Magnesium chelatase subunit D from pea: Characterization of the cDNA, heterologous expression of an enzymatically active protein and immunoassay of the native protein

Plant Molecular Biology

Volumn 41, Issue 6, 1999, Pages 721-731

  Luo, Meizhong ^a,d   Weinstein, Jon D ^b,d   Walker, Caroline J ^c,d  

^a CLEMSON UNIVERSITY   (United States)

^b Portland Press Ltd   (United Kingdom)

^c Brewing Research International   (United Kingdom)

^d CLEMSON UNIVERSITY   (United States)

Author keywords

Chaperonin; Chlorophyll synthesis; Co expression; Mg chelatase; Pea

Indexed keywords

AMINO TERMINAL SEQUENCE; ANTIGEN PRODUCTION; CARBOXY TERMINAL SEQUENCE; CHAPERONIN; COMPLEMENTARY DNA; ENZYME INHIBITION; ENZYME SUBUNIT D; EXPRESSION VECTOR; IMMUNOPRECIPITATION; MAGNESIUM CHELATASE; MAGNESIUM CHLORIDE; PEA; PROTEIN EXPRESSION; PROTEIN INDUCTION; SEQUENCE HOMOLOGY; SOLUBILIZATION;

AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL; BLOTTING, WESTERN; CHAPERONINS; CHEMICAL FRACTIONATION; CHLOROPLASTS; DNA, COMPLEMENTARY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, ENZYMOLOGIC; IMMUNOASSAY; LYASES; MOLECULAR SEQUENCE DATA; PEAS; PRECIPITIN TESTS; RECOMBINANT FUSION PROTEINS; SEQUENCE ANALYSIS, DNA;

EMBRYOPHYTA; ESCHERICHIA COLI; PISUM SATIVUM; PROKARYOTA;

EID: 0033389489     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006335317876     Document Type: Article

References (42)

1. Alberti, M., Burke, D.H. and Hearst, J.E. 1995. Structure and sequence of the photosynthesis gene cluster. In: R.E. Blankenship, M.T. Madigan and C.E. Bauer (Eds.), Anoxygenic Photosynthetic Bacteria, Kluwer Academic Publishers, Dordrecht, Netherlands, pp. 1083-1106.
2. Armstrong, D.J. and Roman, A. 1993. The anomolous electrophoretic behavior of the human papillomavirus type 16 E7 protein is due to the high content of acidic amino acid residues. Biochem. Biophys. Res. Commun. 192: 1380-1387.
3. Bartels, D., Schneider, K., Terstappen, G., Piatkowski, D. and Salamini, F. 1990. Molecular cloning of abscisic acid modulated genes which are induced during desiccation of the resurrection plant, Craterostigma plantagineum. Planta 181: 27-34.
4. Beale, S.I. and Weinstein, J.D. 1990. Tetrapyrrole metabolism in photosynthetic organisms. In: H.A. Dailey (Ed.), Biosynthesis of Heme and Chlorophylls, McGraw-Hill, New York, pp. 287-391.
5. Bollivar, D.W., Suzuki, J.Y., Beatty, J.T., Dobrowolski, J.M. and Bauer, C.E. 1994. Directed mutational analysis of bacteriochlorophyll a biosynthesis in Rhodobacter capsulatus. J. Mol. Biol. 237: 622-640.
6. Caspers, P., Steiger, M. and Burn, P. 1994. Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in Escherichia coli. Cell Mol. Biol. 40: 635-644.
7. Ferreira, G.C., Franco, R., Lloyd, S.G., Moura, J.J. and Huynh, B.H. 1995. Structure and function of ferrochelatase. J. Bioenerg. Biomembr. 27: 221-229.
8. Fling, S.P. and Gregerson, D.S. 1986. Peptide and protein molecular mass determination by electrophoresis using a high molarity Tris buffer system without urea. Anal. Biochem. 155: 83-88.
9. Fuesler, T.P., Wong, Y.-S. and Castelfranco, P.A. 1984. Localization of the Mg-chelatase and Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase activities within isolated, developing cucumber chloroplasts. Plant Physiol. 75: 662-664.
10. Gavel, Y. and von Heijne, G. 1990. A conserved cleavage-site motif in chloroplast transit peptides. FEBS Lett. 261: 455-458.
11. Gibson, L.C.D., Willows, R.D., Kannangara, C.G., von Wettstein, D. and Hunter, C.N. 1995. Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: reconstitution of activity by combining the products of the bchH, -I and -D genes expressed in Escherichia coli. Proc. Natl. Acad. Sci. USA 92: 1941-1944.
12. Gibson, L.C.D., Marrison, J.L., Leech, R.M., Jensen, P.E., Bassham, D.C., Gibson, M. and Hunter, C.N. 1996. A putative Mg chelatase subunit from Arabidopsis thaliana cv. C24. Sequence and transcript analysis of the gene, import of the protein into chloroplasts, and in situ localization of the transcript and protein. Plant Physiol. 111: 61-71.
13. Graceffa, P., Janesco, A. and Mabuchi, K. 1992. Modification of acidic residues normalizes sodium dodecyl sulfate-polyacrylamide gel electrophoresis of caldesmon and other proteins that migrate anomolously. Arch. Biochem. Biophys. 297: 46-51.
14. Guise, A.D., West, S.M. and Chaudhuri, J.B. 1996. Protein folding in vivo and renaturation of recombinant proteins from inclusion bodies. Mol. Biotechnol. 6: 53-64.
15. Guo, R., Luo, M. and Weinstein, J.D. 1998. Mg-chelatase from developing pea leaves: characterization of a soluble extract from chloroplasts and resolution into three required protein fractions. Plant Physiol. 116: 605-615.
16. Hudson, A., Carpenter, R., Doyle, S. and Coen, E.S. 1993. Olive: a key gene required for chlorophyll biosynthesis in Antirrhinum majus. EMBO J. 12: 3711-3719.
17. Jensen, P.E., Gibson, L.E., Henningsen, K.W. and Hunter, C.N. 1996a. Expression of the chlI, chlD and chlII genes from the cyanobacterium Synechocystis PCC6803 in Escherichia coli and demonstration that the three cognate proteins are required for magnesium-protoporphyrin chelatase activity. J. Biol. Chem. 271: 16662-16667.
18. Jensen, P.E., Willows, R.D., Petersen, B.L., Vothknecht, U.C., Stummann, B.M., Kannangara, C.G., von Wettstein, D. and Henningsen, K.W. 1996b. Structural genes for Mg-chelatase subunits in barley: Xantha-f, -g and -h. Mol. Gen. Genet. 250: 383-394.
19. John, M.E. and Keller, G. 1995. Characterization of mRNA for a proline-rich protein of cotton fiber. Plant Physiol. 108: 669-676.
20. Joyard, J., Block, M., Pineau, B., Albrieux, C. and Douce, R. 1990. Envelope membranes from mature spinach chloroplasts contain a NADPH:protochlorophyllide reductase on the cytosolic side of the outer membrane. J. Biol. Chem. 265: 21820-21827.
21. Kannangara, C.G., Vothknecht, U.C., Hansson, M. and von Wettstein, D. 1997. Mg-chelatase: association with ribosomes and mutant complementation studies identify barley subunit Xantha-G as a functional counterpart of Rhodobacter subunit BchD. Mol. Gen. Genet 254: 85-92.
22. Keegstra, K. and Yousif, A.E. 1986. Isolation and characterization of chloroplast envelope membranes. Meth. Enzymol. 118: 316-325.
23. Koncz, C., Mayerhofer, R., Koncz-Kalman, Z., Nawrath, C., Reiss, B., Redei, G.P. and Schell, J. 1990. Isolation of a gene encoding a novel chloroplast protein by T-DNA tagging in Arabidopsis thaliana. EMBO J. 9: 1337-1346.
24. Koonin, E.V. 1993. A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication. Nucl. Acids Res. 21: 2541-2547.
25. Koonin, E.V. 1997. Evidence for a family of archael ATPases. Science 275: 1489-1490.
26. Kruse, E., Mock, H.-P. and Grimm, B. 1997. Isolation and characterisation of tobacco (Nicotania tabacum) cDNA clones encoding proteins involved in magnesium chelation into protoporphyrin IX. Plant Mol. Biol. 35: 1053-1056.
27. Luo, M. and Weinstein, J.D. 1997. Cloning and sequencing of a cDNA encoding the putative Mg-chelatase subunit D (accession no. AF014399) from pea (Pisum sativum L. cv. Spring) (PGR97-139). Plant Physiol. 115: 315.
28. Luo, M., Orsi, R., Patrucco, E., Pancaldi, S. and Cella, R. 1997. Multiple transcription start sites of the carrot dihydrofolate reductase-thymidylate synthase gene, and subcellular localization of the bifunctional protein. Plant Mol. Biol. 33: 709-722.
29. Martin, J. and Hartl, F.U. 1997. Chaperone-assisted folding. Curr. Opin. Struct. Biol. 7: 41-52.
30. Nakayama, M., Masuda, T., Sato, N., Yamagata, H., Bowler, C., Ohta, H., Shioi, Y. and Takamiya, K. 1995. Cloning, subcellular localization and expression of ChlI, a subunit of magnesium-chelatase in soybean. Biochem. Biophys. Res. Commun. 215: 422-428.
31. 2+ concentration-dependent ChlH protein within the chloroplast. Plant Cell Physiol. 39: 275-284.
32. Papenbrock, J., Gräfe, S., Kruse, E., Hänel, F. and Grimm, B. 1997. Mg-chelatase of tobacco: identification of a ChlD cDNA sequence encoding a third subunit, analysis of the interaction of the three subunits with the yeast two-hybrid system, and reconstitution of the enzyme activity by co-expression of recombinant CHL D, CHL H and CHL I. Plant J. 12: 981-990.
33. Pardo, A.D., Chereskin, B.M., Castelfranco, P.A., Franceschi, V.R. and Wezelman, B.E. 1980. ATP requirement for Mg chelatase in developing chloroplasts. Plant Physiol. 65: 956-960.
34. Petersen, B.L., Møller, M.G., Stummann, B.M. and Henningsen, K.W. 1996. Clustering of the genes with function in the biosynthesis of bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium vibrioforme. Hereditas 125: 93-96.
35. Sambrook, J., Fritsch, E.F. and Maniatis, T. 1989. Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Press, Cold Spring Harbor, NY.
36. von Heijne, G., Steppuhn, J. and Herrmann, R.G. 1989. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180: 535-545.
37. Walker, C.J. and Weinstein, J.D. 1991. In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelatase: resolution of the activity into soluble and membrane-bound fractions. Proc. Natl. Acad. Sci. USA 88: 5789-5793.
38. Walker, C.J. and Weinstein, J.D. 1994. The magnesium insertion step of chlorophyll biosynthesis is a two-stage reaction. Biochem. J. 299: 277-284.
39. Walker, C.J. and Weinstein, J.D. 1995. Re-examination of the localization of Mg-chelatase within the chloroplast. Physiol. Plant. 94: 419-424.
40. Walker, C.J. and Willows, R.D. 1997. Mechanism and regulation of Mg-chelatase. Biochem. J. 327: 321-333.
41. Walker, C.J., Hupp, L.R. and Weinstein, J.D. 1992. Activation and stabilization of Mg-chelatase activity by ATP as revealed by a novel in vitro continuous assay. Plant Physiol. Biochem. 30: 263-269.
42. Willows, R.D., Gibson, L.C.D., Kannangara, C.G., Hunter, C.N. and von Wettstein, D. 1996. Three separate proteins constitute the magnesium chelatase of Rhodobacter sphaeroides. Eur. J. Biochem. 235: 438-443.