The sulfhydryl oxidase Erv1 is a substrate of the Mia40-dependent protein translocation pathway

FEBS Letters

Volumn 581, Issue 6, 2007, Pages 1098-1102

  Terziyska, Nadia ^a   Grumbt, Barbara ^a   Bien, Melanie ^b   Neupert, Walter ^a   Herrmann, Johannes M ^b   Hell, Kai ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b Rheinland Pfälzische Technische Universität Kaiserslautern Landau   (Germany)

Author keywords

Disulfide bond; Mia40 import pathway; Mitochondria; Protein import; Sulfhydryl oxidase Erv1

Indexed keywords

CARRIER PROTEIN; MEMBRANE PROTEIN; PROTEIN MIA40; SULFHYDRYL OXIDASE ERV1; THIOL OXIDASE; UNCLASSIFIED DRUG;

ARTICLE; DISULFIDE BOND; IMMUNOBLOTTING; MITOCHONDRIAL MEMBRANE; OUTER MEMBRANE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT;

EID: 33847726691     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.02.014     Document Type: Article

References (23)

1. Herrmann J.M., and Hell K. Chopped, trapped or tacked-protein translocation into the IMS of mitochondria. Trends Biochem. Sci. 30 (2005) 205-211
2. Endo T., Yamamoto H., and Esaki M. Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles. J. Cell Sci. 116 (2003) 3259-3267
3. Mokranjac D., and Neupert W. Protein import into mitochondria. Biochem. Soc. Trans. 33 (2005) 1019-1023
4. Rehling P., Brandner K., and Pfanner N. Mitochondrial import and the twin-pore translocase. Nat. Rev. Mol. Cell. Biol. 5 (2004) 519-530
5. Koehler C.M. New developments in mitochondrial assembly. Annu. Rev. Cell. Dev. Biol. 20 (2004) 309-335
6. Koehler C.M. The small Tim proteins and the twin Cx(3)C motif. Trends Biochem. Sci. 29 (2004) 1-4
7. Beers J., Glerum D.M., and Tzagoloff A. Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle. J. Biol. Chem. 272 (1997) 33191-33196
8. Gabriel K., Milenkovic D., Chacinska A., Muller J., Guiard B., Pfanner N., and Meisinger C. Novel mitochondrial intermembrane space proteins as substrates of the MIA import pathway. J. Mol. Biol. 365 (2007) 612-620
9. Lu H., Allen S., Wardleworth L., Savory P., and Tokatlidis K. Functional TIM10 chaperone assembly is redox-regulated in vivo. J. Biol. Chem. 279 (2004) 18952-18958
10. Lutz T., Neupert W., and Herrmann J.M. Import of small Tim proteins into the mitochondrial intermembrane space. EMBO J. 22 (2003) 4400-4408
11. Chacinska A., et al. Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins. EMBO J. 23 (2004) 3735-3746
12. Naoe M., Ohwa Y., Ishikawa D., Ohshima C., Nishikawa S., Yamamoto H., and Endo T. Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space. J. Biol. Chem. 279 (2004) 47815-47821
13. Terziyska N., Lutz T., Kozany C., Mokranjac D., Mesecke N., Neupert W., Herrmann J.M., and Hell K. Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions. FEBS Lett. 579 (2005) 179-184
14. Allen S., Balabanidou V., Sideris D.P., Lisowsky T., and Tokatlidis K. Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. J. Mol. Biol. 353 (2005) 937-944
15. Mesecke N., Terziyska N., Kozany C., Baumann F., Neupert W., Hell K., and Herrmann J.M. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 121 (2005) 1059-1069
16. Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B., Pfanner N., and Chacinska A. The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins. J. Mol. Biol. 353 (2005) 485-492
17. Lange H., Lisowsky T., Gerber J., Muhlenhoff U., Kispal G., and Lill R. An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep. 2 (2001) 715-720
18. Hofhaus G., Lee J.E., Tews I., Rosenberg B., and Lisowsky T. The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre. Eur. J. Biochem. 270 (2003) 1528-1535
19. Gross E., Sevier C.S., Vala A., Kaiser C.A., and Fass D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9 (2002) 61-67
20. Coppock D.L., and Thorpe C. Multidomain flavin-dependent sulfhydryl oxidases. Antioxid. Redox Signal. 8 (2006) 300-311
21. Allen S., Lu H., Thornton D., and Tokatlidis K. Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10. J. Biol. Chem. 278 (2003) 38505-38513
22. Arnesano F., Balatri E., Banci L., Bertini I., and Winge D.R. Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. Structure 13 (2005) 713-722
23. Webb C.T., Gorman M.A., Lazarou M., Ryan M.T., and Gulbis J.M. Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller. Mol. Cell 21 (2006) 123-133