Dual subcellular distribution of cytochrome b5 in plant, cauliflower, cells

Journal of Biochemistry

Volumn 133, Issue 1, 2003, Pages 115-121

  Zhao, Jingfang ^a,b   Onduka, Toshimitu ^a,c   Kinoshita, Jun ya ^a   Honsho, Masanori ^a,d   Kinoshita, Toshinori ^a   Shimazaki, Ken ichiro ^a   Ito, Akio ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b Panapharm Laboratories Co Ltd   (Japan)

^c FISHERIES RESEARCH AGENCY   (Japan)

^d MAX PLANCK INSTITUTE OF MOLECULAR CELL BIOLOGY AND GENETICS   (Germany)

Author keywords

Cytochrome b5; Dual subcellular localization; Endoplasmic reticulum; Mitochondria; Targeting signal

Indexed keywords

ANTIMYCIN A1; CYTOCHROME B; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CAULIFLOWER; CELL FRACTIONATION; CELLULAR DISTRIBUTION; ENDOPLASMIC RETICULUM; NONHUMAN; ONION; PLANT CELL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN TRANSPORT; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; TRANSPORT KINETICS;

AMINO ACIDS, BASIC; ANIMALS; BRASSICA; COS CELLS; CYTOCHROMES B5; ENDOPLASMIC RETICULUM; FLUORESCENT ANTIBODY TECHNIQUE; MICROSOMES; MITOCHONDRIA; NADH DEHYDROGENASE; ONIONS; PLANTS; PROTEIN TRANSPORT; RATS; YEASTS;

ALLIUM CEPA; BRASSICA; BRASSICA OLERACEA VAR. BOTRYTIS; MAMMALIA;

EID: 0037281652     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg009     Document Type: Article

References (27)

1. Schatz, G. and Dobberstein, B. (1996) Common principles of protein translocation across membranes. Science 271, 1519-1526
2. Walter, P., Gilmore, R., and Blobel, G. (1984) Protein translocation across the endoplasmic reticulum. Cell 38, 5-8
3. Schatz, G. (1989-90) Transport of proteins into mitochondria. Harvey Lect. 85, 109-126
4. Rapoport, T.A., Jungnickel, B., and Kutay, U. (1996) Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303
5. 5 J. Biochem. 87, 63-71
6. Lederer, F., Ghrir, R., Guiard, B., Cortial, S., and Ito, A. (1983) Two homologous cytochromes b5 in a single cell. Eur. J. Biochem. 132, 95-102
7. 5 are necessary for its targeting to the endoplasmic reticulum. EMBO J. 11, 4197-4203
8. De Silvestris, M., D'Arrigo, A., and Borgese, N. (1995) The targeting information of the mitochondrial outer membrane isoform of cytochrome b5 is contained within the carboxyl-terminal region. FEBS Lett. 370, 69-74
9. Kuroda, R., Ikenoue, T., Honsho, M., Tsujimoto, S., Mitoma, J.Y., and Ito, A. (1998) Charged amino acids at the carboxyl-terminal portions determine the intracellular locations of two isoforms of cytochrome b5. J. Biol. Chem. 273, 31097-31102
10. Kearns, E.V., Keck, P., and Somerville, C.R. (1992) Primary structure of cytochrome b5 from cauliflower (Brassica oleracea L.) deduced from peptide and cDNA sequences. Plant Physiol. 99, 1254-1257
11. Smith, M.A., Stobart, A.K., Shewry, P.R., and Napier, J.A. (1994) Tobacco cytochrome b5: cDNA isolation, expression analysis and in vitro protein targeting. Plant Mol. Biol. 25, 527-537
12. Saito, T., Morio, T., and Ochiai, H. (2000) A second functional delta5 fatty acid desaturase in the cellular slime mould Dictyostelium discoideum. Eur. J. Biochem. 267, 1813-1818
13. Kjellbom, P., Larsson, C., Askerlund, P., Schelin, C., and Widell, S. (1985) Cytochrome P-450/420 in plant plasma membranes; a possible component of the blue-light-reducible fiavo flavoprotein-cytochrome complex. Photochem. Photobiol. 42, 779-783
14. Ito, A. (1980) Cytochrome b5-like hemoprotein of outer mitochondrial membrane, OM cytochrome b: II. Contribution of OM cytochrome b to rotenone-insensitive NADH-cytochrome c reductase activity J. Biochem. 87, 73-80
15. Vergeres, G. and Waskell, L. (1992) Expression of cytochrome b5 in yeast and characterization of mutants of the membrane-anchoring domain. J. Biol. Chem. 267, 12583-12591
16. Itai, C. and Roth-Bejerano, N. (1986) The effect of abscisic acid on epidermal cells; protoplast swelling and ATPase activity. Physiol. Plant. 66, 664-668
17. Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983) Transformation of intact yeast cells treated with alkalin cations. J. Bacteriol. 153, 163-168
18. Normington, K., Kohno, K., Kozutsumi, Y., Gething, M.J., and Sambrook, J. (1989) S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57, 1223-1236
19. Meldolesi, J., Corte, G., Pietrini, G., and Borgese, N. (1980) Localization and biosynthesis of NADH-cytochrome b5 reductase, an integral membrane protein, in rat liver cells. II. Evidence that a single enzyme accounts for the activity in its various subcellular locations. J. Cell Biol. 85, 516-526
20. Kuwahara, S., Okada, Y., and Omura, T. (1978) Evidence for molecular identity of microsomal and mitochondrial NADH-cytochrome b5 reductases of rat liver. J. Biochem. 83, 1049-1059
21. Nakayasu, H., Mihara, K., and Sato, R. (1978) Purification and properties of a membrane-bound aldehyde dehydrogenase from rat liver microsomes. Biochem. Biophys. Res. Commun. 83, 697-703
22. Morgenstern, R., Lundqvist, G., Andersson, G., Balk, L., and DePierre, J.W. (1984) The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms. Biochem. Pharmacol. 33, 3609-3614
23. Nishino, H. and Ito, A. (1990) Purification and properties of glutathione S-transferase from outer mitochondrial membrane of rat liver. Biochem. Int. 20, 1059-1066
24. Krajewski, S., Tanaka, S., Takayama, S., Schibler, M.J., Fenton, W., and Reed, J.C. (1993) Investigation of the subeellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53, 4701-4714
25. Nguyen, M., Millar, D.G., Yong, V.W., Korsmeyer, S.J., and Shore, G.C. (1993) Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 268, 25265-25268
26. Tsujimoto, Y. and Croce, C.M. (1986) Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc. Natl. Acad. Sci. USA 83, 5214-5218
27. Ito, A., Hayashi, S., and Yoshida, T. (1981) Participation of a cytochrome b5-like hemoprotein of outer mitochondrial membrane (OM cytochrome b) in NADH-semidehydroascorbic acid reductase activity of rat liver. Biochem. Biophys. Res. Commun. 101,591-598