Chalcogen-Analogs of Arnino Acids Their Use in X-Ray Crystallographic and Folding Studies of Peptides and Proteins

Biological Chemistry

Volumn 378, Issue 3-4, 1997, Pages 211-218

  Besse, Dörthe ^a   Budisa, Nediljko ^a   Karnbrock, Wilhelm ^a   Minks, Caroline ^a   Musiol, Hans Jürgen ^a   Pegoraro, Stefano ^a   Siedler, Frank ^a   Weyher, Elisabeth ^a   Moroder, Luis ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; AMINO ACID TRANSFER RNA LIGASE;

ESCHERICHIA COLI; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN VARIANT; REVIEW; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS; CRYSTALLOGRAPHY, X-RAY; PEPTIDE BIOSYNTHESIS; PEPTIDES; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEINS; SELENOPROTEINS;

ESCHERICHIA COLI;

EID: 0030950573     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.3-4.211     Document Type: Article

References (39)

1. Besse, D., Pegoraro, S., Dierks, T., Kessler, H., and Moroder, L. (1996). Controlled disulfide bridging in multiple cystine-con-taining peptides with built-in selenocysteines. In: Proceedings 6th Akabori Conference, Shimonishi, Y., ed. (Osaka, Japan: Protein Research Foundation), pp. 24-29.
2. Besse, D., Pegoraro, S., Dierks, T., Kessler, H., and Moroder, L., (1997). Selenocysteine as usefull device for selective disulfide pairings in multiple cysteine peptides. In: Peptides 1996, R. Ramage, ed. (Kingswinford, England: Mayflower Scientific, Ltd.), in press.
3. Boles, J.O., Lewinski, K., Kunke, M., Odom, J.D., Dunlap, B.R., Lebioda, L., and Hatada, M. (1994). Bio-incorporation of tellu-romethionine into burried residues of dihydrofolate-reductase. Nature Structural Biology 7, 283-284.
4. Bontems, R., Roumestand, C., Gilquin, B., Ménez, A., and Torna, R (1991). Refined structure of charybdotoxin-common motifs in scorpion toxins and insect defensins. Science 254, 1521-1523.
5. Budisa, N., Steipe, B., Demange, R., Eckerskorn, C., Kellermann, S., and Huber, R. (1995). High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur. J. Biochem. 230, 788-796.
6. Chau, M.-H., and Nelson, J.W. (1992). Cooperative disulfide bond formation in apamin. Biochemistry 37, 4445-4450.
7. Chenault, H.K., Dahmer, J., and Whitesides, G.M. (1989). Kinetic resolution of unnatural and rarely occurring amino acids: enan-tioselective hydrolysis of N-acyl amino acids catalyzed by acylase I. J. Am. Chem. Soc. 777, 6354-6364.
8. Chibata, I., Tosa, T., Sato, T., and Mori, T. (1976). Production of L-amino acids by aminoacylase adsorbed on DEAE-Sephadex. Meth. Enzymol. 44, 746-759.
9. Cornish, V. W., Mendel, D., and Schultz, R. G. (1995). Untersuchungen von Struktur und Funktion von Proteinen mit einem erweiterten genetischen Code. Angew. Chem. 107, 677-690.
10. Cowie, D.B., and Cohen, G.N. (1957). Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur. Biochim. Biophys. Acta 26, 252-261.
11. Deshaies, R.J., Koch, B.D., Werner-Washburne, M., Craig, E.A., and Shekman, R. (1988). A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332, 800-805.
12. Detty, M.R., Friedman, A.F., and Oseroff, A.R. (1994). A mechanism for the oxidation of glutathione to glutathione disulfide with organotellurium(III) and organoselenium(IV) compounds. A stepwise process with implications for photodynamic therapy and other oxidative chemotherapy. J. Org. Chem. 59, 8245-8250.
13. Engman, L., Stern, D., Pelcman, M., and Andersson, C.M. (1994). Thiol peroxidase activity of diorganyl tellurides. J. Org. Chem. 59, 1973-1979.
14. Günther, W.H.H. (1967). Methods in selenium chemistry. III. The reduction of diselenides with dithiothreitol. J. Org. Chem. 32, 3931-3933.
15. Hendrickson, W.A. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
16. Hendrickson, W.A., Horton, J., and LeMaster, D. (1990). Seleno-methionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD)-a vehicle for direct determination of 3-dimensional structure. EMBO J. 9, 1665-1672.
17. Huyghues-Despointes, B.M.P., and Nelson, J.W. (1992). Stabilities of disulfide bond intermediates in the folding of apamin. Biochemistry 37.1476-1483.
18. Karnbrock, W., Weyher, E., Budisa, N., Huber, R., and Moroder, L. (1996). A new efficient synthesis of acetyltelluro-and acetylse-lenomethionine and their use in the biosynthesis of heavy-atom protein analogs. J. Am. Chem. Soc. 7 78, 913-914.
19. Knapp, E.F. (1979). Telluroamino acids-synthesis of telluromethionine. J. Org. Chem. 44, 1007-1009.
20. Koch, T., and Buchardt, O. (1993). Synthesis of L-(+)-selenomethionine. Synthesis, 1065-1067.
21. Koide, T., Itoh, H., Otaka, A., Yasui, H., Kuroda, M., Esaki, N., Soda, K., and Fujii, N. (1993). Synthetic study on selenocys-tine-containing peptides. Chem. Pharm. Bull. 41, 502-506.
22. Koide, T., Otaka, A., and Fujii, N. (1993). Investigation of the dimethylsulfoxide trifluoroacetic-acid oxidation system for the synthesis of cystine-containing peptides. Chem. Pharm. Bull. 41, 1030-1034.
23. Koshi, T., Suzuki, C., Arai, K., Mizoguchi, T., Torii, T., Hirata, M., Ohkuchi, M., and Okabe, T. (1991). Syntheses and biological-activities of endothelin-1 analogs. Chem. Pharm. Bull. Japan 39, 3061-3063.
24. Kumagaye, S.-I., Kurode, H., Nakajima, K., Watanabe, T.X., Kimura, T., Masaki, T., and Sakakibara, S. (1988). Synthesis and disulfide structure determination of porcine endothelin-an endothelium-derived vasoconstricting peptide. Int. J. Peptide Protein Res. 32, 519-526.
25. Mills, R.G., Ralston, G.B., and King, G.F. (1994). The solution structure of sarafotoxin-C-implications for ligand recognition by endothelin. J. Biol. Chem. 269, 23413-23419.
26. Moroder, L., Besse, D., Musiol, H.J., Rudolph-Böhner, S., and Siedler, F (1996). Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies. Biopolymers (Peptide Sci.) 40, 207-234.
27. Moroder, L., Battistuta, R., Besse, D., OttI, J.; Pegoraro, S., and Siedler, F. (1997). Synthesis of multiple-cystine-peptides. In: Peptides 1996, R. Ramage, ed. (Kingswinford, England: Mayflower Scientific, Ltd.), in press.
28. Müller, S., Senn, H., Gsell, B., Vetter, W., Baron. C., and Bock, A. (1994). The formation of diselenide bridges in proteins by incorporation of selenocysteine residues: biosynthesis and characterization of (Se)2-thioredoxin. Biochemistry 33.3404-3412.
29. Munier, R., and Cohen, G.N. (1959). Incorporation of structural analogs of amino acids into bacterial proteins during their synthesis in vivo. Biochim. Biophys. Acta 37, 378-390.
30. Noren, C.J., Anthony-Cahill, S.J., Griffith, M.C., and Schultz, P. G. (1989). General method for site-specific incorporation of unnatural amino-acids into proteins. Science 244, 182-183.
31. Perutz, M.F., Rossmann, M.G., Cullis, A.F., Muirhead, H., Will, G., and North, A.C.T. (1960). Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5Ä resolution, obtained by X-ray analysis. Nature 785.416-422.
32. Reinemer, R., Prade, L. Hof, R., Neuefeind, T., Huber, R., ZettI, R., Palme, K., Schell, J., Koelln, I., Bartunik, H.D., and Bieseler, B. (1996). Three-dimenslonale structure of glutathione S-trans-ferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. J. Mol. Biol. 255, 289-309.
33. Siedler, R., Rudolph-Bohner, S., Doi, M., Musiol, H.-J., and Moroder, L. (1993). Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases. Biochemistry 32, 7488-7495.
34. Silks, L.A., Boles, J.O., Modi. B.R., Dunlap, R.B., and Odom, J.D. (1990). An efficient synthesis of racemic and optically-active telluromethionine. Synth. Commun. 20, 1555-1562.
35. Singh, R., and Whitesides, G.M. (1991). Selenols catalyze the interchange reactions of dithiols and disulfides in water J. Org. Chem. 56, 6931-6933.
36. Stadtman, T.C. (1996). Selenocystelne. Annu. Rev. Biochem. 65, 83-100.
37. Szajewski, R.R., and Whitesides, G.M. (1980). Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione. J. Am. Chem. Soc. 102, 2011-2026.
38. Tam, J.R., Liu, W., Zhang, J.-W., Galantine, M., and de Castiglione, R. (1991). D-Amino acid and alanine scans of endothelin: an approach to study refolding intermediates. In: Peptides 1990, E. Giralt and D. Andreu, eds. (Leiden, Netherlands: ESCOM), pp.160-163.
39. Xu, X., and Nelson, J.W. (1994). One-disulfide intermediates of apamin exhibit native-like structure. Biochemistry 33, 5253-5261.