| Autor: |
Novikova SI; Stepanov Laboratory of Protein Chemistry, Federal Research Center GNIIGenetika, 1st Dorozhny pr., 1, 113545 Moscow, Russia., Serkina AV, Konstantinova GE, Khlebalina OI, Chestukhina GG, Shevelev AB |
| Jazyk: |
ruština |
| Zdroj: |
Voprosy meditsinskoi khimii [Vopr Med Khim] 2001 Jan-Feb; Vol. 47 (1), pp. 123-31. |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
