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  • Abe, Y., Shodai, T., Muto, T., Mihara, K., Torii, H., Nishikawa, S.I., Endo, T., Kohda, D. (2000) Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell, 100, 551560.
  • Allison, D.S. & Schatz, G. (1986) Artificial mitochondrial presequences. Proc. Natl Acad. Sci. USA, 83, 90119015.
  • Arabidopsis Genome Initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature, 408, 796815.DOI: 10.1038/35048692
  • Boutry, M. & Goffeau, A. (1982) Alterations of the alpha or beta subunits of the mitochondrial ATPase in yeast mutants. Eur. J. Biochem. 125, 471477.
  • Chaumont, F., De Catro Silva-Filho, M., Thomas, D., Leterme, S., Boutry, M. (1994) Truncated presequences of mitochondrial F1-ATPase beta subunit from Nicotiana plumbaginifolia transport CAT and GUS proteins into mitochondria of transgenic tobacco. Plant Mol. Biol. 24, 631641.
  • Chou, P.Y. & Fasman, G.D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzym. 47, 145148.
  • De Castro Silva-Filho, M., Chaumont, F., Leterme, S., Boutry, M. (1996) Mitochondrial and chloroplast targeting sequences in tandem modify protein import specificity in plant organelles. Plant Mol. Biol. 30, 769780.
  • De Castro Silva-Filho, M., Wieërs, M.C., Flügge, U.I., Chaumont, F., Boutry, M. (1997) Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein. J. Biol. Chem. 272, 1526415269.
  • De Kerchove d'Exaerde, A., Supply, P., Dufour, J.P., Bogaerts, P., Thinès, D., Goffeau, A., Boutry, M. (1995) Functional complementation of a null mutation of the yeast Saccharomyces cerevisiae plasma membrane H(+)-ATPase by a plant H(+)-ATPase gene. J. Biol. Chem. 270, 2382823837.
  • Eisenberg, D., Schwarz, E., Komarony, M., Wall, R. (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125142.
  • Foury, F. (1989) Cloning and sequencing of the nuclear gene MIP1 encoding the catalytic subunit of the yeast mitochondrial DNA polymerase. J. Biol. Chem. 264, 205552220560.
  • Garnier, J., Gibrat, J.F., Robson, B. (1996) GOR method for predicting protein secondary structure from amino acid sequence. Meth. Enzymol. 266, 540553.
  • Geourjon, C. & Deléage, G. (1995) SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput. Appl. Biosci. 11, 681684.
  • Glaser, E., Sjöling, S., Tanudji, M., Whelan, J. (1998) Mitochondrial protein import in plants. Signals, sorting, targeting, processing and regulation. Plant Mol. Biol. 38, 311338.
  • Grebenok, R.J., Pierson, E., Lambert, G.M., Gong, F.C., Afonso, C.L., Haldeman-Cahill, R., Carrington, J.C., Galbraith, D.W. (1997) Green-fluorescent protein fusions for efficient characterization of nuclear targeting. Plant J. 11, 573586.
  • Hammen, P.K., Waltner, M., Hahnemann, B., Heard, T.S., Weiner, H. (1996) The role of positive charges and structural segments in the presequence of rat liver aldehyde dehydrogenase in import into mitochondria. J. Biol. Chem. 271, 2104121048.
  • Heard, T.S. & Weiner, H. (1998) A regional net charge and structural compensation model to explain how negatively charged amino acids can be accepted within a mitochondrial leader sequence. J. Biol. Chem. 273, 2938929393.
  • Heins, L. & Schmitz, U.K. (1996) A receptor for protein import into potato mitochondria. Plant J. 9, 829839.
  • Horsch, R.B., Klee, H.J., Stachel, S., Winans, S.C., Nester, E.W., Rogers, S.G., Fraley, R.T. (1986) Analysis of Agrobacterium tumefaciens virulence mutants in leaf discs. Proc. Natl Acad. Sci. USA, 83, 25712576.
  • Koehler, C.M. (2000) Protein translocation pathways of the mitochondrion. FEBS Lett. 476, 2731.
  • Kyte, J. & Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105132.
  • Lemire, B.D., Fankhauser, C., Baker, A., Schatz, G. (1989) The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity. J. Biol. Chem. 264, 2020620215.
  • Lukaszewicz, M., Jérouville, B., Boutry, M. (1998) Signs of translational regulation within the transcript leader of a plant plasma membrane H(+)-ATPase gene. Plant J. 14, 413423.
  • Macasev, D., Newbigin, E., Whelan, J., Lithgow, T. (2000) How do plant mitochondria avoid importing chloroplast proteins? Components of the import apparatus Tom20 and Tom22 from Arabidopsis differ from their fungal counterparts. Plant Physiol. 123, 811816.
  • Neupert, W. (1997) Protein import into mitochondria. Annu. Rev. Biochem. 66, 863917.
  • Ni, L., Heard, T.S., Weiner, H. (1999) In vivo mitochondrial import. A comparison of leader sequence charge and structural relationships with the in vitro model resulting in evidence for co-translational import. J. Biol. Chem. 274, 1268512691.
  • Roise, D., Theiler, F., Horvath, S.J., Tomich, J.M., Richards, J.H., Allison, D.S., Schatz, G. (1988) Amphiphilicity is essential for mitochondrial presequence function. EMBO J. 7, 649653.
  • Schneider, G., Sjöling, S., Wallin, E., Wrede, P., Glaser, E., Von Heijne, G. (1998) Feature-extraction from endopeptidase cleavage sites in mitochondrial targeting peptides. Proteins, 30, 4960.DOI: 10.1002/(sici)1097-0134(19980101)30:1<49::aid-prot5>3.3.co;2-p
  • Tanudji, M., Sjöling, S., Glaser, E., Whelan, J. (1999) Signals required for the import and processing of the alternative oxidase into mitochondria. J. Biol. Chem. 274, 12861293.
  • Thomas, B.J. & Rothstein, R. (1989) Elevated recombination rates in transcriptionally active DNA. Cell, 56, 619639.
  • Thompson, J.D., Higgins, D.G., Gibson, T.J. (1994) clustal w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22, 46734680.
  • Vassarotti, A., Stroud, R., Douglas, M. (1987) Independent mutations at the amino terminus of a protein act as surrogate signals for mitochondrial import. EMBO J. 6, 705711.
  • Von Heijne, G. (1986) Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 5, 13351342.
  • Wang, Y. & Weiner, H. (1993) The presequence of rat liver aldehyde dehydrogenase requires the presence of an alpha-helix at its N-terminal region which is stabilized by the helix at its C termini. J. Biol. Chem. 268, 47594765.
  • Zhao, R., Moriau, L., Boutry, M. (1999) Expression analysis of the plasma membrane H+-ATPase pma4 transcription promoter from Nicotiana plumbaginifolia activated by the CaMV 35S promoter enhancer. Plant Sci. 149, 157165.
  • Zwizinski, C. & Neupert, W. (1983) Precursor proteins are transported into mitochondria in the absence of proteolytic cleavage of the additional sequences. J. Biol. Chem. 258, 1334013346.