Old yellow enzyme protects the actin cytoskeleton from oxidative stress

Molecular Biology of the Cell

Volumn 15, Issue 10, 2004, Pages 4522-4531

  Haarer, Brian K ^a   Amberg, David C ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; HYDROGEN PEROXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE;

ACTIN FILAMENT; ARTICLE; CELL PROTECTION; CYTOSKELETON; DISULFIDE BOND; ENZYME ACTIVITY; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE;

ACTINS; CYTOSKELETON; DISULFIDES; HUMANS; MODELS, MOLECULAR; MUTATION; NADPH DEHYDROGENASE; OXIDATION-REDUCTION; OXIDATIVE STRESS; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TWO-HYBRID SYSTEM TECHNIQUES;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 4644328677     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-06-0445     Document Type: Article

References (32)

1. Amberg, D.C., Basart, E., and Botstein, D. (1995a). Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 2, 28-35.
2. Amberg, D.C., Botstein, D., and Beasley, E.M. (1995b). Precise gene disruption in Saccharomyces cerevisiae by double fusion PCR. Yeast 11, 1275-1280.
3. Ayscough, K.R., Stryker, J., Pokala, N., Sanders, M., Crews, P., and Drubin, D.G. (1997). High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 137, 399-416.
4. Belmont, L.D., Patterson, G.M., and Drubin, D.G. (1999). New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites. J. Cell Sci. 112, 1325-1336.
5. Bencsath, F.A., Shartava, A., Monteiro, C.A., and Goodman, S.R. (1996). Identification of the disulfide-linked peptide in irreversibly sickled cell β-actin. Biochem. 35, 4403-4408.
6. Dalle-Donne, I., Rossi, R., Milzani, A., Di Simplicio, P., and Columbo, R. (2001). The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself. Free Radic. Biol. Med. 31, 1624-1632.
7. Durfee, T., Becherer, K., Chen, P.-L., Yeh, S.-H., Yang, Y., Kilburn, A.E., Lee, W.-H., and Elledge, S.J. (1993). The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 7, 555-569.
8. Fabry, M.E., Fine, E., Rajanayagam, V., Factor, S.M., Gore, J., Sylla, M., and Nagel, R.L. (1992). Demonstration of endothelial adhesion of sickle cells in vivo: a distinct role for deformable sickle cell discocytes. Blood 79, 1602-1611.
9. Fox, K.M., and Karplus, P.A. (1994). Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins. Structure 2, 1089-1105.
10. Gasch, A.P., Spellman, P.T., Kao, C.M., Carmel-Harel, O., Eisen, M.B., Storz, G., Botstein, D., and Brown, P.O. (2000). Genomic expression programs in the response of yeast cells to environmental changes. Mol. Biol. Cell 11, 4241-4257.
11. Gourley, C.W., Carpp, L.N., Timpson, P., Winder, S.J., and Ayscough, K.R. (2004). A role for the actin cytoskeleton in cell death and aging in yeast. J. Cell Biol. 164, 803-809.
12. Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., and Pease, L.R. (1989). Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
13. Humphrey, W., Dalke, A., and Schulten, K. (1996). VMD: visual molecular dynamics. J. Mol. Graph. 14, 33-38, 27-28.
14. Jazwinski, S.M. (2002). Growing old: metabolic control and yeast aging. Annu. Rev. Microbiol. 56, 769-792.
15. Kaul, D.K., Fabry, M.E., Windisch, P., Baez, S., and Nagel, R.L. (1983). Erythrocytes in sickle cell anemia are heterogeneous in their rheological and hemodynamic characteristics. J. Clin. Investig. 72, 22-31.
16. Kellis, M., Patterson, N., Endrizzi, M., Birren, B., and Lander, E.S. (2003). Sequencing and comparison of yeast species to identify genes and regulatory elements. Nature 423, 233-234.
17. Kosower, N.S., and Kosower, E.M. (1995). Diamide: an oxidant probe for thiols. Methods Enzymol. 251, 123-133.
18. Laun, P., Pichova, A., Madeo, F., Fuchs, J., Ellinger, A., Kohlwein, S., Dawes, I., Frohlich, K.U., and Breitenbach, M. (2001). Aged mother cells of Saccharomyces cerevisiae show markers of oxidative stress and apoptosis. Mol Microbiol 39, 1166-1173.
19. Lux, S.E., John, K.M., and Karnovsky, M.J. (1976). Irreversible deformation of the spectrin-actin lattice in irreversibly sickled cells. J. Clin. Investig. 58, 955-963.
20. Niino, Y.S., Chakraborty, S., Brown, B., and Massey, V. (1995). A new old yellow enzyme of Saccharomyces cerevisiae. J. Biol. Chem. 270, 1983-1991.
21. Pringle, J.R., Preston, R.A., Adams, A.E., Stearns, T., Drubin, D.G., Haarer, B.K., and Jones, E.W. (1989). Fluorescence microscopy methods for yeast. Methods Cell Biol. 31, 357-435.
22. Rose, M.D., Winston, F., and Hieter, P. (1989). Methods in Yeast Genetics, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
23. Schopfer, L.M., and Massey, V. (1991). Old yellow enzyme. In: A Study of Enzymes, vol. 2, ed. S.A. Kuby, Boston, MA: CRC Press, 247-269.
24. Schutt, C.E., Myslik, J.C., Rozycki, M.D., Goonesekere, N.C.W., and Lindberg, U. (1993). The structure of crystalline profilin-β-actin. Nature 365, 810-816.
25. Shartava, A., Korn, W., Shah, A.K., and Goodman, S.R. (1997). Irreversibly sickled cell β-actin: defective filament formation. Am. J. Hemat. 55, 97-103.
26. Shartava, A., Monteiro, C.A., Bencsath, F.A., Schneider, K., Chait, B.T., Gussio, R., Casoria-Scott, L.A., Shah, A.K., Heuerman, C.A., and Goodman, S.R. (1995). A posttranslational modification of β-actin contributes to the slow dissociation of the spectrin-protein 4.1-actin complex of irreversibly sickled cells. J. Cell Biol. 128, 805-818.
27. Stott, K., Saito, K., Thiele, D.J., and Massey, V. (1993). Old yellow enzyme. The discovery of multiple isozymes and a family of related proteins. J. Biol. Chem. 268, 6097-6106.
28. Thor, H., Smith, M.T., Hartzell, P., Bellomo, G., Jewell, S.A., and Orrenius, S. (1982). The metabolism of menadione (2-methyl-1,4-naphthoquinone) by isolated hepatocyes. J. Biol. Chem. 257, 12419-12425.
29. Warburg, O., and Christian, W. (1933). Biochem. Z. 266, 377-411.
30. Wertman, K.F., Drubin, D.G., and Botstein, D. (1992). Systematic mutational analysis of the yeast ACT1 gene. Genetics 132, 337-350.
31. Wetterstroem, N., Brewer, G.J., Warth, J.A., Mitchinson, A., and Near, K. (1984). Relationship of glutathione levels and Heinz body formation to irreversibly sickled cells in sickle cell anemia. J. Lab. Clin. Med. 103, 589-596.
32. Wheeler, G.L., and Grant, C.M. (2004). Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae. Physiol. Plant 120, 12-20.