메뉴 건너뛰기




Volumn 38, Issue 1-2, 1998, Pages 265-277

Two birds with one stone: Genes that encode products targeted to two or more compartments

Author keywords

Dual targeting; Organelles; Protein import; RNA import

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; CYTOPLASM; PLANT GENETICS; PROTEIN EXPRESSION; TRANSFER RNA;

EID: 0032168849     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-94-011-5298-3_14     Document Type: Article
Times cited : (123)

References (73)
  • 1
    • 0025935374 scopus 로고
    • An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase
    • Arand M, Knehr M, Thomas H, Zeller HD, Oesch F: An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase. FEBS Lett 294: 19-22 (1991).
    • (1991) FEBS Lett , vol.294 , pp. 19-22
    • Arand, M.1    Knehr, M.2    Thomas, H.3    Zeller, H.D.4    Oesch, F.5
  • 2
    • 0031047734 scopus 로고    scopus 로고
    • Reexamination of the intracellular localization of de novo purine synthesis in cowpea nodules
    • Atkins CA, Smith PMC, Storer PJ: Reexamination of the intracellular localization of de novo purine synthesis in cowpea nodules. Plant Physiol 113: 127-135 (1997).
    • (1997) Plant Physiol , vol.113 , pp. 127-135
    • Atkins, C.A.1    Smith, P.M.C.2    Storer, P.J.3
  • 3
    • 0029105386 scopus 로고
    • Accumulation of 15-kilodalton zein in novel protein bodies in transgenic tobacco
    • Bagga S, Adams H, Kemp JD, Sengupta-Gopalan C: Accumulation of 15-kilodalton zein in novel protein bodies in transgenic tobacco. Plant Physiol 107: 13-23 (1995).
    • (1995) Plant Physiol , vol.107 , pp. 13-23
    • Bagga, S.1    Adams, H.2    Kemp, J.D.3    Sengupta-Gopalan, C.4
  • 4
    • 0030885876 scopus 로고    scopus 로고
    • Nuclear localization signal binding protein from Arabidopsis mediates nuclear import of Agrobacterium VirD2 protein
    • Ballas N, Citovsky V: Nuclear localization signal binding protein from Arabidopsis mediates nuclear import of Agrobacterium VirD2 protein. Proc Natl Acad Sci USA 94: 10723-10728 (1997).
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10723-10728
    • Ballas, N.1    Citovsky, V.2
  • 5
    • 0028280864 scopus 로고
    • Subcellular locations of MOD5 proteins: Mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms comingle in the cytosol
    • Boguta M, Hunter LA, Shen W-C, Gillman EC, Martin NC, Hopper AK: Subcellular locations of MOD5 proteins: mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms comingle in the cytosol. Mol Cell Biol 14: 2298-2306 (1994).
    • (1994) Mol Cell Biol , vol.14 , pp. 2298-2306
    • Boguta, M.1    Hunter, L.A.2    Shen, W.-C.3    Gillman, E.C.4    Martin, N.C.5    Hopper, A.K.6
  • 6
    • 0030469993 scopus 로고    scopus 로고
    • 5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes
    • 5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes. J Cell Biol 135: 1501-1513 (1996).
    • (1996) J Cell Biol , vol.135 , pp. 1501-1513
    • Borgese, N.1    Aggujaro, D.2    Carrera, P.3    Pietrini, G.4    Bassetti, M.5
  • 7
    • 0027105131 scopus 로고
    • A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast
    • Bossie MA, DeHoratius C, Barcelo G, Silver P: A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast. Mol Biol Cell 3: 875-893 (1992).
    • (1992) Mol Biol Cell , vol.3 , pp. 875-893
    • Bossie, M.A.1    DeHoratius, C.2    Barcelo, G.3    Silver, P.4
  • 8
    • 0028237677 scopus 로고
    • Preproteins of chloroplast envelope inner membrane contain targeting information for receptor-dependent import into fungal mitochondria
    • Brink S, Flugge UI, Chaumont F, Boutry M, Emmermann M, Schmilz U, Becker K, Pfanner N: Preproteins of chloroplast envelope inner membrane contain targeting information for receptor-dependent import into fungal mitochondria. J Biol Chem 269: 16478-16485 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 16478-16485
    • Brink, S.1    Flugge, U.I.2    Chaumont, F.3    Boutry, M.4    Emmermann, M.5    Schmilz, U.6    Becker, K.7    Pfanner, N.8
  • 9
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown MS, Goldstein JL: The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89: 331-340 (1997).
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 10
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey PJ: Protein lipidation in cell signaling. Science 268: 221-225 (1995).
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 11
    • 0023902156 scopus 로고
    • The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases
    • Chatton B, Walter P, Ebel JP, Lacroute F, Fasiolo F: The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases. J Biol Chem 263: 52-57 (1988).
    • (1988) J Biol Chem , vol.263 , pp. 52-57
    • Chatton, B.1    Walter, P.2    Ebel, J.P.3    Lacroute, F.4    Fasiolo, F.5
  • 13
    • 0028500157 scopus 로고
    • An Arabidopsis chloroplast RNA-binding protein gene encodes multiple mRNAs with different 5′ ends
    • Cheng S-H, Cline K, DeLisle AJ: An Arabidopsis chloroplast RNA-binding protein gene encodes multiple mRNAs with different 5′ ends. Plant Physiol 106: 303-311 (1994).
    • (1994) Plant Physiol , vol.106 , pp. 303-311
    • Cheng, S.-H.1    Cline, K.2    DeLisle, A.J.3
  • 15
    • 0030786269 scopus 로고    scopus 로고
    • A single precursor protein for ferrochelatase-I from Arabidopsis is imported in vitro into both chloroplasts and mitochondria
    • Chow KS, Singh DP, Roper JM, Smith AG: A single precursor protein for ferrochelatase-I from Arabidopsis is imported in vitro into both chloroplasts and mitochondria. J Biol Chem 272: 27565-27571 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 27565-27571
    • Chow, K.S.1    Singh, D.P.2    Roper, J.M.3    Smith, A.G.4
  • 16
    • 0029347014 scopus 로고
    • Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco
    • Creissen G, Reynolds H, Xue Y, Mullineaux P: Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco. Plant J 8: 167-175 (1995).
    • (1995) Plant J , vol.8 , pp. 167-175
    • Creissen, G.1    Reynolds, H.2    Xue, Y.3    Mullineaux, P.4
  • 17
    • 0030919438 scopus 로고    scopus 로고
    • The Arabidopsis thaliana FPS1 gene generates a novel mRNA that encodes a mitochondrial farnesyl-diphospate synthase isoform
    • Cunillera N, Boronat A, Ferrer A: The Arabidopsis thaliana FPS1 gene generates a novel mRNA that encodes a mitochondrial farnesyl-diphospate synthase isoform. J Biol Chem 272: 15381-15388 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 15381-15388
    • Cunillera, N.1    Boronat, A.2    Ferrer, A.3
  • 18
    • 0029015912 scopus 로고
    • How can the products of a single gene be localized to more than one intracellular compartment?
    • Danpure CJ: How can the products of a single gene be localized to more than one intracellular compartment? Trends Cell Biol 5: 230-238 (1995).
    • (1995) Trends Cell Biol , vol.5 , pp. 230-238
    • Danpure, C.J.1
  • 19
    • 0031127316 scopus 로고    scopus 로고
    • Variable peroxisomal and mitochondrial targeting of alanine: Glyoxylate aminotransferase in mammalian evolution and disease
    • Danpure CJ: Variable peroxisomal and mitochondrial targeting of alanine: glyoxylate aminotransferase in mammalian evolution and disease. Bioessays 19: 317-326 (1997).
    • (1997) Bioessays , vol.19 , pp. 317-326
    • Danpure, C.J.1
  • 20
    • 0030087937 scopus 로고    scopus 로고
    • Mitochondrial and chloroplast targeting sequences in tandem modify protein import specificity in plant organelles
    • de Castro Silva Filho M, Chaumont F, Leterme S, Boutry M: Mitochondrial and chloroplast targeting sequences in tandem modify protein import specificity in plant organelles. Plant Mol Biol 30: 769-780 (1996).
    • (1996) Plant Mol Biol , vol.30 , pp. 769-780
    • De Castro Silva Filho, M.1    Chaumont, F.2    Leterme, S.3    Boutry, M.4
  • 21
    • 0001160047 scopus 로고    scopus 로고
    • Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein
    • de Castro Silva-Filho M, Wieers MC, Flugge UI, Chaumont F, Boutry M: Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein. J Biol Chem 272: 15264-15269 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 15264-15269
    • De Castro Silva-Filho, M.1    Wieers, M.C.2    Flugge, U.I.3    Chaumont, F.4    Boutry, M.5
  • 24
    • 0000785054 scopus 로고    scopus 로고
    • Isolation and characterization of a glycyl-tRNA synthetase sequence from Arabidopsis thaliana (Accession No. AJ002062)
    • Duchene A-M, Dietrich A: Isolation and characterization of a glycyl-tRNA synthetase sequence from Arabidopsis thaliana (Accession No. AJ002062). Plant Physiol 115: 1730 (1997).
    • (1997) Plant Physiol , vol.115 , pp. 1730
    • Duchene, A.-M.1    Dietrich, A.2
  • 25
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, Nagata S: A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391: 43-50 (1998).
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 26
    • 0032168083 scopus 로고    scopus 로고
    • The endoplasmic reticulum of plant cells and its role in maturation of secretory proteins and biogenesis of oil bodies
    • this issue
    • Galili G, Sengupta-Gopalan C, Ceriotti A: The endoplasmic reticulum of plant cells and its role in maturation of secretory proteins and biogenesis of oil bodies. Plant Mol Biol, this issue (1998).
    • (1998) Plant Mol Biol
    • Galili, G.1    Sengupta-Gopalan, C.2    Ceriotti, A.3
  • 27
    • 0032169540 scopus 로고    scopus 로고
    • Mitochondrial protein import in plants: Signals, sorting, targeting, processing and regulation
    • this issue
    • Glaser E, Sjöling S, Tanudij M, Whelan J: Mitochondrial protein import in plants: signals, sorting, targeting, processing and regulation. Plant Mol Biol, this issue (1998).
    • (1998) Plant Mol Biol
    • Glaser, E.1    Sjöling, S.2    Tanudij, M.3    Whelan, J.4
  • 28
    • 0031080071 scopus 로고    scopus 로고
    • The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER
    • Gomord V, Denmat L-A, Fitchette-Lainé A-C, Satiat-Jeunemaitre B, Hawes C, Faye L: The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER. Plant J 11: 313-325 (1997).
    • (1997) Plant J , vol.11 , pp. 313-325
    • Gomord, V.1    Denmat, L.-A.2    Fitchette-Lainé, A.-C.3    Satiat-Jeunemaitre, B.4    Hawes, C.5    Faye, L.6
  • 29
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich D, Mattaj IW: Nucleocytoplasmic transport. Science 271: 1513-1518 (1996).
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.W.2
  • 33
    • 0030811859 scopus 로고    scopus 로고
    • Comparative analysis of the genomes of the bacteria Mycoplasma pneumoniae and Mycoplasma genitalium
    • Himmelreich R, Plagens H, Hilbert H, Reiner B, Herrmann R: Comparative analysis of the genomes of the bacteria Mycoplasma pneumoniae and Mycoplasma genitalium. Nucl Acids Res 25: 701-712 (1997).
    • (1997) Nucl Acids Res , vol.25 , pp. 701-712
    • Himmelreich, R.1    Plagens, H.2    Hilbert, H.3    Reiner, B.4    Herrmann, R.5
  • 34
    • 0025576261 scopus 로고
    • A yeast mitochondrial leader peptide functions in vivo as a dual targeting signal for both chloroplasts and mitochondria
    • Huang J, Hack E, Thornburg RW, Myers AM: A yeast mitochondrial leader peptide functions in vivo as a dual targeting signal for both chloroplasts and mitochondria. Plant Cell 2: 1249-1260 (1990).
    • (1990) Plant Cell , vol.2 , pp. 1249-1260
    • Huang, J.1    Hack, E.2    Thornburg, R.W.3    Myers, A.M.4
  • 35
    • 0000032646 scopus 로고
    • The cleavable pre-sequence of an imported chloroplast protein directs attached polypeptides into yeast mitochondria
    • Hurt EC, Soltanifar N, Goldschmidt-Clermont M, Rochaix J-D, Schatz G: The cleavable pre-sequence of an imported chloroplast protein directs attached polypeptides into yeast mitochondria. EMBO J 5: 1343-1350 (1986).
    • (1986) EMBO J , vol.5 , pp. 1343-1350
    • Hurt, E.C.1    Soltanifar, N.2    Goldschmidt-Clermont, M.3    Rochaix, J.-D.4    Schatz, G.5
  • 36
    • 0031460023 scopus 로고    scopus 로고
    • Context sequences of translation initiation codon in plants
    • Joshi CP, Zhou H, Huang X, Chiang VL: Context sequences of translation initiation codon in plants. Plant Mol Biol 35: 993-1001 (1997).
    • (1997) Plant Mol Biol , vol.35 , pp. 993-1001
    • Joshi, C.P.1    Zhou, H.2    Huang, X.3    Chiang, V.L.4
  • 37
    • 0038620661 scopus 로고    scopus 로고
    • Exchange of protein molecules through connections between higher plant plastids
    • Köhler RH, Cao J, Zipfel WR, Webb WW, Hanson MR: Exchange of protein molecules through connections between higher plant plastids. Science 276: 2039-2042 (1997).
    • (1997) Science , vol.276 , pp. 2039-2042
    • Köhler, R.H.1    Cao, J.2    Zipfel, W.R.3    Webb, W.W.4    Hanson, M.R.5
  • 38
    • 0031104715 scopus 로고    scopus 로고
    • The green fluorescent protein as a marker to visualize plant mitochondria in vivo
    • Köhler RH, Zipfel WR, Webb WW, Hanson MR: The green fluorescent protein as a marker to visualize plant mitochondria in vivo. Plant J 11: 613-621 (1997).
    • (1997) Plant J , vol.11 , pp. 613-621
    • Köhler, R.H.1    Zipfel, W.R.2    Webb, W.W.3    Hanson, M.R.4
  • 39
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors
    • Kornfeld S: Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors. Annu Rev Biochem 61: 307-330 (1992).
    • (1992) Annu Rev Biochem , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 40
    • 0028607170 scopus 로고
    • Determinants of translational fidelity and efficiency in vertebrate mRNAs
    • Kozak M: Determinants of translational fidelity and efficiency in vertebrate mRNAs. Biochimie 76: 815-821 (1994).
    • (1994) Biochimie , vol.76 , pp. 815-821
    • Kozak, M.1
  • 41
    • 0030791450 scopus 로고    scopus 로고
    • The human dUTPase gene encodes both nuclear and mitochondrial isoforms
    • Ladner RD, Caradonna SJ: The human dUTPase gene encodes both nuclear and mitochondrial isoforms. J Biol Chem 272: 19072-19080 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 19072-19080
    • Ladner, R.D.1    Caradonna, S.J.2
  • 42
    • 0029379562 scopus 로고
    • The use of an alternative promoter in the Arabidopsis thaliana HMG1 gene generates an mRNA that encodes a novel 3-hydroxy-methylglutaryl coenzyme a reductase isoform with an extended N-terminal region
    • Lumbreras V, Campos N, Boronat A: The use of an alternative promoter in the Arabidopsis thaliana HMG1 gene generates an mRNA that encodes a novel 3-hydroxy-methylglutaryl coenzyme A reductase isoform with an extended N-terminal region. Plant J 8: 541-549 (1995).
    • (1995) Plant J , vol.8 , pp. 541-549
    • Lumbreras, V.1    Campos, N.2    Boronat, A.3
  • 43
    • 0031105834 scopus 로고    scopus 로고
    • Multiple transcription start sites of the carrot dihydrofolate reductase-thymidylate synthase gene, and sub-cellular localization of the bifunctional protein
    • R. C
    • Luo M, Orsi R, Patrucco E, Pancaldi S, R. C: Multiple transcription start sites of the carrot dihydrofolate reductase-thymidylate synthase gene, and sub-cellular localization of the bifunctional protein. Plant Mol Biol 33: 709-722 (1997).
    • (1997) Plant Mol Biol , vol.33 , pp. 709-722
    • Luo, M.1    Orsi, R.2    Patrucco, E.3    Pancaldi, S.4
  • 44
    • 0028657592 scopus 로고
    • How single genes provide tRNA processing enzymes to mitochondria, nuclei and the cytosol
    • Martin NC, Hopper AK: How single genes provide tRNA processing enzymes to mitochondria, nuclei and the cytosol. Biochimie 76: 1161-1167 (1994).
    • (1994) Biochimie , vol.76 , pp. 1161-1167
    • Martin, N.C.1    Hopper, A.K.2
  • 45
    • 0018793912 scopus 로고
    • Import of nuclear deoxyribonucleic acid coded lysine-accepting transfer ribonucleic acid (anticodon C-U-U) into yeast mitochondria
    • Martin RP, Schneller JM, Stahl AJC, Dirheimer G: Import of nuclear deoxyribonucleic acid coded lysine-accepting transfer ribonucleic acid (anticodon C-U-U) into yeast mitochondria. Biochemistry 18: 4600-4605 (1979).
    • (1979) Biochemistry , vol.18 , pp. 4600-4605
    • Martin, R.P.1    Schneller, J.M.2    Stahl, A.J.C.3    Dirheimer, G.4
  • 46
    • 0029015799 scopus 로고
    • Arabidopsis COP1 protein specifically interacts in vitro with a cytoskeleton-associated protein, CIP1
    • Matsui M, Stoop CD, von Arnim AG, Wei N, Deng X-W: Arabidopsis COP1 protein specifically interacts in vitro with a cytoskeleton-associated protein, CIP1. Proc Natl Acad Sci USA 92: 4239-4243 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4239-4243
    • Matsui, M.1    Stoop, C.D.2    Von Arnim, A.G.3    Wei, N.4    Deng, X.-W.5
  • 47
    • 0030175064 scopus 로고    scopus 로고
    • The same Arabidopsis gene encodes both cytosolic and mitochondrial alanyl-tRNA synthetases
    • Mireau H, Lancelin D, Small ID: The same Arabidopsis gene encodes both cytosolic and mitochondrial alanyl-tRNA synthetases. Plant Cell 8: 1027-1039 (1996).
    • (1996) Plant Cell , vol.8 , pp. 1027-1039
    • Mireau, H.1    Lancelin, D.2    Small, I.D.3
  • 48
    • 0025764782 scopus 로고
    • The role of phosphorylation and the CDC28 protein kinase in cell cycle- Regulated nuclear import of the S. cerevisiae transcription factor SWI5
    • Moll T, Tebb G, Surana U, Robitsch H, Nasmyth K: The role of phosphorylation and the CDC28 protein kinase in cell cycle- regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell 66: 743-758 (1991).
    • (1991) Cell , vol.66 , pp. 743-758
    • Moll, T.1    Tebb, G.2    Surana, U.3    Robitsch, H.4    Nasmyth, K.5
  • 49
    • 0032168206 scopus 로고    scopus 로고
    • Deposition of storage proteins
    • this issue
    • Müntz K: Deposition of storage proteins. Plant Mol Biol, this issue (1998).
    • (1998) Plant Mol Biol
    • Müntz, K.1
  • 50
    • 0022470359 scopus 로고
    • The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine-tRNA synthetases of S. cerevisiae
    • Natsoulis G, Hilger F, Fink GR: The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine-tRNA synthetases of S. cerevisiae. Cell 46: 235-243 (1986).
    • (1986) Cell , vol.46 , pp. 235-243
    • Natsoulis, G.1    Hilger, F.2    Fink, G.R.3
  • 51
    • 0028002143 scopus 로고
    • Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: Low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space
    • Neuhaus J-M, Pietrzak M, Boller T: Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space. Plant J 5: 45-54 (1994).
    • (1994) Plant J , vol.5 , pp. 45-54
    • Neuhaus, J.-M.1    Pietrzak, M.2    Boller, T.3
  • 52
    • 0032169928 scopus 로고    scopus 로고
    • Sorting of proteins to vacuoles in plant cells
    • this issue
    • Neuhaus J-M, Rogers JC: Sorting of proteins to vacuoles in plant cells. Plant Mol Biol, this issue (1998).
    • (1998) Plant Mol Biol
    • Neuhaus, J.-M.1    Rogers, J.C.2
  • 53
    • 0026769570 scopus 로고
    • Transfer RNA genes in the mitochondrial genome from a liverwort, Marchantia polymorpha: The absence of chloroplast-like tRNAs
    • Oda K, Yamato K, Ohta E, Nakamura Y, Takemura M, Nozato N, Akashi K, Ohyama K: Transfer RNA genes in the mitochondrial genome from a liverwort, Marchantia polymorpha: the absence of chloroplast-like tRNAs. Nucl Acids Res 20: 3773-3777 (1992).
    • (1992) Nucl Acids Res , vol.20 , pp. 3773-3777
    • Oda, K.1    Yamato, K.2    Ohta, E.3    Nakamura, Y.4    Takemura, M.5    Nozato, N.6    Akashi, K.7    Ohyama, K.8
  • 54
    • 0001009574 scopus 로고    scopus 로고
    • Compartmentation of poteins in the endomembrane system of plant cells
    • Okita TW: Compartmentation of poteins in the endomembrane system of plant cells. Annu Rev Plant Physiol Plant Mol Biol 47: 327-350 (1996).
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 327-350
    • Okita, T.W.1
  • 55
    • 0023441954 scopus 로고
    • Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor
    • Picard D, Yamamoto KR: Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J 11: 3333-3340 (1987).
    • (1987) EMBO J , vol.11 , pp. 3333-3340
    • Picard, D.1    Yamamoto, K.R.2
  • 56
    • 0026026630 scopus 로고
    • The rate of nuclear cytoplasmic protein transport is determined by the casein kinase n site flanking the nuclear localization sequence of the SV40 T-antigen
    • Rihs H-P, Jans DA, Fan H, Peters R: The rate of nuclear cytoplasmic protein transport is determined by the casein kinase n site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J 10: 633-639 (1991).
    • (1991) EMBO J , vol.10 , pp. 633-639
    • Rihs, H.-P.1    Jans, D.A.2    Fan, H.3    Peters, R.4
  • 57
    • 0032169929 scopus 로고    scopus 로고
    • Multiple pathways for the targeting of thylakoid proteins in chloroplasts
    • this issue
    • Robinson C, Hynds PJ, Robinson D, Mant A: Multiple pathways for the targeting of thylakoid proteins in chloroplasts. Plant Mol Biol, this issue (1998).
    • (1998) Plant Mol Biol
    • Robinson, C.1    Hynds, P.J.2    Robinson, D.3    Mant, A.4
  • 58
    • 0024787847 scopus 로고
    • A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein
    • Sadler I, Chiang A, Kurihara T, Rothblatt J, Way J, Silver P: A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein. J Cell Biol 109: 2665-2675 (1989).
    • (1989) J Cell Biol , vol.109 , pp. 2665-2675
    • Sadler, I.1    Chiang, A.2    Kurihara, T.3    Rothblatt, J.4    Way, J.5    Silver, P.6
  • 59
    • 0028305713 scopus 로고
    • Isolation of a cDNA encoding chloroplast ferrochelatase from Arabidopsis thaliana by functional complementation of a yeast mutant
    • Smith AG, Santana MA, Wallace-Cook AD, Roper JM, Labbe-Bois R: Isolation of a cDNA encoding chloroplast ferrochelatase from Arabidopsis thaliana by functional complementation of a yeast mutant. J Biol Chem 269: 13405-13413 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 13405-13413
    • Smith, A.G.1    Santana, M.A.2    Wallace-Cook, A.D.3    Roper, J.M.4    Labbe-Bois, R.5
  • 60
    • 0031153924 scopus 로고    scopus 로고
    • Importin α from Arabidopsis thaliana is a nuclear import receptor that recognizes three classes of import signals
    • Smith HM, Hicks GR, Raikhel NV: Importin α from Arabidopsis thaliana is a nuclear import receptor that recognizes three classes of import signals. Plant Physiol 114: 411-417 (1997).
    • (1997) Plant Physiol , vol.114 , pp. 411-417
    • Smith, H.M.1    Hicks, G.R.2    Raikhel, N.V.3
  • 61
    • 0032055825 scopus 로고    scopus 로고
    • AIR synthase in cowpea nodules: A single gene product targeted to two organelles?
    • Smith PMC, Mann AJ, Atkins CA: AIR synthase in cowpea nodules: a single gene product targeted to two organelles? Plant Mol Biol 36: 811-820 (1998).
    • (1998) Plant Mol Biol , vol.36 , pp. 811-820
    • Pmc, S.1    Mann, A.J.2    Atkins, C.A.3
  • 62
    • 0032168004 scopus 로고    scopus 로고
    • Protein translocation into and across the chloroplastic envelope membranes
    • this issue
    • Soll J, Tien R: Protein translocation into and across the chloroplastic envelope membranes. Plant Mol Biol, this issue (1998).
    • (1998) Plant Mol Biol
    • Soll, J.1    Tien, R.2
  • 63
    • 0031170901 scopus 로고    scopus 로고
    • The plant ER: A dynamic organelle composed of a large number of discrete functional domains
    • Staehelin: The plant ER: a dynamic organelle composed of a large number of discrete functional domains. Plant J 11: 1151-1165 (1997).
    • (1997) Plant J , vol.11 , pp. 1151-1165
    • Staehelin1
  • 64
    • 0029017974 scopus 로고
    • Mitochondrial import of a cytoplasmic lysine-tRNA in yeast is mediated by cooperation of cytoplasmic and mitochondrial lysyl-tRNA synthetases
    • Tarassov I, Entelis N, Martin RP: Mitochondrial import of a cytoplasmic lysine-tRNA in yeast is mediated by cooperation of cytoplasmic and mitochondrial lysyl-tRNA synthetases. EMBO J 14: 3461-3471 (1995).
    • (1995) EMBO J , vol.14 , pp. 3461-3471
    • Tarassov, I.1    Entelis, N.2    Martin, R.P.3
  • 65
    • 0031149960 scopus 로고    scopus 로고
    • Intracellular localization of GBF proteins and blue-light induced import of GBF2 fusion proteins into the nucleus of cultured Arabidopsis and soybean cells
    • Terzaghi WB, Bertekap Jr. RL, Cashmore AR: Intracellular localization of GBF proteins and blue-light induced import of GBF2 fusion proteins into the nucleus of cultured Arabidopsis and soybean cells. Plant J 11: 967-982 (1997).
    • (1997) Plant J , vol.11 , pp. 967-982
    • Terzaghi, W.B.1    Bertekap Jr., R.L.2    Cashmore, A.R.3
  • 66
    • 0031021278 scopus 로고    scopus 로고
    • The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides
    • Unseld M, Marienfeld JR, Brandt P, Brennicke A: The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides. Nature Genet 15: 57-61 (1997).
    • (1997) Nature Genet , vol.15 , pp. 57-61
    • Unseld, M.1    Marienfeld, J.R.2    Brandt, P.3    Brennicke, A.4
  • 67
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G, Steppuhn J, Herrmann RG: Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535-545 (1989).
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 68
    • 0029868470 scopus 로고    scopus 로고
    • Phosphorylation of the transit sequence of chloroplast precursor proteins
    • Waegemann K, Soil J: Phosphorylation of the transit sequence of chloroplast precursor proteins. J Biol Chem 271: 6545-6554 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 6545-6554
    • Waegemann, K.1    Soil, J.2
  • 69
    • 0031443640 scopus 로고    scopus 로고
    • The glyoxysomal and plastid molecular chaperones (70-kDa heat shock protein) of watermelon cotyledons are encoded by a single gene
    • Wimmer B, Lottspeich F, van der Klei I, Veenhuis M, Gietl C: The glyoxysomal and plastid molecular chaperones (70-kDa heat shock protein) of watermelon cotyledons are encoded by a single gene. Proc Natl Acad Sci USA 94: 13624-13629 (1997).
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13624-13629
    • Wimmer, B.1    Lottspeich, F.2    Van Der Klei, I.3    Veenhuis, M.4    Gietl, C.5
  • 70
    • 0029915703 scopus 로고    scopus 로고
    • Mechanisms leading to and the consequences of altering the normal distribution of ATP(CTP):tRNA nucleotidyltransferase in yeast
    • Wolfe CL, Hopper AK, Martin NC: Mechanisms leading to and the consequences of altering the normal distribution of ATP(CTP):tRNA nucleotidyltransferase in yeast. J Biol Chem 271: 4679-4686 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 4679-4686
    • Wolfe, C.L.1    Hopper, A.K.2    Martin, N.C.3
  • 71
    • 0026447426 scopus 로고
    • Function and evolution of a minimal plastid genome from a nonphotosynthetic plant
    • Wolfe KH, Morden CW, Palmer JD: Function and evolution of a minimal plastid genome from a nonphotosynthetic plant. Proc Natl Acad Sci USA 89: 10648-10652 (1992).
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10648-10652
    • Wolfe, K.H.1    Morden, C.W.2    Palmer, J.D.3
  • 72
    • 0030740461 scopus 로고    scopus 로고
    • Suspensor-derived polyembryony caused by altered expression of valyl-tRNA synthetase in the twn2 mutant of Arabidopsis
    • Zhang JZ, Somerville CR: Suspensor-derived polyembryony caused by altered expression of valyl-tRNA synthetase in the twn2 mutant of Arabidopsis. Proc Natl Acad Sci USA 94: 7349-7355 (1997).
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7349-7355
    • Zhang, J.Z.1    Somerville, C.R.2
  • 73
    • 0028791882 scopus 로고
    • Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery
    • Zoladek T, Vaduva G, Hunter LA, Boguta M, Go BD, Martin NC, Hopper AK: Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery. Mol Cell Biol 15: 6884-6894 (1995).
    • (1995) Mol Cell Biol , vol.15 , pp. 6884-6894
    • Zoladek, T.1    Vaduva, G.2    Hunter, L.A.3    Boguta, M.4    Go, B.D.5    Martin, N.C.6    Hopper, A.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.