Yeast aconitase in two locations and two metabolic pathways: Seeing small amounts is believing

Molecular Biology of the Cell

Volumn 16, Issue 9, 2005, Pages 4163-4171

  Regev Rudzki, Neta ^a   Karniely, Sharon ^a   Ben Haim, Nitzan Natani ^a   Pines, Ophry ^a  

^a HEBREW UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; BETA GALACTOSIDASE; GLYOXYLIC ACID; HYBRID PROTEIN; ISOENZYME; PEPTIDE;

ACO1 URA3 GENE; ARTICLE; CELL COMPARTMENTALIZATION; CITRIC ACID CYCLE; CONTROLLED STUDY; CYTOSOL; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME METABOLISM; GENETIC COMPLEMENTATION; HYBRID GENE; ISOLATION PROCEDURE; MITOCHONDRION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN TARGETING; SACCHAROMYCES CEREVISIAE;

ACETATES; ACONITATE HYDRATASE; AMINO ACID SEQUENCE; BETA-GALACTOSIDASE; CYTOSOL; ETHANOL; FUNGAL PROTEINS; IRON REGULATORY PROTEIN 1; ISOENZYMES; MITOCHONDRIA; MOLECULAR SEQUENCE DATA; MUTATION; ORGANISMS, GENETICALLY MODIFIED; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SIGNAL TRANSDUCTION;

SACCHAROMYCES CEREVISIAE;

EID: 24344441532     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-11-1028     Document Type: Article

References (28)

1. Abbas-Terki, T., and Picard, D. (1999). α-Complemented β-galactosidase. An in vivo model substrate for the molecular chaperone heat-shock protein 90 in yeast. Eur. J. Biochem. 266, 517-523.
2. Alani, E., and Kleckner, N. (1987). A new type of fusion analysis applicable to many organisms: protein fusions to the URA3 gene of yeast. Genetics 117, 5-12.
3. Ausubel, F., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K. (eds.) (1991). Current Protocols in Molecular Biology, New York: Greene Publishing Associates.
4. Branda, S. S., and Isaya, G. (1995). Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase. J. Biol. Chem. 270, 27366-27373.
5. Charlton, W. L., Johnson, B., Graham, I. A., and Baker, A. (2004). Non-coordinate expression of peroxisome biogenesis, β-oxidation and glyoxylate cycle genes in mature Arabidopsis plants. Plant Cell Rep. 23, 647-653.
6. Dubaquie, Y., Looser, R., Funfschilling, U., Jeno, P., and Rospert, S. (1998). Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. EMBO J. 17, 5868-5876.
7. Fansler, B., and Lowenstein, J. M. (1969). Aconitase from pig heart. Methods Enzymol. 13, 26-30.
8. Fukuhara, H. (2003). The Kluyver effect revisited. FEMS Yeast Res. 3, 327-331.
9. Gangloff, S. P., Marguet, D., and Lauquin, G. J. (1990). Molecular cloning of the yeast mitochondrial aconitase gene (ACO1) and evidence of a synergistic regulation of expression by glucose plus glutamate. Mol. Cell. Biol. 10, 3551-3561.
10. Gardner, P. R. (1997). Superoxide-driven aconitase FE-S center cycling. Biosci. Rep. 17, 33-42.
11. Gerber, J., Muhlenhoff, U., and Lill, R. (2003). An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 4, 906-911.
12. Hentze, M. W., and Kuhn, L. C. (1996). Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. USA 93, 8175-8182.
13. Knox, C., Sass, E., Neupert, W., and Pines, O. (1998). Import into mitochondria, folding and retrograde movement of fumarase in yeast. J. Biol. Chem. 273, 25587-25593.
14. McAlister-Henn, L., and Small, W. C. (1997). Molecular genetics of yeast TCA cycle isozymes. Prog. Nucleic Acid Res. Mol. Biol. 57, 317-339.
15. McCammon, M. T., Veenhuis, M., Trapp, S. B., and Goodman, J. M. (1990). Association of glyoxylate and β-oxidation enzymes with peroxisomes of Saccharomyces cerevisiae. J. Bacteriol. 172, 5816-5827.
16. Moosmann, P., and Rusconi, S. (1996). α Complementation of LacZ in mammalian cells. Nucleic Acids Res. 24, 1171-1172.
17. Muhlenhoff, U., Balk, J., Richhardt, N., Kaiser, J. T., Sipos, K., Kispal, G., and Lill, R. (2004). Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae. J. Biol. Chem. 279, 36906-36915.
18. Mumberg, D., Muller, R., and Funk, M. (1994). Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res. 22, 5767-5768.
19. Nakai, Y., Nakai, M., Hayashi, H., and Kagamiyama, H. (2001). Nuclear localization of yeast Nfs1p is required for cell survival. J. Biol. Chem. 276, 8314-8320.
20. Nakai, Y., Umeda, N., Suzuki, T., Nakai, M., Hayashi, H., Watanabe, K., and Kagamiyama, H. (2004). Yeast Nfs1p is involved in thio-modification of both mitochondrial and cytoplasmic tRNAs. J. Biol. Chem. 279, 12363-12368.
21. Rouault, T. A., and Klausner, R. D. (1996). Iron-sulfur clusters as biosensors of oxidants and iron. Trends Biochem. Sci. 21, 174-177.
22. Sass, E., Blachinsky, E., Karniely, S., and Pines, O. (2001). Mitochondrial and cytosolic isoforms of yeast fumarase are derivatives of a single translation product and have identical amino termini. J. Biol. Chem. 276, 46111-46117.
23. Sass, E., Karniely, S., and Pines, O. (2003). Folding of fumarase during mitochondrial import determines its dual targeting in yeast. J. Biol. Chem. 278, 45109-45116.
24. Stein, I., Peleg, Y., Even-Ram, S., and Pines, O. (1994). The single translation product of the FUM1 gene (fumarase) is processed in mitochondria before being distributed between the cytosol and mitochondria in Saccharomyces cerevisiae. Mol. Cell. Biol. 14, 4770-4778.
25. Strobel, G., Zollner, A., Angermayr, M., and Bandlow, W. (2002). Competition of spontaneous protein folding and mitochondrial import causes dual subcellular location of major adenylate kinase. Mol. Biol. Cell 13, 1439-1448.
26. Ullmann, A., Jacob, F., and Monod, J. (1967). Characterization by in vitro complementation of a peptide corresponding to an operator-proximal segment of the β-galactosidase structural gene of Escherichia coli. J. Mol. Biol. 24, 339-343.
27. Waizenegger, T., Habib, S. J., Lech, M., Mokranjac, D., Paschen, S. A., Hell, K., Neupert, W., and Rapaport, D. (2004). Tob38, a novel essential component in the biogenesis of β-barrel proteins of mitochondria. EMBO Rep. 5, 704-709.
28. Wu, M., and Tzagoloff, A. (1987). Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are encoded by a single nuclear gene FUM1 J. Biol. Chem. 262, 12275-12282.