Functional destination of propeptides and precursors in bacillar secretory proteases remains uncertain. Formerly deletion assay demonstrated folding and secretion of subtilisin E, chymotrypsin-like protease SGPB from S. griseus and B. cereus metalloprotease to depend on full-length propeptide in the precursors. Actually an artificial B. amyloliquefaciens metalloprotease gene with deletion of 51 amino acid residues from N-terminus was constructed with regard to carry out functional mapping of secretory metalloprotease propeptides. B. subtilis wprA gene 5’-terminal region spanning promoter and secretory leader was coupled to provide transcription to the truncated gene and secretion to its product. B. subtilis clones bearing a plasmid with the modified gene synthesised an active mature metalloprotease
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Novikova S.I., Serkina A.V., Konstantinova G.E., Khlebalina O.I., Chestukhina G.G., Shevelev A.B. (2001) Study of structural and functional oreganization in B. amyloliquefaciens metalloendopeptidase precursor by deletion analysis. Voprosy Meditsinskoi Khimii, 47(1), 123-131.
Novikova S.I. et al. Study of structural and functional oreganization in B. amyloliquefaciens metalloendopeptidase precursor by deletion analysis // Voprosy Meditsinskoi Khimii. - 2001. - V. 47. -N 1. - P. 123-131.
Novikova S.I. et al., "Study of structural and functional oreganization in B. amyloliquefaciens metalloendopeptidase precursor by deletion analysis." Voprosy Meditsinskoi Khimii 47.1 (2001): 123-131.
Novikova, S. I., Serkina, A. V., Konstantinova, G. E., Khlebalina, O. I., Chestukhina, G. G., Shevelev, A. B. (2001). Study of structural and functional oreganization in B. amyloliquefaciens metalloendopeptidase precursor by deletion analysis. Voprosy Meditsinskoi Khimii, 47(1), 123-131.
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