The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle toE. coli-based protein production
| Autor: | Ei-ichi Matsuo, Koreaki Ito, Gen-ichi Sampei, Kiyoshi Mizobuchi |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Recombinant protein
Hydrolases medicine.medical_treatment Proteolysis Biophysics Biology medicine.disease_cause Biochemistry law.invention OmpP Plasmid Bacterial Proteins Structural Biology law Escherichia coli Genetics medicine Protein biosynthesis OmpT Molecular Biology Protease medicine.diagnostic_test Escherichia coli Proteins Serine Endopeptidases SecY Gene Expression Regulation Bacterial Cell Biology Molecular biology Recombinant Proteins Membrane protein Genes Bacterial F plasmid Recombinant DNA SEC Translocation Channels Bacterial Outer Membrane Proteins Plasmids |
| Zdroj: | FEBS Letters. 461:6-8 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(99)01418-0 |
| Popis: | OmpT, an outer membrane-localized protease of Escherichia coli, cleaves a number of exogenous and endogenous proteins during their purification. SecY, an endogenous membrane protein, is a target of this artificial proteolysis in vitro. Here we report that SecY cleavage occurs even in cell extracts from ompT-disrupted cells, if they carry an F plasmid derivative. A gene, ompP, on the F plasmid was shown to be responsible for this proteolysis. These results indicate that the absence of an F-like plasmid should be checked when choosing a host strain for E. coli-based protein production. |
| Databáze: | OpenAIRE |
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