The efficiency of processing and secretion of the thermolysin-like neutral protease from Bacillus cereus does not require the whole prosequence, but does depend on the nature of the amino acid sequence in the region of the cleavage site
| Autor: | Diana R. Wetmore, Rodney S. Roche, Sui-Lam Wong |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
chemistry.chemical_classification
Protease Base Sequence medicine.medical_treatment Molecular Sequence Data Thermolysin Bacillus cereus Metalloendopeptidases Biology Cleavage (embryo) biology.organism_classification Microbiology Amino acid chemistry Biochemistry Consensus sequence medicine Secretion Amino Acid Sequence Sequence Analysis Molecular Biology Peptide sequence |
| Zdroj: | Molecular Microbiology. 12:747-759 |
| ISSN: | 1365-2958 0950-382X |
| DOI: | 10.1111/j.1365-2958.1994.tb01062.x |
| Popis: | Summary Using deletion mutants, It is shown that part of the prosequence, the Ω-peptide (-4, -24), of the thermolysin-like neutral protease (TNP) from Bacillus cereus, Cnp, is not required for efficient processing and secretion of fully functional mature protease. It is demonstrated that the rate and selectivity of pro-protein processing is dependent on both the flexibility and primary sequence of the processing site. Processing is found to be particularly sensitive to the nature of the amino acid three residues upstream from the site of cleavage. A consensus sequence for TNP pro-protein processing has been identified, which provides further Insights. Finally, a larger deletion of a portion of the Cnp prosequence upstream from the Ω-peptide that includes amino acids conserved among TNPs reduces the rate of processing and secretion of Cnp and results in the accumulation of export-incompetent pre-proprotein in the cell fraction. |
| Databáze: | OpenAIRE |
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