Reinvestigation of the proteolytic activity of neocarzinostatin

Journal of Bacteriology

Volumn 182, Issue 7, 2000, Pages 1812-1818

  Heyd, Bernadette ^a   Lerat, Guilhem ^a   Adjadj, Elisabeth ^b   Minard, Philippe ^a   Desmadril, Michel ^a  

^a UNIVERSITÉ PARIS SACLAY   (France)

^b INSTITUT CURIE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; HISTONE; PROTEINASE; RECOMBINANT PROTEIN; ZINOSTATIN;

ARTICLE; CHROMATOGRAPHY; ENZYME ACTIVITY; ENZYME SPECIFICITY; GENE EXPRESSION SYSTEM; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STABILITY; RECOMBINANT GENE; STREPTOMYCES; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANIMALS; APOPROTEINS; ARTIFACTS; CATALYSIS; CATTLE; CIRCULAR DICHROISM; DRUG CONTAMINATION; ENDOPEPTIDASES; ENZYME STABILITY; ESCHERICHIA COLI; FALSE POSITIVE REACTIONS; HEAT; HISTONES; MAGNETIC RESONANCE SPECTROSCOPY; PROTEASE INHIBITORS; RECOMBINANT PROTEINS; REPRODUCIBILITY OF RESULTS; SENSITIVITY AND SPECIFICITY; STREPTOMYCES; SUBSTRATE SPECIFICITY; ZINOSTATIN;

ACTINOBACTERIA (CLASS); ESCHERICHIA COLI; STREPTOMYCES; UNCULTURED ACTINOMYCETE;

EID: 0034101939     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.7.1812-1818.2000     Document Type: Article

References (24)

1. Adjadj, E., J. Mispelter, E. Quiniou, J.-L. Dimicoli, V. Favaudon, and J.-M. Lhoste. 1990. Proton NMR studies of apo-neocarzinostatin from Streptomyces carzinostaticus. Sequence-specific assignment and secondary structure. Eur. J. Biochem. 190:263-271.
2. Adjadj, E., E. Quiniou, J. Mispelter, V. Favaudon, and J. M. Lhoste. 1991. Three-dimensional solution structure of apo-neocarzinostatin from Streptomyces carzinostaticus determined by NMR spectroscopy. Eur. J. Biochem. 203:505-511.
3. Beerman, T. A., G. Mueller, and H. Grimmond. 1982. Effects of neocarzinostatin on chromatin in HeLa S3 nuclei. Mol. Pharmacol. 23:493-499.
4. Bradbury, E. M. 1983. Conformations and flexibilities of histones and high mobility group (HMG) proteins in chromatin structure and function. Ciba Found. Symp. 93:246-270.
5. de Nooij, E. H., and H. G. K. Westenbrink. 1962. Isolation of a homogenous Lys-rich histone from calf thymus. Biochim. Biophys. Acta 62:608-609.
6. Favaudon, V. 1983. Gamma-radiolysis study of the reductive activation of neocarzinostatin by the carboxyl radical. Biochimie 65:593-607.
7. Fisher, W. R., H. Taniuchi, and C. B. Anfinsen. 1973. On the role of heme in the formation of the structure of cytochrome c. J. Biol. Chem. 248:3188-3193.
8. Goldberg, I. H., T. Hatayama, L. S. Kappen, M. A. Napier, and L. F. Povirk. 1981. Molecular actions and targets for cancer chemiotherapeutic agents, vol. 1, p. 163-191. Academic Press, New York, N.Y.
9. Hatayama, T., and M. Yukioka. 1982. Action of neocarzinostatin on cell nuclei: release of specific chromatin. Biochem. Biophy. Res. Commun. 104: 889-896.
10. Kappen, L. S., T. E. Ellenberger, and I. H. Goldberg. 1987. Mechanism and base specificity of DNA breakage in intact cells by neocarzinostatin. Biochemistry 26:384-390.
11. Kappen, L. S., M. A. Napier, and I. H. Goldberg. 1980. Roles of chromophore and apoprotein in neocarzinostatin action. Proc. Natl. Acad. Sci. USA 7:1970-1974.
12. Kikushi, M., M. Shoji, and N. Ishida. 1974. Pre-neocarzinostatin, a specific antagonist of neocarzinostatin. J. Antibiot. 27:766-774.
13. Kim, K.-H., B.-M. Kwon, A. G. Myers, and D. R. Rees. 1993. Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex. Science 262:1042-1046.
14. Lazarus, H., V. Raso, and T. S. A. Samy. 1977. In vitro inhibition of human leukemic cells CCRF-CEM) by agarose-immobilized neocarzinostatin. Cancer Res. 37:3731-3138.
15. Mohanty, S., L. C. Sieker, and G. P. Drobny. 1994. Sequential 1H NMR assignment of the complex of aponeocarzinostatin with ethidium bromide and investigation of protein-drug interactions in the chromophore binding site. Biochemistry 33:10579-10590.
16. Perczel, A., and M. Hollosi. 1996. Turns, p. 285-381. In G. Fasman (ed.), Circular dichroism and the conformational analysis of biomolecules. Plenum Press, New York, N.Y.
17. Privalov, P. L., E. I. Tiktopulo, S. Venyaminov, Y. V. Griko, G. I. Makhatadze, and N. N. Khechinashvili. 1989. Heat capacity and conformation of proteins in the denatured state. J. Mol. Biol. 205:737-750.
18. Sakata, N., K. S. Tsuchiya, Y. Moriya, H. Havashi, M. Hori, T. Otani, M. Nagai, and T. Aoyagi. 1991. Aminopeptidase activity of an antitumor antibiotic, C-1027. J. Antibiot. 45:113-117.
19. Teplyakov, A., G. Obmolova, K. Wilson, and K. Kuromizu. 1993. Crystal structure of apo-neocarzinostatin at 0.15-nm resolution. Eur. J. Biochem. 213:737-741.
20. Tien, K. M., and T. S. A. Samy. 1978. Effects of neocarzinostatin on mammalian nuclei: release of nucleosomes. Biochim. Biophys. Acta 518:186-190.
21. Zaheer, A., S. Zaheer, and R. Montgomery. 1985. Peptidase activity of macromomycin apoprotein. J. Biol. Chem. 260:11787-11792.
22. Zein, N., A. M. Casazza, T. W. Doyle, J. E. Leet, D. R. Schroeder, W. Solomon, and S. G. Nadler. 1993. Selective proteolytic activity of the antitumor agent kedarcidin. Proc. Natl. Acad. Sci. USA 90:8009-8012.
23. Zein, N., W. Solomon, K. L. Colson, and D. R. Schroeder. 1995. Maduropeptin: an antitumor chromoprotein with selective protease activity and DNA cleaving properties. Biochemistry 34:11591-11597.
24. Zein, N., P. Reiss, M. Bernatowicz, and M. Bolgar. 1995. The proteolytic specificity of the natural enediyne-containing chromoproteins is unique to each chromoprotein. Chem. Biol. 7:451-455.