Biological function of the pld gene product that degrades -poly-l-lysine in Streptomyces albulus
| Autor: | Hiroshi Takagi, Toyokazu Yoshida, Toru Nagasawa, Y. Hamano, Shigeru Nakamori, M. Kito |
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| Rok vydání: | 2006 |
| Předmět: |
DNA
Bacterial Sequence analysis Molecular Sequence Data Mutant Applied Microbiology and Biotechnology Streptomyces Gene product Open Reading Frames Sequence Analysis Protein Gene Order Polylysine Amino Acid Sequence Cloning Molecular Peptide sequence Gene biology Streptomycetaceae Sequence Analysis DNA General Medicine biology.organism_classification Molecular biology Anti-Bacterial Agents enzymes and coenzymes (carbohydrates) Open reading frame Biochemistry Genes Bacterial lipids (amino acids peptides and proteins) Sequence Alignment Gene Deletion Peptide Hydrolases Biotechnology |
| Zdroj: | Applied Microbiology and Biotechnology. 72:173-181 |
| ISSN: | 1432-0614 0175-7598 |
| Popis: | Epsilon-poly-L-lysine (epsilon-PL) is one of the few naturally occurring biopolymers and is characterized by a peptide bond between the alpha-carboxyl and epsilon-amino groups. Previously, we purified and characterized the epsilon-PL-degrading enzyme (Pld) from Streptomyces albulus, which is an epsilon-PL producer, and this enzyme was expected to confer self-resistance to the epsilon-PL produced by the organism itself. The gene encoding Pld was cloned based on the N-terminal amino acid sequence determined in this study, and a sequencing analysis revealed eight open reading frames (ORFs), i.e., ORF1 to ORF8 in the flanking region surrounding the pld gene (present in ORF5). To investigate the biological function of Pld, we constructed a knockout mutant in which the pld gene is inactivated. Studies on epsilon-PL susceptibility, epsilon-PL-degrading activity, and epsilon-PL productivity demonstrated that the pld gene does play a partial role in self-resistance and that S. albulus was found to produce other epsilon-PL-degrading enzyme(s) in addition to Pld. To the best of our knowledge, this is the first report on a self-resistance gene for a biopolymer possessing antibacterial activity. |
| Databáze: | OpenAIRE |
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