Summary
The gene encoding lysostaphin of Staphylococcus staphylolyticus was cloned in Escherichia coli and its DNA sequence was determined. The complete coding region comprises 1440 base pairs corresponding to a precursor of 480 amino acids (molecular weight 51669). It was shown by NH2-terminal amino acid sequence analysis of the purified extracellular lysostaphin from S. staphylolyticus that the mature lysostaphin consists of 246 amino acid residues (molecular weight 26926). Polyacrylamide gel electrophoresis revealed a similar molecular weight for the most active form. By computer analysis the secondary protein structure was predicted. It revealed three distinct regions in the precursor protein: a typical signal peptide (ca. 38 aa), a hydrophilic and highly ordered protein domain with 14 repetitive sequences (296 aa) and the hydrophobic mature lysostaphin. The lysostaphin precursor protein appears to be organized as a preprolysostaphin.
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Abbreviations
- aa:
-
amino acid(s)
References
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Communicated by J. Lengeler
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Heinrich, P., Rosenstein, R., Böhmer, M. et al. The molecular organization of the lysostaphin gene and its sequences repeated in tandem. Mol Gen Genet 209, 563–569 (1987). https://doi.org/10.1007/BF00331163
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DOI: https://doi.org/10.1007/BF00331163