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Volumn 265, Issue 1, 1999, Pages 171-180

A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii

Author keywords

Chlamydomonas reinhardtii; Chloroplast preproteins; NMR; Peptide conformation; Transit peptide

Indexed keywords

CARRIER PROTEIN;

EID: 0033215007     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00701.x     Document Type: Article
Times cited : (34)

References (79)
  • 1
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • 1. von Heijne, G., Steppuhn, J. & Herrmann, R.G. (1989) Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180, 535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 2
    • 0028281852 scopus 로고
    • NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution
    • 2. Lancelin, J.-M., Bally, I., Arlaud, G.J., Blackledge, M., Gans, P., Stein, M. & Jacquot, J.-P. (1994) NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution. FEBS Lett. 343, 261-266.
    • (1994) FEBS Lett. , vol.343 , pp. 261-266
    • Lancelin, J.-M.1    Bally, I.2    Arlaud, G.J.3    Blackledge, M.4    Gans, P.5    Stein, M.6    Jacquot, J.-P.7
  • 3
    • 0030570809 scopus 로고    scopus 로고
    • NMR structures of a mitochondrial transit peptide from the green alga Chlamydomonas reinhardtii
    • 3. Lancelin, J.-M., Gans, P., Bouchayer, E., Bally, I., Arlaud, G.J. & Jacquot, J.-P. (1996) NMR structures of a mitochondrial transit peptide from the green alga Chlamydomonas reinhardtii. FEBS Lett. 391, 203-208.
    • (1996) FEBS Lett. , vol.391 , pp. 203-208
    • Lancelin, J.-M.1    Gans, P.2    Bouchayer, E.3    Bally, I.4    Arlaud, G.J.5    Jacquot, J.-P.6
  • 4
    • 0024723123 scopus 로고
    • N-terminal half of a mitochondrial presequence peptide takes a helical conformation when bound to dodecylphosphocholine micelles: A proton nuclear magnetic resonance study
    • 4. Endo, T., Shimada, I., Roise, D. & Inagaki, F. (1989) N-terminal half of a mitochondrial presequence peptide takes a helical conformation when bound to dodecylphosphocholine micelles: a proton nuclear magnetic resonance study. J. Biochem. (Tokyo) 106, 396-400.
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 396-400
    • Endo, T.1    Shimada, I.2    Roise, D.3    Inagaki, F.4
  • 5
    • 0026643606 scopus 로고
    • Biophysical characterization of a transit peptide directing chloroplast protein import
    • 5. Theg, S.M. & Geske, F.J. (1992) Biophysical characterization of a transit peptide directing chloroplast protein import. Biochemistry 31, 5053-5060.
    • (1992) Biochemistry , vol.31 , pp. 5053-5060
    • Theg, S.M.1    Geske, F.J.2
  • 6
    • 0026683021 scopus 로고
    • The chloroplast-targeting domain of plastocyanin transit peptide can form a helical structure but does not have a high affinity for lipid bilayers
    • 6. Endo, T., Kawamura, K. & Nakai, M. (1992) The chloroplast-targeting domain of plastocyanin transit peptide can form a helical structure but does not have a high affinity for lipid bilayers. Eur. J. Biochem. 207, 671-675.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 671-675
    • Endo, T.1    Kawamura, K.2    Nakai, M.3
  • 7
    • 0026646504 scopus 로고
    • Secondary structure and folding of a functional chloroplast precursor protein
    • 7. Pilon, M., Rietveld, A.G., Weisbeek, P.J. & de Kruijff, B. (1992.) Secondary structure and folding of a functional chloroplast precursor protein. J. Biol. Chem. 267, 19907-19913.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19907-19913
    • Pilon, M.1    Rietveld, A.G.2    Weisbeek, P.J.3    De Kruijff, B.4
  • 8
    • 0027295559 scopus 로고
    • Import, processing, and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase
    • 8. Thornton, K., Wang, Y., Weiner, H. & Gorenstein, D.G. (1993) Import, processing, and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 268, 19906-19914.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19906-19914
    • Thornton, K.1    Wang, Y.2    Weiner, H.3    Gorenstein, D.G.4
  • 9
    • 0027426139 scopus 로고
    • The secondary structure of the ferredoxin transit sequence is modulated by its interaction with negatively charged lipids
    • 9. Horniak, L., Pilon, M., van't Hof, R. & de Kruijff, B. (1993) The secondary structure of the ferredoxin transit sequence is modulated by its interaction with negatively charged lipids. FEBS Lett. 334, 241-246.
    • (1993) FEBS Lett. , vol.334 , pp. 241-246
    • Horniak, L.1    Pilon, M.2    Van't Hof, R.3    De Kruijff, B.4
  • 11
    • 0028855710 scopus 로고
    • Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10
    • 11. Jarvis, J.A., Ryan, M.T., Hoogenraad, N.J., Craik, D.J. & Høj, P.B. (1995) Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10. J. Biol. Chem. 270, 1323-1331.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1323-1331
    • Jarvis, J.A.1    Ryan, M.T.2    Hoogenraad, N.J.3    Craik, D.J.4    Høj, P.B.5
  • 13
    • 0019885995 scopus 로고
    • Melittin bound to dodecylphosphocholine micelles. H-NMR assignments and global conformational features
    • 13. Brown, L.R. & Wüthrich, K. (1981) Melittin bound to dodecylphosphocholine micelles. H-NMR assignments and global conformational features. Biochim. Biophys. Acta 647, 95-111.
    • (1981) Biochim. Biophys. Acta , vol.647 , pp. 95-111
    • Brown, L.R.1    Wüthrich, K.2
  • 14
    • 0020068157 scopus 로고
    • High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface
    • 14. Brown, L.R., Braun, W., Kumar, A. & Wüthrich, K. (1982) High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface. Biophys. J. 37, 319-328.
    • (1982) Biophys. J. , vol.37 , pp. 319-328
    • Brown, L.R.1    Braun, W.2    Kumar, A.3    Wüthrich, K.4
  • 15
    • 0025978713 scopus 로고
    • Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 2D-NMR and distance geometry calculation
    • 15. Ikura, T., Go, N. & Inagaki, F. (1991) Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 2D-NMR and distance geometry calculation. Proteins 9, 81-89.
    • (1991) Proteins , vol.9 , pp. 81-89
    • Ikura, T.1    Go, N.2    Inagaki, F.3
  • 16
    • 0028022950 scopus 로고
    • Vesicle-bound conformation of melittin: Transferred nuclear overhauser enhancement analysis in the presence of perdeuterated phosphatidylcholine vesicles
    • 16. Okada, A., Wakamatsu, K., Miyazawa, T. & Higashijima, T. (1994) Vesicle-bound conformation of melittin: transferred nuclear Overhauser enhancement analysis in the presence of perdeuterated phosphatidylcholine vesicles. Biochemistry 33, 9438-9446.
    • (1994) Biochemistry , vol.33 , pp. 9438-9446
    • Okada, A.1    Wakamatsu, K.2    Miyazawa, T.3    Higashijima, T.4
  • 17
    • 0030012220 scopus 로고    scopus 로고
    • Structure and dynamics of melittin in lysomyristoyl phosphatidylcholine micelles determined by nuclear magnetic resonance
    • 17. Yuan, P., Fisher, P.J., Prendergast, F.G. & Kemple, M.D. (1996) Structure and dynamics of melittin in lysomyristoyl phosphatidylcholine micelles determined by nuclear magnetic resonance. Biophys. J. 70, 2223-2238.
    • (1996) Biophys. J. , vol.70 , pp. 2223-2238
    • Yuan, P.1    Fisher, P.J.2    Prendergast, F.G.3    Kemple, M.D.4
  • 18
    • 0023712129 scopus 로고
    • The solution conformation of the antibacterial peptide cecropin a: A nuclear magnetic resonance and dynamical simulated annealing study
    • 18. Holak, T.A., Engström, A., Kraulis, P.J., Lindeberg, G., Bennich, H., Jones, T.A., Gronenborn, A.M. & Clore, M. (1988) The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27, 7620-7629.
    • (1988) Biochemistry , vol.27 , pp. 7620-7629
    • Holak, T.A.1    Engström, A.2    Kraulis, P.J.3    Lindeberg, G.4    Bennich, H.5    Jones, T.A.6    Gronenborn, A.M.7    Clore, M.8
  • 19
    • 0026738175 scopus 로고
    • The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR
    • 19. Sipos, D., Andersson, M. & Ehrenberg, A. (1992) The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR. Eur. J. Biochem. 209, 163-169.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 163-169
    • Sipos, D.1    Andersson, M.2    Ehrenberg, A.3
  • 20
    • 0030852756 scopus 로고    scopus 로고
    • The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, litoria splendida
    • 20. Wong, H., Bowie, J.H. & Carver, J.A. (1997) The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida. Eur. J. Biochem. 247, 545-557.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 545-557
    • Wong, H.1    Bowie, J.H.2    Carver, J.A.3
  • 21
    • 0032546559 scopus 로고    scopus 로고
    • Secondary structure of an antibacterial peptide Abp3 studied by two-dimensional proton-NMR
    • 21. Xia, W., Liu, Q., Xia, Y. & Qu, X. (1998) Secondary structure of an antibacterial peptide Abp3 studied by two-dimensional proton-NMR. Biochim. Biophys. Acta 1384, 299-305.
    • (1998) Biochim. Biophys. Acta , vol.1384 , pp. 299-305
    • Xia, W.1    Liu, Q.2    Xia, Y.3    Qu, X.4
  • 22
    • 0032169930 scopus 로고    scopus 로고
    • The role of lipids in plastid protein transport
    • 22. Bruce, B.D. (1998) The role of lipids in plastid protein transport. Plant Mol. Biol. 38, 223-246.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 223-246
    • Bruce, B.D.1
  • 23
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • 23. Neupert, W. (1997) Protein import into mitochondria. Annu. Rev. Biochem. 66, 863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 24
    • 0031900451 scopus 로고    scopus 로고
    • The preprotein translocase of the mitochondrial outer membrane
    • 24. Ryan, M.T. & Pfanner, N. (1998) The preprotein translocase of the mitochondrial outer membrane. Biol. Chem. 379, 289-294.
    • (1998) Biol. Chem. , vol.379 , pp. 289-294
    • Ryan, M.T.1    Pfanner, N.2
  • 25
    • 0031463305 scopus 로고    scopus 로고
    • The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein
    • 25. Caliebe, A., Grimm, R., Kaiser, G., Lubeck, J., Soll, J. & Heins, L. (1997) The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein. EMBO J. 16, 7342-7350.
    • (1997) EMBO J. , vol.16 , pp. 7342-7350
    • Caliebe, A.1    Grimm, R.2    Kaiser, G.3    Lubeck, J.4    Soll, J.5    Heins, L.6
  • 26
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • 26. Hinnah, S.C., Hill, K., Wagner, R., Schlicher, T. & Soll, J. (1997) Reconstitution of a chloroplast protein import channel. EMBO J. 16, 7351-7360.
    • (1997) EMBO J. , vol.16 , pp. 7351-7360
    • Hinnah, S.C.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 27
    • 0031408330 scopus 로고    scopus 로고
    • Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts
    • 27. Kouranov, A. & Schnell, D.J. (1997) Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts. J. Cell. Biol. 139, 1677-1685.
    • (1997) J. Cell. Biol. , vol.139 , pp. 1677-1685
    • Kouranov, A.1    Schnell, D.J.2
  • 28
    • 0029905725 scopus 로고    scopus 로고
    • Protein translocation at the envelope and thylakoid membranes of chloroplasts
    • 28. Kouranov, A. & Schnell, D.J. (1996) Protein translocation at the envelope and thylakoid membranes of chloroplasts. J. Biol. Chem. 271, 31009-31012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31009-31012
    • Kouranov, A.1    Schnell, D.J.2
  • 29
    • 0029731659 scopus 로고    scopus 로고
    • Import and routing of nucleus-encoded chloroplast proteins
    • 29. Cline, K. & Henry, R. (1996) Import and routing of nucleus-encoded chloroplast proteins. Annu. Rev. Cell. Dev. Biol. 12, 1-26.
    • (1996) Annu. Rev. Cell. Dev. Biol. , vol.12 , pp. 1-26
    • Cline, K.1    Henry, R.2
  • 30
    • 0029798054 scopus 로고    scopus 로고
    • Interaction of the protein import and folding machineries of the chloroplast
    • 30. Kessler, F. & Blobel, G. (1996) Interaction of the protein import and folding machineries of the chloroplast. Proc. Natl Acad. Sci. USA 93, 7684-7689.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7684-7689
    • Kessler, F.1    Blobel, G.2
  • 31
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • 31. Rost, B. & Sander, C. (1993) Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 32
    • 0027169638 scopus 로고
    • Improved prediction of protein secondary structure by use of sequence profiles and neural networks
    • 32. Rost, B. & Sander, C. (1993) Improved prediction of protein secondary structure by use of sequence profiles and neural networks. Proc. Natl Acad. Sci. USA 90, 7558-7562.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7558-7562
    • Rost, B.1    Sander, C.2
  • 33
    • 0028158628 scopus 로고
    • PHD: An automatic mail server for protein secondary structure prediction
    • 33. Rost, B., Sander, C. & Scheinder, R. (1994) PHD: an automatic mail server for protein secondary structure prediction. Comput. Appl. Biosci. 10, 53-60.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Scheinder, R.3
  • 34
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • 34. Rost, B. & Sander, C. (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 584-599.
    • (1994) Proteins , vol.19 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 35
    • 0027639430 scopus 로고
    • A cDNA clone encoding Chlamydomonas reinhardtii preferredoxin
    • 35. Stein, M., Jacquot, J.-P. & Miginiac-Maslow, M. (1993) A cDNA clone encoding Chlamydomonas reinhardtii preferredoxin. Plant Physiol. 102, 1349-1350.
    • (1993) Plant Physiol. , vol.102 , pp. 1349-1350
    • Stein, M.1    Jacquot, J.-P.2    Miginiac-Maslow, M.3
  • 37
    • 0024297458 scopus 로고
    • cDNA sequence and predicted primary structure of the gamma subunit from the ATP synthase from Chlamydomonas reinhardtii
    • 37. Yu, L.M. & Selman, B.R. (1988) cDNA sequence and predicted primary structure of the gamma subunit from the ATP synthase from Chlamydomonas reinhardtii. J. Biol. Chem. 263, 19342-19345.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19342-19345
    • Yu, L.M.1    Selman, B.R.2
  • 38
    • 15844384218 scopus 로고    scopus 로고
    • The 4-kDa nuclear-encoded PetM polypeptide of the chloroplast cytochrome b6f complex. Nucleic acid and protein sequences, targeting signals, transmembrane topology
    • 38. de Vitry, C., Breyton, C., Pierre, Y. & Popot, J.L. (1996) The 4-kDa nuclear-encoded PetM polypeptide of the chloroplast cytochrome b6f complex. Nucleic acid and protein sequences, targeting signals, transmembrane topology. J. Biol. Chem. 271, 10667-10671.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10667-10671
    • De Vitry, C.1    Breyton, C.2    Pierre, Y.3    Popot, J.L.4
  • 39
    • 0026815409 scopus 로고
    • The early genetic response to light in the green unicellular alga Chlamydomonas eugametos grown under light/dark cycles involves genes that represent direct responses to light and photosynthesis
    • 39. Gagne, G. & Guertin, M. (1992) The early genetic response to light in the green unicellular alga Chlamydomonas eugametos grown under light/dark cycles involves genes that represent direct responses to light and photosynthesis. Plant Mol. Biol. 18, 429-445.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 429-445
    • Gagne, G.1    Guertin, M.2
  • 41
    • 0029126297 scopus 로고
    • The plastid aldolase gene from Chlamydomonas reinhardtii: Intron/exon organization, evolution, and promoter structure
    • 41. Pelzer-Reith, B., Freund, S., Schnarrenberger, C., Yatsuki, H. & Hori, K. (1995) The plastid aldolase gene from Chlamydomonas reinhardtii: intron/exon organization, evolution, and promoter structure. Mol. Gen. Genet. 248, 481-486.
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 481-486
    • Pelzer-Reith, B.1    Freund, S.2    Schnarrenberger, C.3    Yatsuki, H.4    Hori, K.5
  • 43
    • 0028006223 scopus 로고
    • Five identical intron positions in ancient duplicated genes of eubacterial origin
    • 43. Kersanach, R., Brinkmann, H., Liaud, M.F., Zhang, D.X., Martin, W. & Cerff, R. (1994) Five identical intron positions in ancient duplicated genes of eubacterial origin. Nature (London) 367, 387-389.
    • (1994) Nature (London) , vol.367 , pp. 387-389
    • Kersanach, R.1    Brinkmann, H.2    Liaud, M.F.3    Zhang, D.X.4    Martin, W.5    Cerff, R.6
  • 44
    • 0001009720 scopus 로고
    • Primary structure of Chlamydomonas reinhardtii ribulose 1,5-bisphosphate carboxylase/oxygenase activase and evidence for a single polypeptide
    • 44. Roesler, K.R. & Ogren, W.L. (1990) Primary structure of Chlamydomonas reinhardtii ribulose 1,5-bisphosphate carboxylase/ oxygenase activase and evidence for a single polypeptide. Plant Physiol. 93, 188-193.
    • (1990) Plant Physiol. , vol.93 , pp. 188-193
    • Roesler, K.R.1    Ogren, W.L.2
  • 45
    • 0029286788 scopus 로고
    • Cloning and sequencing of a cDNA clone encoding the photosystem I PsaD subunit from Chlamydomonas reinhardtii
    • 45. Farah, J., Frank, G., Zuber, H. & Rochaix, J.-D. (1995) Cloning and sequencing of a cDNA clone encoding the photosystem I PsaD subunit from Chlamydomonas reinhardtii. Plant Physiol. 107, 1485-1486.
    • (1995) Plant Physiol. , vol.107 , pp. 1485-1486
    • Farah, J.1    Frank, G.2    Zuber, H.3    Rochaix, J.-D.4
  • 46
    • 0000952526 scopus 로고
    • Isolation and characterization of cDNA clones encoding the 17.9 and 8.1 kDa subunits of photosystem I from Chlamydomonas reinhardtii
    • 46. Franzén, L.G., Frank, G., Zuber, H. & Rochaix, J.-D. (1989) Isolation and characterization of cDNA clones encoding the 17.9 and 8.1 kDa subunits of photosystem I from Chlamydomonas reinhardtii. Plant Mol. Biol. 12, 463-474.
    • (1989) Plant Mol. Biol. , vol.12 , pp. 463-474
    • Franzén, L.G.1    Frank, G.2    Zuber, H.3    Rochaix, J.-D.4
  • 47
    • 0024742242 scopus 로고
    • Isolation and characterization of cDNA clones encoding photosystem 1 subunits with molecular masses 11.0, 10.0 and 8.4 kDa from Chlamydomonas reinhardtii
    • 47. Franzén, L.G., Frank, G., Zuber, H. & Rochaix, J.-D. (1989) Isolation and characterization of cDNA clones encoding photosystem 1 subunits with molecular masses 11.0, 10.0 and 8.4 kDa from Chlamydomonas reinhardtii. Mol. Gen. Genet. 219, 137-144.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 137-144
    • Franzén, L.G.1    Frank, G.2    Zuber, H.3    Rochaix, J.-D.4
  • 48
    • 0028338910 scopus 로고
    • Characterization of the gene of the chloroplast Rieske iron-sulfur protein in Chlamydomonas reinhardtii. Indications for an uncleaved lumen targeting sequence
    • 48. de Vitry, C. (1994) Characterization of the gene of the chloroplast Rieske iron-sulfur protein in Chlamydomonas reinhardtii. Indications for an uncleaved lumen targeting sequence. J. Biol. Chem. 269, 7603-7609.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7603-7609
    • De Vitry, C.1
  • 49
    • 0001009719 scopus 로고
    • Primary structure of Chlamydomonas reinhardtii ribulose 1,5-bisphosphate carboxylase/oxygenase,activase and evidence for a single polypeptide
    • 49. Roesler, K.R. & Ogren, W.L. (1990) Primary structure of Chlamydomonas reinhardtii ribulose 1,5-bisphosphate carboxylase/oxygenase,activase and evidence for a single polypeptide. Plant Physiol. 94, 1837-1841.
    • (1990) Plant Physiol. , vol.94 , pp. 1837-1841
    • Roesler, K.R.1    Ogren, W.L.2
  • 50
    • 0023042758 scopus 로고
    • Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/oxygenase in Chlamydomonas reinhardti
    • 50. Goldschmidt-Clermont, M. & Rahire, M. (1986) Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/oxygenase in Chlamydomonas reinhardti. J. Mol. Biol. 191, 421-432.
    • (1986) J. Mol. Biol. , vol.191 , pp. 421-432
    • Goldschmidt-Clermont, M.1    Rahire, M.2
  • 51
    • 0018651445 scopus 로고
    • 2-terminal amino acid sequences of precursor and mature forms of the ribulose-1,5-bisphosphate carboxylase small subunit from Chlamydomonas reinhardtii
    • 2-terminal amino acid sequences of precursor and mature forms of the ribulose-1,5-bisphosphate carboxylase small subunit from Chlamydomonas reinhardtii. J. Cell Biol. 83, 615-622.
    • (1979) J. Cell Biol. , vol.83 , pp. 615-622
    • Schmidt, G.W.1    Devillers-Thiery, A.2    Desruisseaux, H.3    Blobel, G.4    Chua, N.H.5
  • 52
    • 0028398545 scopus 로고
    • Nucleotide sequence of a cDNA encoding the chloroplast sedoheptulose-1,7-bisphosphatase from Chlamydomonas reinhardtii
    • 52. Hahn, D. & Kuck, U. (1994) Nucleotide sequence of a cDNA encoding the chloroplast sedoheptulose-1,7-bisphosphatase from Chlamydomonas reinhardtii. Plant Physiol. 104, 1101-1102.
    • (1994) Plant Physiol. , vol.104 , pp. 1101-1102
    • Hahn, D.1    Kuck, U.2
  • 53
    • 0029310608 scopus 로고
    • Chlamydomonas reinhardtii thioredoxins: Structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties
    • 53. Stein, M., Jacquot, J.-P., Jeanette, E., Decottignies, P., Hodges, M., Lancelin, J.-M., Mittard, V., Schmitter, J.-M. & Miginiac-Maslow, M. (1995) Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties. Plant. Mol. Biol. 28, 487-503.
    • (1995) Plant. Mol. Biol. , vol.28 , pp. 487-503
    • Stein, M.1    Jacquot, J.-P.2    Jeanette, E.3    Decottignies, P.4    Hodges, M.5    Lancelin, J.-M.6    Mittard, V.7    Schmitter, J.-M.8    Miginiac-Maslow, M.9
  • 54
    • 0026501065 scopus 로고
    • PCR cloning of a nucleotidic sequence coding for the mature part of Chlamydomonas reinhardtii thioredoxin Ch2
    • 54. Jacquot, J.-P., Stein, M., Hodges, M. & Miginiac-Maslow, M. (1992) PCR cloning of a nucleotidic sequence coding for the mature part of Chlamydomonas reinhardtii thioredoxin Ch2. Nucleic Acids Res. 20, 617.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 617
    • Jacquot, J.-P.1    Stein, M.2    Hodges, M.3    Miginiac-Maslow, M.4
  • 55
    • 0025328146 scopus 로고
    • Purification, characterization, and complete amino acid sequence of a thioredoxin from a green alga, Chlamydomonas reinhardtii
    • 55. Decottignies, P., Schmitter, J.-M., Jacquot, J.-P., Dutka, S., Picaud, A. & Gadal, P. (1990) Purification, characterization, and complete amino acid sequence of a thioredoxin from a green alga, Chlamydomonas reinhardtii. Arch. Biochem. Biophys. 280, 112-121.
    • (1990) Arch. Biochem. Biophys. , vol.280 , pp. 112-121
    • Decottignies, P.1    Schmitter, J.-M.2    Jacquot, J.-P.3    Dutka, S.4    Picaud, A.5    Gadal, P.6
  • 56
    • 13344276445 scopus 로고
    • SN 1 and SN 2 mechanisms for the deprotection of synthetic peptides by hydrogen fluoride. Studies to minimize the tyrosine alkylation side reaction
    • 56. Tam, J.P., Heath, W.F. & Merrfield, R.B. (1983) SN 1 and SN 2 mechanisms for the deprotection of synthetic peptides by hydrogen fluoride. Studies to minimize the tyrosine alkylation side reaction. J. Am. Chem. Soc. 105, 6442-6445.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 6442-6445
    • Tam, J.P.1    Heath, W.F.2    Merrfield, R.B.3
  • 57
    • 0027490945 scopus 로고
    • Localization of a putative magnesium-binding site within the cytoplasmic domain of the sarcoplasmic reticulum Ca (2+)-ATPase
    • 57. Girardet, J.-L., Bally, I., Arlaud, G.J. & Dupont, Y. (1993) Localization of a putative magnesium-binding site within the cytoplasmic domain of the sarcoplasmic reticulum Ca (2+)-ATPase. Eur. J. Biochem. 217, 225-231.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 225-231
    • Girardet, J.-L.1    Bally, I.2    Arlaud, G.J.3    Dupont, Y.4
  • 58
    • 0025219614 scopus 로고
    • Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region
    • 58. Thielens, N.M., Van Dorsselaer, A., Gagnon, J. & Arlaud, G.J. (1990) Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region. Biochemistry 29, 3570-3578.
    • (1990) Biochemistry , vol.29 , pp. 3570-3578
    • Thielens, N.M.1    Van Dorsselaer, A.2    Gagnon, J.3    Arlaud, G.J.4
  • 59
    • 0000477505 scopus 로고    scopus 로고
    • GIFA V.4: A complete package for NMR data set processing
    • 59. Pons, J.L., Malliavin, T.E. & Delsuc, M.-A. (1996) GIFA V.4: a complete package for NMR data set processing. J. Biomol. NMR 8, 445-452.
    • (1996) J. Biomol. NMR , vol.8 , pp. 445-452
    • Pons, J.L.1    Malliavin, T.E.2    Delsuc, M.-A.3
  • 61
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • 61. Braunschweiler, L. & Ernst, R.R. (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 62
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartman-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartman-Hahn spectroscopy. J. Am. Chem. Soc. 107, 2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davies, D.G.1    Bax, A.2
  • 63
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • 63. Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 64
    • 49049150378 scopus 로고
    • Two-dimensional chemical exchange and cross relaxation spectroscopy of coupled nuclear spins
    • 64. Macura, S., Hyang, Y., Suter, D. & Ernst, R.R. (1981) Two-dimensional chemical exchange and cross relaxation spectroscopy of coupled nuclear spins. J. Magn. Reson. 43, 259-281.
    • (1981) J. Magn. Reson. , vol.43 , pp. 259-281
    • Macura, S.1    Hyang, Y.2    Suter, D.3    Ernst, R.R.4
  • 65
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • 65. Marion, D., Ikura, M., Tschudin, R. & Bax, A. (1989) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J. Magn. Reson. 85, 393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 68
    • 0003769049 scopus 로고    scopus 로고
    • Yale University Press, New Haven, CT, USA
    • 68. Brünger, A.T. (1996) X-PLOR, Version 3.851, Yale University Press, New Haven, CT, USA.
    • (1996) X-PLOR, Version 3.851
    • Brünger, A.T.1
  • 69
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 69. Koradi, R., Billeter, M. & Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 70
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • 70. Laskowski, R.A., Rullmann, J.A.C., MacArthur, M.W., Kaptein, R. & Thornton, J.M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 71
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding
    • 71. Nilges, M., Clore, G.M. & Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Lett. 239, 129-136.
    • (1988) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 72
    • 0026676167 scopus 로고
    • Sampling and efficiency of metric matrix distance geometry: A novel partial metrization algorithm
    • 72. Kuszewski, J., Nilges, M. & Brünger, A.T. (1992) Sampling and efficiency of metric matrix distance geometry: a novel partial metrization algorithm. J. Biomol. NMR. 2, 33-56.
    • (1992) J. Biomol. NMR , vol.2 , pp. 33-56
    • Kuszewski, J.1    Nilges, M.2    Brünger, A.T.3
  • 73
    • 0028187338 scopus 로고
    • NMR, alcohols, protein salvation and protein denaturation
    • (Jansson, B., Jörnvall, H., Rydberg, U., Terenius, L., Vallee, B.L., eds), Birkhäuser Verlag, Basel
    • 73. Wüthrich, K. (1994) NMR, alcohols, protein salvation and protein denaturation. Toward a Molecular Basis of Alcohol Use and Abuse (Jansson, B., Jörnvall, H., Rydberg, U., Terenius, L., Vallee, B.L., eds), pp. 261-268. Birkhäuser Verlag, Basel.
    • (1994) Toward A Molecular Basis of Alcohol Use and Abuse , pp. 261-268
    • Wüthrich, K.1
  • 74
    • 0027200689 scopus 로고
    • Common sequence motifs coding for higher-plant and prokaryotic O-acetylserine (thiol)-lyases: Bacterial origin of a chloroplast transit peptide?
    • 74. Rolland, N., Job, D. & Douce, R. (1993) Common sequence motifs coding for higher-plant and prokaryotic O-acetylserine (thiol)-lyases: bacterial origin of a chloroplast transit peptide? Biochem. J. 293, 829-833.
    • (1993) Biochem. J. , vol.293 , pp. 829-833
    • Rolland, N.1    Job, D.2    Douce, R.3
  • 75
    • 45149135688 scopus 로고
    • Chloroplast transit peptides from the green alga Chlamydomonas reinhardtii shares features with both mitochondrial and higher plant chloroplast presequences
    • 75. Franzèn, L.G., Rochaix, J.D. & von Heijne, G. (1990) Chloroplast transit peptides from the green alga Chlamydomonas reinhardtii shares features with both mitochondrial and higher plant chloroplast presequences. FEBS Lett. 260, 165-168.
    • (1990) FEBS Lett. , vol.260 , pp. 165-168
    • Franzèn, L.G.1    Rochaix, J.D.2    Von Heijne, G.3
  • 76
    • 0026097503 scopus 로고
    • Chloroplast transit peptides. The perfect random coil?
    • 76. von Heijne, G. & Nishikawa, K. (1991) Chloroplast transit peptides. The perfect random coil? FEBS Lett. 278, 1-3.
    • (1991) FEBS Lett. , vol.278 , pp. 1-3
    • Von Heijne, G.1    Nishikawa, K.2
  • 77
    • 0027748987 scopus 로고
    • Analysis of chloroplast transit peptide function using mutations in the carboxyl-terminal region
    • 77. Archer, E.K. & Keegstra, K. (1993) Analysis of chloroplast transit peptide function using mutations in the carboxyl-terminal region. Plant Mol. Biol. 23, 1105-1115.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 1105-1115
    • Archer, E.K.1    Keegstra, K.2
  • 78
    • 0032558380 scopus 로고    scopus 로고
    • Functional and structural properties of the mitochondrial outer membrane receptor Tom20
    • 78. Schleiff, E. & Turnbull, J.L. (1998) Functional and structural properties of the mitochondrial outer membrane receptor Tom20. Biochemistry 37, 13043-13051.
    • (1998) Biochemistry , vol.37 , pp. 13043-13051
    • Schleiff, E.1    Turnbull, J.L.2
  • 79
    • 0032558427 scopus 로고    scopus 로고
    • Characterization of the N-terminal targeting signal binding domain of the mitochondrial outer membrane receptor, Tom20
    • 79. Schleiff, E. & Turnbull, J.L. (1998) Characterization of the N-terminal targeting signal binding domain of the mitochondrial outer membrane receptor, Tom20. Biochemistry 37, 13052-13058.
    • (1998) Biochemistry , vol.37 , pp. 13052-13058
    • Schleiff, E.1    Turnbull, J.L.2


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