Polymorphism of trypsin and chymotrypsin binding loops in Bowman-Birk inhibitors from common bean (Phaseolus vulgaris L.)

Plant Science

Volumn 166, Issue 6, 2004, Pages 1525-1531

  Piergiovanni, Angela R ^a   Galasso, Incoronata ^a  

^a Institute of Biosciences and Bioresources   (Italy)

Author keywords

Bowman Birk inhibitor; Canonical loop; Common bean; Diversity; Proteinase inhibitors

Indexed keywords

CROPS; DNA; ENZYME INHIBITION;

BOWMAN-BRICK INHIBITORS (BBI); POLYMORPHISM; TRYPSIN BINDING LOOP;

PROTEINS;

PHASEOLUS (ANGIOSPERM); PHASEOLUS VULGARIS;

EID: 1942510393     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2004.02.005     Document Type: Article

References (28)

1. J.J. Rachis, W.J. Wolf, E.C. Baker, Proteinase inhibitors in plant foods: content and inactivation, in: M. Friedman (Ed.), Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods, Plenum Press, New York, 1986, pp. 299-347.
2. Gupta Y.P. Antinutritional and toxic factors in food legumes: a review. Plant Food Hum. Nutr. 37:1987;201-228.
3. Ryan C.A. Proteinase inhibitors in plants: genes for improving defences against insects and pathogens. Annu. Rev. Phytopathol. 28:1990;425-449.
4. Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49:1980;593-626.
5. Kennedy A.R. Chemopreventive agents: protease inhibitors. Pharmacol. Ther. 78:1998;167-209.
6. Schecter J., Berger A. On the size of the active site proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:1967;157-162.
7. McBride J.D., Watson E.M., Brauer A.B.E., Jaulent A.M., Leatherbarrow R.J. Peptide mimics of the Bowman-Birk inhibitor reactive site loop. Biopolymers (Pept. Sci.). 66:2002;79-92.
8. Nishino N., Aoyagi H., Kato T., Izumiya N. Studies on the synthesis of proteinase inhibitors. J. Biochem. 82:1977;901-909.
9. 2′ variation in cyclic peptides encompassing the reactive site loop Biochem. Biophys. Acta. 1431:1999;232-237.
10. McBride J.D., Freeman N., Domingo G.J., Leatherbarrow R.J. Selection of chymotrypsin inhibitors from a conformational-constrained combinatorial peptide library. J. Mol. Biol. 259:1996;819-827.
11. 2 variation in cyclic peptides encompassing the reactive site loop. J. Mol. Biol. 282:1998;447-458.
12. Tan-Wilson A.L., Wilson K.A. Relevance of multiple soybean trypsin inhibitor forms to nutritional quality. Adv. Exp. Med. Biol. 199:1986;391-411.
13. Wu C., Whitaker J.R. Purification and partial characterisation of four trypsin/chymotrypsin inhibitors from red kidney beans (Phaseolus vulgaris var. Linden). J. Agric. Food Chem. 38:1990;1523-1529.
14. Bergeron D., Nielsen S.S. Partial characterisation of trypsin inhibitors and N-terminal sequences of five trypsin isoinhibitors of Great Northern Beans (Phaseolus vulgaris). J. Agric. Food Chem. 41:1993;1544-1549.
15. Domoney C., Welham T., Sidebottom C. Purification and characterisation of Pisum seed trypsin inhibitors. J. Exp. Bot. 44:1993;701-709.
16. Welham T., O'Neill M., Johnson S., Wang T.L., Domoney C. Expression patterns of genes encoding seed trypsin inhibitors in Pisum sativum. Plant Sci. 131:1998;13-24.
17. Page D., Aubert G., Due G., Welham T., Domoney C. Combinatorial variation in coding and promoter sequences of genes at the Tri locus in Pisum sativum accounts for variation in trypsin inhibitor activity in seeds. Mol. Genet. Genomics. 267:2002;359-369.
18. Limongelli G., Laghetti G., Perrino P., Piergiovanni A.R. Variation of seed storage proteins in landraces of common bean (Phaseolus vulgaris L.) from Basilicata, Southern Italy. Euphytica. 92:1996;393-399.
19. Piergiovanni A.R., Cerbino D., Brandi M. The common bean populations from Basilicata (Southern Italy). An evaluation of their variation. Genet. Resour. Crop Evol. 47:2000;489-495.
20. Piergiovanni A.R., Pignone D. Effect of year-to-year variation and genotype on trypsin inhibitor level in common bean (Phaseolus vulgaris L.) seeds. J. Sci. Food Agric. 83:2003;473-476.
21. De Miera L.E.S., de la Vega M.P. A comparative studies of vicilin genes in Lens: negative evidences of concerted evolution. Mol. Biol. Evol. 15:1998;303-311.
22. Mello M.O., Tanaka A.S., Silva-Filho M.C. Molecular evolution of Bowman-Birk type proteinase inhibitors in flowering plants. Mol. Phylogenet. Evol. 27:2003;103-112.
23. 1 NMR solution structure of the antitryptic core peptide of Bowman-Birk inhibitor proteins: a minimal 'Canonical loop'. J. Biomol. Struct. Dyn. 20:2002;59-70.
24. Brauer A.B.E., McBride J.D., Cooke R.M., Matthews S.J., Leatherbarrow R.J. The Bowman-Birk inhibitor reactive site loop sequence represents an independent structural β-harpin motif. J. Mol. Biol. 306:2001;799-807.
25. Yavelow J., Collins M., Birk Y., Troll W., Kenned A.R. Nanomolar concentrations of Bowman-Birk proteinase inhibitor suppress X-ray induced transformation in vitro. Proc. of Natl. Acad. Sci. U.S.A. 82:1985;5395-5399.
26. Rahbé Y., Ferrasson E., Rabesona H., Quillien L. Toxicity to the pea aphid Acyrthosiphon pisum of anti-chymotrypsin isoforms and fragments of Bowman-Birk protease inhibitors from pea seeds. Insect Biochem. Mol. Biol. 33:2003;299-306.S.
27. Odani, T.J. Ono, Chemical substitutions of the reactive site leucine residue in soybean Bowman-Birk proteinase inhibitor with other amino acids, J. Biochem. 88 (1980) 1555-1558
28. Welham T., Domoney C. Temporal and spatial activity of a promoter from a pea enzyme inhibitor gene and its exploitation for seed quality improvement. Plant Sci. 159:2000;289-299.