Examination of mitochondrial protein targeting of haem synthetic enzymes: In vivo identification of three functional haem-responsive motifs in 5-aminolaevulinate synthase

Biochemical Journal

Volumn 386, Issue 2, 2005, Pages 381-386

  Dailey, Tamara A ^a   Woodruff, John H ^a   Dailey, Harry A ^a  

^a UNIVERSITY OF GEORGIA   (United States)

Author keywords

Aminolaevulinate; Ferrochelatase; Haem; Mitochondria; Protoporphyrinogen; Targeting

Indexed keywords

BACTERIA; BINDING ENERGY; BIOSYNTHESIS; CELLS;

ERYTHROID PRECURSOR CELLS; MITOCHONDRION; PROTOPORPHYRINOGEN OXIDASE (PPO);

ENZYMES;

5 AMINOLEVULINATE SYNTHASE; 5 AMINOLEVULINATE SYNTHASE 1; 5 AMINOLEVULINATE SYNTHASE 2; BACTERIAL ENZYME; COPROPORPHYRINOGEN OXIDASE; FERROCHELATASE; HEME; HOUSEKEEPING PROTEIN; ISOENZYME; MITOCHONDRIAL PROTEIN; PROTOPORPHYRINOGEN OXIDASE; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BACILLUS SUBTILIS; HUMAN; IN VIVO STUDY; INTRACELLULAR TRANSPORT; MAMMAL CELL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN SYNTHESIS; PROTEIN TARGETING; PROTEIN TRANSPORT;

5-AMINOLEVULINATE SYNTHETASE; AMINO ACID MOTIFS; ANIMALS; CARCINOMA, HEPATOCELLULAR; CELL LINE, TUMOR; CLONING, MOLECULAR; COPROPORPHYRINOGEN OXIDASE; EXONS; FERROCHELATASE; FLAVOPROTEINS; HEME; HUMANS; LIVER NEOPLASMS, EXPERIMENTAL; MICE; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PEPTIDE FRAGMENTS; PROTOPORPHYRINOGEN OXIDASE; PROTOPORPHYRINS;

BACILLUS SUBTILIS; MAMMALIA;

EID: 14844322251     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040570     Document Type: Article

References (30)

1. Dailey, H. A. (1997) Enzymes of heme biosynthesis. J. Biol. Inorg. Chem. 2 411-417
2. Sadlon, T. J., Dell'Oso, T., Surinya, K. H. and May, B. K. (1999) Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis. Int. J. Biochem. Cell Biol. 31, 1153-1167
3. Ades, I. Z. and Harpe, K. G. (1981) Biogenesis of mitochondrial proteins: identification of the mature and precursor forms of the subunit of δ-aminolevulinic acid synthase from embryonic chick liver. J. Biol. Chem. 250, 9329-9333
4. Elder, G. H. and Evans, J. O. (1978) Evidence that coproporphyrinogen oxidase activity of rat liver is situated in the intermembrane space of mitochondria. Biochem. J. 172, 345-347
5. Ferreira, G. C., Andrew, T., Karr, S. W. and Dailey, H. A. (1988) Organization of the terminal two enzymes of the heme biosynthetic pathway. Orientation of protoporphyrinogen oxidase and evidence for a membrane complex. J. Biol. Chem. 263, 3835-3839
6. Harbin, B. M. and Dailey, H. A. (1985) Orientation of ferrochelatase in bovine liver mitochondrial. Biochemistry 24, 366-370
7. Furuyama, K., Harigae, H. and Sassa, S. (2001) Structure of the human succinyl CoA synthetase bet A-subunit gene and increased gene expression during erythroid differentiation. Blood 98, 29
8. Lathrop, J. T. and Timko, M. P. (1993) Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science 259, 522-525
9. Delfau-Larue, M. H., Martasek, P. and Grandchamp, B. (1994) Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping. Hum. Mol. Genet. 3, 1325-1330
10. Medlock, A. and Dailey, H. A. (1996) Human coproporphyrinogen oxidase is not a metalloenzyme. J. Biol. Chem. 271, 32507-32510
11. Arnould, S., Takahashi, M. and Camadro, J.-M. (1999) Acylation stabilizes a protease-resistant conformation of protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides. Proc. Natl. Acad. Sci. U.S.A. 96, 14825-14830
12. Koch, M., Breithaupt, C., Kiefersauer, R., Greigang, J., Huber, R. and Messerschmidt, A. (2004) Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis. EMBO J. 23, 1-9
13. Dailey, T. A. and Dailey, H. A. (1996) Human protoporphyrinogen oxidase. Expression, purification, and characterization of the cloned enzyme. Protein Sci. 5, 98-105
14. Karr, S. R. and Dailey, H. A. (1988) The synthesis of marine ferrochelatase in vitro and in vivo. Biochem. J. 254, 799-803
15. Dailey, H. A., Dailey, T. A., Wu, C.-K., Medlock, A. E., Wang, K.-F., Rose, J. P. and Wang, B.-C. (2000) Ferrochelatase at the millennium: structures, mechanisms, and [2Fe-2S] clusters. Cell. Mol. Life Sci. 57, 1909-1926
16. Kohno, H., Furukawa, T., Yoshinaga, T., Tokunaga, R. and Taketani, S. (1993) Coproporphyrinogen oxidase: purification, molecular cloning, and induction of mRNA during erythroid differentiation. J. Biol. Chem. 268, 21359-21363
17. Eldridge, M. G. and Dailey, H. A. (1992) Serum free, defined medium for the growth and differentiation of murine erythroleukemia cells. Biotechniques 12, 848-852
18. Emanuelsson, O., Nielsen, H., Brunak, S. and von Heljne, G. (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence, J. Mol. Biol. 300, 1005-1016
19. Conder, L. H., Woodard, S. I. and Dailey, H. A. (1991) Multiple mechanisms for regulation of haem synthesis during erythroid cell differentiation. Possible role for coproporphyrinogen oxidase. Biochem. J. 275, 321-326
20. Takahashi, S., Taketani, S., Akasaka, J. E., Kobayashi, A., Hayashi, N., Yamamoto, M. and Nagai, T. (1998) Differential regulation of coproporphyrinogen oxidase gene between erythroid and nonerythroid cells. Blood 92, 3436-3444
21. Binda, C., Newton-Vinson, P., Hubalek, F., Edmondson, D. E. and Mattevi, A. (2002) Structure of human monoamine oxidase B, a drug target for the treatment of neurologica disorders. Nat. Struct. Biol. 9, 22-26
22. Dailey, T. A., Meissner, P. and Dailey, H. A. (1994) Expression of a cloned protoporphyrinogen oxidase. J. Biol. Chem. 269, 813-815
23. Prasad, A. R. K. and Dailey, H. A. (1995) Effect of cellular location on the function of ferrochelatase. J. Biol. Chem. 270, 18198-18200
24. Yamauchi, K., Hayashi, N. and Kikuchi, G. (1980) Translocation of 5-aminolevolinate synthase from the cytosol to the mitochondria and its regulation by hemin in rat liver. J. Biol. Chem. 255, 1746-1751
25. Susa, S., Daimon, M., Ono, H., Li, S., Yoshida, T. and Kato, T. (2002) Heme inhibits the mitochondrial import of coproporphyrinogen oxidase. Blood 100, 4678-4679
26. Dailey, T. A. and Dailey, H. A. (1998) Identification of an FAD superfamily containing protoporphyrinogen oxidase, monoamine oxidases, and phytoene desaturase. Expression and characterization of phytoene desaturase of Myxococcus xanthus. J. Biol. Chem. 273, 13658-13662
27. Lithgow, T. (2000) Targeting of proteins to mitochondria. FEBS Lett. 476, 22-26
28. Fraunberg, M. V., Nyronen, T. and Kauppinen, R. (2003) Mitochondrial targeting of normal and mutant protoporphyrinogen oxidase. J. Biol. Chem. 278, 13376-13381
29. Morgan, R. R., Errington, R. and Elder, G. H. (2004) Identification of sequences requited for the import of human protoporphyrinogen oxidase to mitochondria. Biochem. J. 377, 281-287
30. Gora, M., Rytka, J. and Labbe-Bois, R. (1999) Activity and cellular location in Saccharomyces cerevisiae of chimeric mouse/yeast and Bacillus subtilis/yeast ferrochelatases. Arch. Biochem. Biophys. 361, 231-240