003) Plant Physiol , vol.133 , pp. 875-884
    • Focke, M.1    Gieringer, E.2    Schwan, S.3    Jänsch, L.4    Binder, S.5    Braun, H.P.6
  • 16
    • 0032169540 scopus 로고    scopus 로고
    • Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation
    • Glaser, E., Sjöling, S., Tanudji, M., and Whelan, J. (1998). Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation. Plant Mol. Biol. 38: 311-338.
    • (1998) Plant Mol. Biol , vol.38 , pp. 311-338
    • Glaser, E.1    Sjöling, S.2    Tanudji, M.3    Whelan, J.4
  • 17
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood, J.L., Tonti-Filippini, J.S., Gout, A.M., Day, D.A., Whelan, J., and Millar, A.H. (2004). Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16: 241-256.
    • (2004) Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 18
    • 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, N.L., Whelan, J., and Millar, A.H. (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
  • 19
    • 29344448488 scopus 로고    scopus 로고
    • Dual targeting of xylanase to chloroplasts and peroxisomes as a means to increase protein accumulation in plant cells
    • Hyunjong, B., Lee, D.-S., and Hwang, I. (2006). Dual targeting of xylanase to chloroplasts and peroxisomes as a means to increase protein accumulation in plant cells. J. Exp. Bot. 57: 161-169.
    • (2006) J. Exp. Bot , vol.57 , pp. 161-169
    • Hyunjong, B.1    Lee, D.-S.2    Hwang, I.3
  • 20
    • 0033619787 scopus 로고    scopus 로고
    • Mitochondrial processing peptidase: Multiple-site recognition of precursor proteins
    • Ito, A. (1999). Mitochondrial processing peptidase: Multiple-site recognition of precursor proteins. Biochem. Biophys. Res. Commun. 265: 611-616.
    • (1999) Biochem. Biophys. Res. Commun , vol.265 , pp. 611-616
    • Ito, A.1
  • 21
    • 0034923482 scopus 로고    scopus 로고
    • A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis
    • Jin, J.B., Kim, Y.A., Kim, S.J., Lee, S.H., Kim, D.H., Cheong, G.-W., and Hwang, I. (2001). A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis. Plant Cell 13: 1511-1526.
    • (2001) Plant Cell , vol.13 , pp. 1511-1526
    • Jin, J.B.1    Kim, Y.A.2    Kim, S.J.3    Lee, S.H.4    Kim, D.H.5    Cheong, G.-W.6    Hwang, I.7
  • 22
    • 0033616726 scopus 로고    scopus 로고
    • Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane
    • Kanamori, T., Nishikawa, S., Nakai, M., Shin, I., Schultz, P.G., and Endo, T. (1999). Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane. Proc. Natl. Acad. Sci. USA 96: 3634-3639.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 3634-3639
    • Kanamori, T.1    Nishikawa, S.2    Nakai, M.3    Shin, I.4    Schultz, P.G.5    Endo, T.6
  • 23
    • 0035098276 scopus 로고    scopus 로고
    • Trafficking of phosphatidyl-inositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells
    • Kim, D.H., Eu, Y.J., Yoo, C.M., Kim, Y.W., Pih, K.T., Jin, J.B., Kim, S.J., Stenmark, H., and Hwang, I. (2001). Trafficking of phosphatidyl-inositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells. Plant Cell 13: 287-301.
    • (2001) Plant Cell , vol.13 , pp. 287-301
    • Kim, D.H.1    Eu, Y.J.2    Yoo, C.M.3    Kim, Y.W.4    Pih, K.T.5    Jin, J.B.6    Kim, S.J.7    Stenmark, H.8    Hwang, I.9
  • 24
    • 57749094259 scopus 로고    scopus 로고
    • Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs
    • Lee, D.W., Kim, J.K., Lee, S., Choi, S., Kim, S., and Hwang, I. (2008). Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs. Plant Cell 20: 1603-1622.
    • (2008) Plant Cell , vol.20 , pp. 1603-1622
    • Lee, D.W.1    Kim, J.K.2    Lee, S.3    Choi, S.4    Kim, S.5    Hwang, I.6
  • 25
    • 33646835436 scopus 로고    scopus 로고
    • Functional characterization of sequence motifs in the transit peptide of Arabidopsis small subunit of rubisco
    • Lee, D.W., Lee, S., Lee, G.J., Lee, K.H., Kim, S., Cheong, G.W., and Hwang, I. (2006). Functional characterization of sequence motifs in the transit peptide of Arabidopsis small subunit of rubisco. Plant Physiol. 140: 466-483.
    • (2006) Plant Physiol , vol.140 , pp. 466-483
    • Lee, D.W.1    Lee, S.2    Lee, G.J.3    Lee, K.H.4    Kim, S.5    Cheong, G.W.6    Hwang, I.7
  • 26
    • 70349225929 scopus 로고    scopus 로고
    • Multiple sequence motifs in the rubisco small subunit transit peptide independently contribute to Toc159-dependent import of proteins into chloroplasts
    • Lee, D.W., Lee, S., Oh, Y.J., and Hwang, I. (2009). Multiple sequence motifs in the rubisco small subunit transit peptide independently contribute to Toc159-dependent import of proteins into chloroplasts. Plant Physiol. 151: 129-141.
    • (2009) Plant Physiol , vol.151 , pp. 129-141
    • Lee, D.W.1    Lee, S.2    Oh, Y.J.3    Hwang, I.4
  • 27
    • 79957740991 scopus 로고    scopus 로고
    • Both the hydrophobicity and a positively charged region flanking the C-terminal region of the transmembrane domain of signal-anchored proteins play critical roles in determining their targeting specificity to the endoplasmic reticulum or endosymbiotic organelles in Arabidopsis cells
    • Lee, J., Lee, H., Kim, J., Lee, S., Kim, D.H., Kim, S., and Hwang, I. (2011). Both the hydrophobicity and a positively charged region flanking the C-terminal region of the transmembrane domain of signal-anchored proteins play critical roles in determining their targeting specificity to the endoplasmic reticulum or endosymbiotic organelles in Arabidopsis cells. Plant Cell 23: 1588-1607.
    • (2011) Plant Cell , vol.23 , pp. 1588-1607
    • Lee, J.1    Lee, H.2    Kim, J.3    Lee, S.4    Kim, D.H.5    Kim, S.6    Hwang, I.7
  • 28
    • 0038313173 scopus 로고    scopus 로고
    • In vivo import experiments in protoplasts reveal the importance of the overall context but not specific amino acid residues of the transit peptide during import into chloroplasts
    • Lee, K.H., Kim, D.H., Lee, S.W., Kim, Z.H., and Hwang, I. (2002). In vivo import experiments in protoplasts reveal the importance of the overall context but not specific amino acid residues of the transit peptide during import into chloroplasts. Mol. Cells 14: 388-397.
    • (2002) Mol. Cells , vol.14 , pp. 388-397
    • Lee, K.H.1    Kim, D.H.2    Lee, S.W.3    Kim, Z.H.4    Hwang, I.5
  • 29
    • 3442891848 scopus 로고    scopus 로고
    • Identification of signals required for import of the soybean F(A)d subunit of ATP synthase into mitochondria
    • Lee, M.N., and Whelan, J. (2004). Identification of signals required for import of the soybean F(A)d subunit of ATP synthase into mitochondria. Plant Mol. Biol. 54: 193-203.
    • (2004) Plant Mol. Biol , vol.54 , pp. 193-203
    • Lee, M.N.1    Whelan, J.2
  • 30
    • 75649148551 scopus 로고    scopus 로고
    • Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis
    • Lee, S., Lee, D.W., Lee, Y., Mayer, U., Stierhof, Y.D., Lee, S., Jürgens, G., and Hwang, I. (2009). Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis. Plant Cell 21: 3984-4001.
    • (2009) Plant Cell , vol.21 , pp. 3984-4001
    • Lee, S.1    Lee, D.W.2    Lee, Y.3    Mayer, U.4    Stierhof, Y.D.5    Lee, S.6    Jürgens, G.7    Hwang, I.8
  • 31
    • 37849017986 scopus 로고    scopus 로고
    • Functional definition of outer membrane proteins involved in preprotein import into mitochondria
    • Lister, R., Carrie, C., Duncan, O., Ho, L.H., Howell, K.A., Murcha, M.W., and Whelan, J. (2007). Functional definition of outer membrane proteins involved in preprotein import into mitochondria. Plant Cell 19: 3739-3759.
    • (2007) Plant Cell , vol.19 , pp. 3739-3759
    • Lister, R.1    Carrie, C.2    Duncan, O.3    Ho, L.H.4    Howell, K.A.5    Murcha, M.W.6    Whelan, J.7
  • 33
    • 0032403138 scopus 로고    scopus 로고
    • The yeast mitochondrial intermembrane space: Purification and analysis of two distinct fractions
    • Martin, H., Eckerskorn, C., Gärtner, F., Rassow, J., Lottspeich, F., and Pfanner, N. (1998). The yeast mitochondrial intermembrane space: Purification and analysis of two distinct fractions. Anal. Biochem. 265: 123-128.
    • (1998) Anal. Biochem , vol.265 , pp. 123-128
    • Martin, H.1    Eckerskorn, C.2    Gärtner, F.3    Rassow, J.4    Lottspeich, F.5    Pfanner, N.6
  • 35
    • 33751514488 scopus 로고    scopus 로고
    • Binding of mitochondrial leader sequences to Tom20 assessed using a bacterial two-hybrid system shows that hydrophobic interactions are essential and that some mutated leaders that do not bind Tom20 can still be imported
    • Mukhopadhyay, A., Yang, C.S., and Weiner, H. (2006). Binding of mitochondrial leader sequences to Tom20 assessed using a bacterial two-hybrid system shows that hydrophobic interactions are essential and that some mutated leaders that do not bind Tom20 can still be imported. Protein Sci. 15: 2739-2748.
    • (2006) Protein Sci , vol.15 , pp. 2739-2748
    • Mukhopadhyay, A.1    Yang, C.S.2    Weiner, H.3
  • 36
    • 0033452914 scopus 로고    scopus 로고
    • Import of precursor proteins into mitochondria from soybean tissues during development
    • Murcha, M.W., Huang, T., and Whelan, J. (1999). Import of precursor proteins into mitochondria from soybean tissues during development. FEBS Lett. 464: 53-59.
    • (1999) FEBS Lett , vol.464 , pp. 53-59
    • Murcha, M.W.1    Huang, T.2    Whelan, J.3
  • 37
    • 0035895431 scopus 로고    scopus 로고
    • NMR identification of the Tom20 binding segment in mitochondrial presequences
    • Muto, T., Obita, T., Abe, Y., Shodai, T., Endo, T., and Kohda, D. (2001). NMR identification of the Tom20 binding segment in mitochondrial presequences. J. Mol. Biol. 306: 137-143.
    • (2001) J. Mol. Biol , vol.306 , pp. 137-143
    • Muto, T.1    Obita, T.2    Abe, Y.3    Shodai, T.4    Endo, T.5    Kohda, D.6
  • 38
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W., and Herrmann, J.M. (2007). Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76: 723-749.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 39
    • 0027967490 scopus 로고
    • Arginine residues in the extension peptide are required for cleavage of a precursor by mitochondrial processing peptidase. Demonstration using synthetic peptide as a substrate
    • Niidome, T., Kitada, S., Shimokata, K., Ogishima, T., and Ito, A. (1994). Arginine residues in the extension peptide are required for cleavage of a precursor by mitochondrial processing peptidase. Demonstration using synthetic peptide as a substrate. J. Biol. Chem. 269: 24719-24722.
    • (1994) J. Biol. Chem , vol.269 , pp. 24719-24722
    • Niidome, T.1    Kitada, S.2    Shimokata, K.3    Ogishima, T.4    Ito, A.5
  • 40
    • 0037466277 scopus 로고    scopus 로고
    • Peptide library approach with a disulfide tether to refine the Tom20 recognition motif in mitochondrial presequences
    • Obita, T., Muto, T., Endo, T., and Kohda, D. (2003). Peptide library approach with a disulfide tether to refine the Tom20 recognition motif in mitochondrial presequences. J. Mol. Biol. 328: 495-504.
    • (2003) J. Mol. Biol , vol.328 , pp. 495-504
    • Obita, T.1    Muto, T.2    Endo, T.3    Kohda, D.4
  • 41
    • 0037099608 scopus 로고    scopus 로고
    • The protein import motor of mitochondria: A targeted molecular ratchet driving unfolding and translocation
    • Okamoto, K., Brinker, A., Paschen, S.A., Moarefi, I., Hayer-Hartl, M., Neupert, W., and Brunner, M. (2002). The protein import motor of mitochondria: A targeted molecular ratchet driving unfolding and translocation. EMBO J. 21: 3659-3671.
    • (2002) EMBO J , vol.21 , pp. 3659-3671
    • Okamoto, K.1    Brinker, A.2    Paschen, S.A.3    Moarefi, I.4    Hayer-Hartl, M.5    Neupert, W.6    Brunner, M.7
  • 42
    • 0031251763 scopus 로고    scopus 로고
    • A dynamin-like protein, ADL1, is present in membranes as a high-molecular-mass complex in Arabidopsis thaliana
    • Park, J.M., Kang, S.G., Pih, K.T., Jang, H.J., Piao, H.L., Yoon, H.W., Cho, M.J., and Hwang, I. (1997). A dynamin-like protein, ADL1, is present in membranes as a high-molecular-mass complex in Arabidopsis thaliana. Plant Physiol. 115: 763-771.
    • (1997) Plant Physiol , vol.115 , pp. 763-771
    • Park, J.M.1    Kang, S.G.2    Pih, K.T.3    Jang, H.J.4    Piao, H.L.5    Yoon, H.W.6    Cho, M.J.7    Hwang, I.8
  • 43
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N., and Geissler, A. (2001). Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell Biol. 2: 339-349.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 44
    • 0242607644 scopus 로고    scopus 로고
    • Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins
    • Rapaport, D. (2003). Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins. EMBO Rep. 4: 948-952.
    • (2003) EMBO Rep , vol.4 , pp. 948-952
    • Rapaport, D.1
  • 46
    • 79959195166 scopus 로고    scopus 로고
    • Crystallographic snapshots of Tom20-mitochondrial presequence interactions with disulfide-stabilized peptides
    • Saitoh, T., Igura, M., Miyazaki, Y., Ose, T., Maita, N., and Kohda, D. (2011). Crystallographic snapshots of Tom20-mitochondrial presequence interactions with disulfide-stabilized peptides. Biochemistry 50: 5487-5496.
    • (2011) Biochemistry , vol.50 , pp. 5487-5496
    • Saitoh, T.1    Igura, M.2    Miyazaki, Y.3    Ose, T.4    Maita, N.5    Kohda, D.6
  • 47
    • 36248989141 scopus 로고    scopus 로고
    • Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states
    • Saitoh, T., Igura, M., Obita, T., Ose, T., Kojima, R., Maenaka, K., Endo, T., and Kohda, D. (2007). Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states. EMBO J. 26: 4777-4787.
    • (2007) EMBO J , vol.26 , pp. 4777-4787
    • Saitoh, T.1    Igura, M.2    Obita, T.3    Ose, T.4    Kojima, R.5    Maenaka, K.6    Endo, T.7    Kohda, D.8
  • 48
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and Dobberstein, B. (1996). Common principles of protein translocation across membranes. Science 271: 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 49
    • 33749265140 scopus 로고    scopus 로고
    • Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of soluble cargo proteins in plant cells via interactions with clathrin, AP-1, VTI11, and VSR1
    • Song, J., Lee, M.H., Lee, G.-J., Yoo, C.M., and Hwang, I. (2006). Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of soluble cargo proteins in plant cells via interactions with clathrin, AP-1, VTI11, and VSR1. Plant Cell 18: 2258-2274.
    • (2006) Plant Cell , vol.18 , pp. 2258-2274
    • Song, J.1    Lee, M.H.2    Lee, G.-J.3    Yoo, C.M.4    Hwang, I.5
  • 50
    • 77953020406 scopus 로고    scopus 로고
    • On the mechanism of preprotein import by the mitochondrial presequence translocase
    • van der Laan, M., Hutu, D.P., and Rehling, P. (2010). On the mechanism of preprotein import by the mitochondrial presequence translocase. Biochim. Biophys. Acta 1803: 732-739.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 732-739
    • van der Laan, M.1    Hutu, D.P.2    Rehling, P.3
  • 51
    • 0027482105 scopus 로고
    • Co-translational protein import into mitochondria: An alternative view
    • Verner, K. (1993). Co-translational protein import into mitochondria: An alternative view. Trends Biochem. Sci. 18: 366-371.
    • (1993) Trends Biochem. Sci , vol.18 , pp. 366-371
    • Verner, K.1
  • 52
    • 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
  • 53
    • 0037009130 scopus 로고    scopus 로고
    • Molecular chaperones as essential mediators of mitochondrial biogenesis
    • Voos, W., and Röttgers, K. (2002). Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim. Biophys. Acta 1592: 51-62.
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 51-62
    • Voos, W.1    Röttgers, K.2
  • 54
    • 0029240442 scopus 로고
    • Studies on the import and processing of the alternative oxidase precursor by isolated soybean mitochondria
    • Whelan, J., Hugosson, M., Glaser, E., and Day, D.A. (1995). Studies on the import and processing of the alternative oxidase precursor by isolated soybean mitochondria. Plant Mol. Biol. 27: 769-778.
    • (1995) Plant Mol. Biol , vol.27 , pp. 769-778
    • Whelan, J.1    Hugosson, M.2    Glaser, E.3    Day, D.A.4
  • 55
    • 78651083176 scopus 로고    scopus 로고
    • Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria
    • Yamamoto, H., et al. (2011). Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria. Proc. Natl. Acad. Sci. USA 108: 91-96.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 91-96
    • Yamamoto, H.1
  • 56
    • 55249113916 scopus 로고    scopus 로고
    • Step-size analyses of the mitochondrial Hsp70 import motor reveal the Brownian ratchet in operation
    • Yamano, K., Kuroyanagi-Hasegawa, M., Esaki, M., Yokota, M., and Endo, T. (2008). Step-size analyses of the mitochondrial Hsp70 import motor reveal the Brownian ratchet in operation. J. Biol. Chem. 283: 27325-27332.
    • (2008) J. Biol. Chem , vol.283 , pp. 27325-27332
    • Yamano, K.1    Kuroyanagi-Hasegawa, M.2    Esaki, M.3    Yokota, M.4    Endo, T.5
  • 57
    • 78549279787 scopus 로고    scopus 로고
    • The molecular recognition mechanism for superoxide dismutase presequence binding to the mitochondrial protein import receptor Tom20 from Oryza sativa involves an LRTLA motif
    • Zhang, Y., Baaden, M., Yan, J., Shao, J., Qiu, S., Wu, Y., andDing, Y. (2010). The molecular recognition mechanism for superoxide dismutase presequence binding to the mitochondrial protein import receptor Tom20 from Oryza sativa involves an LRTLA motif. J. Phys. Chem. B 114: 13839-13846.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 13839-13846
    • Zhang, Y.1    Baaden, M.2    Yan, J.3    Shao, J.4    Qiu, S.5    Wu, Y.6    Ding, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.