Streptokinase secretion by Serratia marcescens signaled by the C-terminal 41 amino acid segment of metalloprotease
| Autor: | Kwang-Hee Bae, Il Chul Kim, Si Myung Byun, Yong Chul Shin, Ki Seok Kim |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Signal peptide
Cytoplasm Recombinant Fusion Proteins Clinical Biochemistry Biochemistry Genetics Streptokinase Secretion Molecular Biology Gene Serratia marcescens chemistry.chemical_classification Metalloproteinase biology Metalloendopeptidases Biological Transport Cell Biology biology.organism_classification Fusion protein Culture Media Amino acid chemistry Genes Bacterial Plasmids |
| Zdroj: | IUBMB Life. 45:725-733 |
| ISSN: | 1521-6543 |
| DOI: | 10.1080/15216549800203132 |
| Popis: | In order to investigate the secretion signal of Serratia marcescens metalloprotease (SMP) and examine the ability of the secretion signal to secrete foreign proteins, hybrid genes encoding the passenger-SMP C-terminal segments were constructed. As a passenger protein, streptokinase (SK) deprived of its signal peptide was used. Three kinds of SMP C-terminal segments containing 41, 80, or 220 amino acid residues were fused to the C-terminus of SK as secretion signals. The SK-SMP chimeric proteins containing 41 or 220 amino acid segments of the SMP C-terminus were secreted into the culture medium by the SMP transporter of S. marcescens. This result suggests that cytoplasmic SK is secreted into the external medium by the C-terminal segments of SMP and also shows that the smallest, 41 amino acid segment of the SMP C-terminus functions as a secretion signal of foreign proteins as well as SMP. |
| Databáze: | OpenAIRE |
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