The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus
| Autor: | Diana R. Wetmore, Rodney S. Roche, Sui-Lam Wong |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
medicine.medical_treatment
Mutant Blotting Western Molecular Sequence Data Bacillus cereus Thermolysin Bacillus subtilis Microbiology Sequence Homology Nucleic Acid medicine Amino Acid Sequence Cloning Molecular Molecular Biology chemistry.chemical_classification Enzyme Precursors Bacillaceae Protease biology Base Sequence Nucleic acid sequence Metalloendopeptidases biology.organism_classification Molecular biology Amino acid Biochemistry chemistry Mutation Protein Processing Post-Translational |
| Zdroj: | Molecular microbiology. 6(12) |
| ISSN: | 0950-382X |
| Popis: | Summary The Bacillus cereus cnp gene coding for the thermolysin-like neutral protease (TNP) has been cloned, sequenced, and expressed in Bacillus subtilis. The protease is first produced as a pre-pro-protein (Mr= 61000); the pro-peptide is approximately two-thirds of the size of the mature protein. The pro-sequence has been compared with those of six other TNPs, and significant homologies have been found. Additionally, the TNP pro-sequences are shown to be homologous to the pro-sequence of Pseudomonas aeruginosa elastase. A mutant has been constructed from cnp, in which 23 amino acids upstream from the pro-protein processing site have been deleted. This region has no homologous analogue in any of the other TNP pro-sequences. The detection results in a delay of six to eight hours in detection of active protease in the growth medium, as well as a 75% decrease in maximum protease production. N-terminal analysis of the mutant mature protein demonstrates that the processing site is unaltered by the pro-sequence deletion. The deletion must, therefore, modulate the kinetics of processing and/or secretion of the pro-protein. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text