[Deletion analysis of the structural-functional organization of metalloendopeptidase precursor in B. amyloliquefaciens].
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.
Novikova
S I
SI
Stepanov Laboratory of Protein Chemistry, Federal Research Center GNIIGenetika, 1st Dorozhny pr., 1, 113545 Moscow, Russia.
Serkina
A V
AV
Konstantinova
G E
GE
Khlebalina
O I
OI
Chestukhina
G G
GG
Shevelev
A B
AB
D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins; D001483:Base Sequence; D004792:Enzyme Precursors / Q000235:genetics* / Q000302:isolation & purification; D008666:Metalloendopeptidases / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D017384:Sequence Deletion; D012697:Serine Endopeptidases / Q000235:genetics / Q000302:isolation & purification
D001426:Bacterial Proteins; D004792:Enzyme Precursors; D012697:Serine Endopeptidases; C104015:WprA protein, Bacillus subtilis; C024984:streptogrisin B; D008666:Metalloendopeptidases