Functional expression and enzymatic properties of two Sitophilus zeamais cysteine proteinases showing different autolytic processing profiles in vitro

Journal of Biochemistry

Volumn 123, Issue 4, 1998, Pages 693-700

  Matsumoto, Ichiro ^a   Abe, Keiko ^a   Arai, Soichi ^a   Emori, Yasufumi ^b  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

Cysteine proteinase; Recombinant enzyme; Sitophilus zeamais

Indexed keywords

CATHEPSIN L; CYSTEINE PROTEINASE; HEMOGLOBIN;

ARTICLE; AUTOLYSIS; CARBOXY TERMINAL SEQUENCE; CLONING VECTOR; COLUMN CHROMATOGRAPHY; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; GENE FUSION; HYDROLYSIS; INSECT; MOLECULAR CLONING; NONHUMAN; PH; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN PURIFICATION;

ARACHNIDA; ESCHERICHIA COLI; HEXAPODA; INSECTA; MAMMALIA; SITOPHILUS ZEAMAIS;

EID: 0031958707     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021993     Document Type: Article

References (41)

1. Berti, P.J. and Storer, A.C. (1995) Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246, 273-283
2. Kominami, E., Ueno, T., Muno, D., and Katunuma, N. (1991) The selective role of cathepsins B and D in the lysosomal degradation of endogenous and exogenous proteins. FEBS Lett. 287, 189-192
3. Kakegawa, H., Nikawa, T., Tagami, K., Kamioka, H., Sumitani, K., Kawata, T., Drobnic-Kosorok, M., Lenarcic, B., Turk, V., and Katunuma, N. (1993) Participation of cathepsin L on bone resorption. FEBS Lett. 321, 247-250
4. Homma, K., Kurata, S., and Natori, S. (1994) Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly), and its involvment in the differentiation of imaginal discs. J. Biol. Chem. 269, 15258-15264
5. Yamamoto, Y., Takimoto, K., Izumi, S., Toriyama-Sakurai, M., Kageyama, T., and Takahashi, S.Y. (1994) Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori. J. Biochem. 116, 1330-1335
6. Matsumoto, I., Watanabe, H., Abe, K., Arai, S and Emori, Y. (1995) A putative digestive cysteine proteinase from Drosophila melanogaster is predominantly expressed in the embryonic and larval midgut. Eur. J. Biochem. 227, 582-587
7. Matsumoto, I., Emori, Y., Abe, K., and Arai, S. (1997) Characterization of a gene family encoding cysteine proteinases of Sitophilus zeamais (maize weevil), and analysis of the protein distribution in various tissues including alimentary tracts and germ cells. J. Biochem. 121, 464-476
8. Takahashi, S.Y., Zhao, X., Kageyama, T., and Yamamoto, Y. (1992) Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: tissue distribution, developmental changes and the site of synthesis for the enzyme. Insect Biochem. Mol. Biol. 22, 369-377
9. Yamamoto, Y. and Takahashi, S.Y. (1993) Cysteine proteinase from Bombyx eggs: role in programmed degradation of yolk proteins during embryogenesis. Comp. Biochem. Physiol. 106B, 35-45
10. Takahashi, S.Y., Yamamoto, Y., Shionoya, Y., and Kageyama, T. (1993) Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: identification of a latent enzyme and characterization of activation proteolytic processing in vivo and in vitro. J. Biochem. 114, 267-272
11. Gal, S. and Gottesman, M.M. (1986) The major excreted protein of transformed fibroblasts is an activable acid-protease. J. Biol. Chem. 261, 1760-1765
12. Mason, R.W., Gal, S., and Gottesman, M.M. (1987) The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L. Biochem. J. 248, 449-454
13. Mort, J.S., Tam, A., Steiner, D.F., and Chan, S.J. (1988) Expression of rat and mouse cathepsin B precursors in Escherichia coli. Biol. Chem. Hoppe-Seyler 369, 163-167
14. Smith, S.M. and Gottesman, M.M. (1989) Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli. J. Biol. Chem. 264, 20487-20495
15. Rowan, A.D., Mason, P., Mach, L., and Mort, J.S. (1992) Rat procathepsin B: proteolytic processing to the mature form in vitro. J. Biol. Chem. 267, 15993-15999
16. Brömme, D., Bonneau, P.R., Lachance, P., Wiederanders, B., Kirschke, H., Peters, C., Thomas, D.Y., Storer, A.C., and Vernet, T. (1993) Functional expression of human cathepsin S in Saccharomyces cerevisiae: purification and characterization of the recombinant enzyme. J. Biol. Chem. 268, 4832-4838
17. Mach, L., Mort, J.S., and Glössl, J. (1994) Maturation of human procathepsin B: proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes. J. Biol. Chem. 269, 13030-13035
18. Kuhelj, R., Dolinar, M., Pungercar, J., and Turk, V. (1995) The preparation of catalytically active human cathepsin B from its precursor expressed in Escherichia coli in the form of inclusion bodies. Eur. J. Biochem. 229, 533-539
19. Kopitar, G., Dolinar, M., Strukelj, B., Pungercat, J., and Turk, V. (1996) Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli. Eur. J. Biochem. 236, 558-562
20. Vernet, T., Tessier, D.C., Laliberté, F., Dignard, D., and Thomas, D.Y. (1989) The expression in Escherichia coli of a synthetic gene coding for the precursor of papain is prevented by its own putative signal sequence. Gene 77, 229-236
21. Cohen, L.W., Fluharty, C., and Dihel, L.C. (1990) Synthesis of papain in Escherichia coli. Gene 88, 263-267
22. Vernet, T., Tessier, D.C., Richardson, C., Laliberté, F., Khouri, H.E., Bell, A.W., Storer, A.C., and Thomas, D.Y. (1990) Secretion of functional papain precursor from insect cells. J. Biol. Chem. 265, 16661-16666
23. Taylor, M.A.J., Pratt, K.A., Revell, D.F., Baker, K.C., Sumnar, I.G., and Goodenough, P.W. (1992) Active papain renatured and processed from insoluble recombinant propapain expressed in Escherichia coli. Protein Eng. 5, 455-459
24. Vernet, T., Chatellier, J., Tessier, D.C., and Thomas, D.Y. (1993) Expression of functional papain precursor in Saccharomyces cerevisiae: rapid screening of mutants. Protein Eng. 6, 213-219
25. Nakano, H., Yamazaki, T., Ikeda, M., Masai, H., Miyatake, S., and Saito, T. (1994) Purification of glutathione S-transferase fusion proteins as a non-degraded form by using a protease-negative E. coli strain, AD202. Nucleic Acids Res. 22, 543-544
26. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
27. Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, New York
28. 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. J. Biol. Chem. 263, 7655-7659
29. Misaka, T., Kuroda, M., Iwabuchi, K., Abe, K., and Arai, S. (1996) Soyacystatin, a novel cysteine proteinase inhibitor in soybean, is distinct in protein structure and gene organization from other cystatins of animal and plant origins. Eur. J. Biochem. 240, 609-614
30. Eakin, A.E., Mills, A.A., Harth, G., McKerrow, J.H., and Craik, C.S. (1992) The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi. J. Biol. Chem. 267, 7411-7420
31. Vernet, T., Khouri, H.E., Laflamme, P., Tessier, D.C., Musil, R., Gour-Salin, B.J., Storer, A.C., and Thomas, D.Y. (1991) Processing of the papain precursor: purification of the zymogen and characterization of its mechanism of processing. J. Biol. Chem. 266, 21451-21457
32. Kageyama, T. and Takahashi, S.Y. (1990) Purification and characterization of a cysteine proteinase from silkworm eggs. Eur. J. Biochem. 193, 203-210
33. Mason, R.W. and Massey, S.D. (1992) Surface activation of pro-cathepsin L. Biochem. Biophys. Res. Commun. 189, 1659-1666
34. Mason, R.W., Walker, J.E., and Northrop, F.D. (1986) The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Biochem. J. 240, 373-377
35. Watanabe, H., Abe, K., Emori, Y., Hosoyama, H., and Arai, S. (1991) Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (Oryzains). J. Biol. Chem. 266, 16897-16902
36. Cohen, L.W., Coghlan, V.M., and Dihel, L.C. (1986) Cloning and sequencing of papain-encoding cDNA. Gene 48, 219-227
37. Barrett, A.J. and Kirschke, H. (1981) Methods Enzymol. 80, 535-561
38. Abe, K., Emori, Y., Kondo, H., Suzuki, K., and Arai, S. (1987) Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). J. Biol. Chem. 262, 16793-16797
39. Petanceska, S. and Devi, L. (1992) Sequence analysis, tissue distribution, and expression of rat cathepsin S. J. Biol. Chem. 267, 26038-26043
40. Ishidoh, K. and Kominami, E. (1994) Multi-step processing of procathepsin L in vitro. FEBS Lett. 352, 281-284
41. Terra, W.R. and Ferreira, C. (1994) Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. 109B, 1-62