Determination of the regulatory disulfide bonds of NADP-dependent malate dehydrogenase from Pisum sativum by site-directed mutagenesis

Biological Chemistry

Volumn 378, Issue 9, 1997, Pages 983-988

  Rießland, Robin ^a   Jaenicke, Rainer ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Chloroplast MDH; Disulfide bonds; Malate dehydrogenase; Pisum sativum; Redox modulation

Indexed keywords

CYSTEINE; DITHIOTHREITOL; GUANIDINE; MALATE DEHYDROGENASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; DISULFIDE BOND; ELECTROPHORETIC MOBILITY; ENZYME ACTIVATION; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBUNIT; GENETIC TRANSFORMATION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SIMULATION; SITE DIRECTED MUTAGENESIS;

PISUM SATIVUM;

EID: 0343990074     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.9.983     Document Type: Article

References (26)

1. Auerbach, G. (1994). Aufklärung der 3D Struktur der LDH aus dem hyperthermophilen Bakterium Thermotoga maritima und der MDH aus Pisum sativum mittels "Homology Modelling". Thesis, Regensburg University.
2. Bell, J.N., Ryder, T.B., Wingate, U.P.M., Baitey, J.A., and Lamp, C.J. (1986). Differential accumulation of plant defense gene transcripts in a compatible plant-pathogen interaction. Mol. Cell Biol. 6, 1615-1623.
3. Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248-254.
4. Buchanan, B.B. (1980). Role of light in the regulation of chloroplast enzymes. Annu. Rev. Plant Physiol. 31, 341-357.
5. Geisselsoder, J., Witney, F., and Yuckenberg, P. (1987). Efficient site-directed in vitro mutagenesis. Biotechniques 5, 786-791.
6. Gill, S.C., and von Hippel, P.H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
7. Hanes, C.S. (1932). Studies on plant amylases. I. The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem. J. 26, 1406-1421.
8. Hatch, M.D., and Agostino, A. (1992). Bilevel disulfide group reduction in the activation of C4 leaf NADP-MDH. Plant Physiol. 100, 360-366.
9. Hill, E., Tsernoglou, D., Webb, L., and Nanaszak, J. (1972). Polypeptide conformation of cytoplasmic MDH from the electron density map at 3.0 Å resolution. J. Mol. Biol. 72, 577-591.
10. Innis, M.A., Gelsand, D.H., Sninsky, J.J., and White, T.J. (1990). PCR-Protocols: A Guide to Methods and Applications. (San Diego, USA: Academic Press).
11. Issakidis, E., Miginiak-Maslow, M., Decottignies, P., Jacquot, J.-P., Crétin, C., and Gadal, P. (1992). Site-directed mutagenesis reveals the involvement of an additional thioredoxin-dependent regulatory site in the activation of recombinant Sorghum leaf NADPH-MDH. J. Biol. Chem. 267, 21577-21583.
12. Issakidis, E., Decottignies, P., and Miginiak-Maslow, M. (1993). A thioredoxin-independent fully active NADP-MDH obtained by site-directed mutagenesis. FEBS Lett. 321, 55-58.
13. Issakidis, E., Saarinen, M., Decottignies, P., Jacquot, J.-P., Crétin, C., Gadal, P., and Miginiak-Maslow, M.P. (1994). Identification and characterization of the second regulatory disulfide bridge of recombinant Sorghum leaf NADP-MDH. J. Biol. Chem. 269, 3511-3517.
14. Jacquot, J.-P., Buchanan, B.B., Martin, F., and Vidal, J. (1981). Enzyme regulation in C4 photosynthesis. Plant Physiol. 68, 300-304.
15. Jacquot, J.-P., Gadal, P., Nishizawa, A.N., Yee, B.C., Crawford, N.A., and Buchanan, B.B. (1984). Enzyme regulation in C4 photosynthesis: Mechanism of activation of NADP-MDH by reduced thioredoxin. Arch. Biochem. Biophys. 228, 170-178.
16. Kunkel, T.A., Roberts, J.D., and Zakour, R.A. (1987). Rapid and efficient site-directed mutagenesis without phenotypic selection. Meth. Enzymol. 154, 367-382.
17. Miginiak-Maslow, M., Decottignies, P., Jacquot, J.-P., and Gadal, P. (1990). Regulation of corn leaf NADP-MDH light activation by photosynthetic electron flow. Biochim. Biophys. Acta 1017, 273-279.
18. Ocheretina, O., and Scheibe, R. (1994). Cysteines of chloroplast NADP-MDH from mixed disulfides. FEBS Lett. 355, 254-258.
19. Reng, W. (1993). Klonierung, Expression und Charakterisierung der NADP-abhängigen MDH aus Chloroplasten von Pisum sativum. Ph.D. Thesis, Regensburg University.
20. Reng, W., Rießland, R., Scheibe, R., and Jaenicke, R. (1993). Cloning, site-directed specific mutagenesis, expression and characterization of full-length chloroplast NADP-MDH from Pisum sativum. Eur. J. Biochem. 217, 189-197.
21. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular cloning: A Laboratory Manual (2nd Ed.) (Cold Spring Harbor Laboratory Press, N.Y., USA: Cold Spring Harbor Laboratory Press).
22. Sanger, F., Micklen, S., and Coulson, A.R. (1977). DNA sequencing with chain termination inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
23. Scheibe, R. (1984). Quantitation of the thiol groups involved in the eductive activation of NADP-MDH. Biochim. Biophys. Acta 788, 241-247.
24. Scheibe, R., Rudolph, R., Reng, W., and Jaenicke, R. (1990). Structural and catalytic properties of oxidized and reduced chloroplast NADP-MDH upon denaturation and renaturation. Eur. J. Biochem. 189, 581-587.
25. v fragments in E. coli: Improved vectors and a generally applicable purification technique. Bio/Technology 9, 273-278.
26. Vieira, J., and Messing, J. (1987). Production of single-stranded plasmid DNA. Meth. Enzymol. 153, 3-11.