Determination of the gene sequence and the molecular structure of the enterococcal peptide antibiotic AS-48
Autor: | Antonio Gálvez, Manuel Martínez-Bueno, Jacques Coyette, Mercedes Maqueda, Eva Valdivia, B Samyn, J. Van Beeumen |
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Rok vydání: | 1994 |
Předmět: |
DNA
Bacterial Signal peptide Protein Conformation Sequence analysis Molecular Sequence Data Peptide Biology Peptides Cyclic Microbiology PEST sequence Protein structure Bacterial Proteins Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence chemistry.chemical_classification Base Sequence Peptide sequence tag Peptide Fragments Cyclic peptide Anti-Bacterial Agents Biochemistry chemistry Genes Bacterial Peptides Protein Processing Post-Translational Sequence Analysis Enterococcus Research Article |
Zdroj: | Journal of Bacteriology. 176:6334-6339 |
ISSN: | 1098-5530 0021-9193 |
DOI: | 10.1128/jb.176.20.6334-6339.1994 |
Popis: | The structural gene of the enterococcal peptide antibiotic AS-48 (as-48) has been identified and cloned by using two degenerate 17-mer DNA oligonucleotides on the basis of the amino acid sequences of two peptides obtained by digestion of the antibiotic with Glu-C endoproteinase. That as-48 gene codes for a 105-amino-acid prepeptide, giving rise to a 70-amino-acid mature protein. Comparative analysis demonstrated that the 16-amino-acid sequence of one of the AS-48 Glu-C peptides, designated V8-5, was composed of a 12-amino-acid sequence corresponding to the C-terminal end sequence (from isoleucine +59 to tryptophan +70 [I+59 to W+70]) of the prepeptide and terminated in four residues forming the N terminus (M+1 to E+4) of a putative AS-48 propeptide. These data, combined with the characteristics of the gene sequence, strongly suggested that the antibiotic peptide was a 70-residue cyclic molecule. We propose that the AS-48 translated primary product is very likely submitted to a posttranslational modification during secretion (i) by an atypical or a typical signal peptidase that cleaves off a 35-residue or shorter signal peptide, respectively, from the prepeptide molecule and (ii) by the linkage of the methionine residue (M+1) to the C-terminal tryptophan residue (W+70) to obtain the cyclic peptide (a tail-head linkage). |
Databáze: | OpenAIRE |
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