Identification of genes encoding for peptide synthetases in the gram-negative bacterium Lysobacter sp. ATCC 53042 and the fungus Cylindrotrichum oligospermum

References

• Bolivar R. “Construction and characterization of new cloning vehicles III. Derivates of plasmid pBR322 carrying unique EcoRI sites for selection of EcoRI generated recombinant molecules”. Gene 1978; 4: 121–136
   PubMed Web of Science ®Google Scholar
• Bonner D. P., O'Sullivan J., Tanaka S. K., Clark J. M., Whitney R. R. “Lysobactin, a novel antibacterial agent produced by Lysobacter sp. II. Biological properties”. J. Antibiotics 1988; 12: 1745–1751
   Google Scholar
• Borchert S., Patil S. S., Marahiel M. A. “Identification of putative multifunctional peptide synthetase genes using highly conserved oligonucleotide sequences derived from known synthetases”. FEMS Microbiol. Letters 1992; 92: 175–180
   Google Scholar
• Christensen P., Cook F. D. “Lysobacter, a new genus of nonfruiting, gliding bacteria with a high base ratio”. Int. J. Syst. Bacteriol. 1978; 28: 367–393
   Google Scholar
• Cosmina P., Rodriguez F., De Ferra F., Perego M., Venema G., Van Sinderen D. “Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus sub-tilis”. Molec. Microbiol. 1993; 8: 821–831
   PubMedGoogle Scholar
• Diez B., Gutierrez S., Barredo J. L., Van Solingen P., Van Der Voort L. H.M., Martin J. F. “The Cluster of Penicillin Biosynthetic Genes”. J. Biol. Chem. 1990; 265: 16358–16365
   PubMed Web of Science ®Google Scholar
• Gocht M., Marahiel M. A. “Analysis of Core Sequences in the D-Phe Activating Domain of the Multifunctional Peptide Synthetase TycA by Site-Directed Mutagenesis”. J. Bacteriol. 1994; 176: 2654–2662
   PubMedGoogle Scholar
• Gutierrez S., Diez B., Montenegro E., Martin J. F. “Characterization of the Cephalosporium acremonium pcbAB Gene Encoding α-Aminoadipyl-Cysteinyl-Valine Synthetase, a Large Multidomain Peptide Synthetase: Linkage to the pcbC Gene as a Cluster of Early Cephalosporin Biosynthetic Genes and Evidence of Multiple Functional Domains”. J. Bacteriol. 1991; 173: 2354–2365
   PubMed Web of Science ®Google Scholar
• Harada S., Tsubotani S., Hida T., Ono H., Okazaki H. “Structure of Lactivicin, an Antibiotic having a new nucleus and similar biological activities to β-lactam antibiotics”. Tetrahedron Letters 1986; 27: 6229–6232
   Google Scholar
• Hohn B., Collins J. “A small cosmid for efficient cloning of large DNA fragments”. Gene 1980; 11: 291–298
   PubMed Web of Science ®Google Scholar
• Kato T., Hinoo H., Terui Y., Kikuchi J., Shoji J. “The Structures of Katanosins A and B”. J. Antibiotics 1988; 41: 719–725
   PubMedGoogle Scholar
• Kimura H., Miyashita H., Sumino Y. Taheda Yakuhin Kogyo Co., Osaka. Patent 2–291274, 1994
   Google Scholar
• Kleinkauf H., DÖHren H. “Nonribosomal biosynthesis of peptide antibiotics”. Eur. J. Biochem. 1990; 192: 1–15
   PubMedGoogle Scholar
• Lawen A., Traber R., Geyl D. “In vitro biosynthesis of [Thr 2, Leu 5, D-Hiv 8, Leu 10]-cyclosporin, a cyclosporin related peptolide with immunosuppressive activity by a multienzyme polypeptide”. J. Biol. Chem. 1991; 266: 15567–15570
   PubMedGoogle Scholar
• Lawen A., Traber R. “Substrate Specificities of Cyclosporin Synthetase and Peptolide SDZ 214–103 Synthetase”. J. Biol. Chem. 1993; 268: 20452–20465
   PubMedGoogle Scholar
• Maccabe A. P., Van Liempt H., Palissa H., Unkles S. E., Riach M. B.R., Pfeifer E., Von DÖHren H., Kinghorn J. R. “δ-(L-α Aminoadipyl)-L-cysteinyl-D-valine Synthetase from Aspergillus nidulans”. J. Biol. Chem. 1991; 266: 12646–12654
   PubMed Web of Science ®Google Scholar
• Ono H., Nozaki Y., Katayama N., Okazaki H. “Cephabacins, new cephem antibiotics of bacterial origin”. J. Antibiotics 1984; 37: 1528–1535
   PubMed Web of Science ®Google Scholar
• O'Sullivan J., McCullough J. E., Tymiak A. A., Kirsch D. R., Trejo W. T., Principe P. A. “Lysobactin, a novel antibacterial agent produced by Lysobacter sp. I. Taxonomy, Isolation and partial Characterization”. J. Antibiotics 1988; 12: 1740–1744
   Google Scholar
• Priefer U., Simon R., PÜHler A. “Extension of the host range of Escherichia coli vectors by incorporation of RSF1010 replication and mobilization functions”. J. Bacterial. 1985; 163: 324–330
   PubMed Web of Science ®Google Scholar
• Sambrook J., Fritsch E. F., Maniatis T. “Molecular cloning: A Laboratory Manual”. Cold Spring Harbor Laboratory Press, New York 1989
   Google Scholar
• Schmidt B., Riesner D., Lawen A., Kleinkauf H. “Cyclosporin synthetase is a 1.4 MDa multienzyme polypeptide. Re-evaluation of the molecular mass of various peptide synthetases”. FEBS Lett. 1992; 307: 355–360
   PubMedGoogle Scholar
• Stachelhaus T., Marahiel M. A. “Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis”. FEMS Microbiol. Lett. 1995; 125: 3–14
   PubMed Web of Science ®Google Scholar
• Stachelhaus T., Schneider A., Marahiel M. A. “Rational Design of Peptide Antibiotics by Targeted Replacement of Bacterial and Fungal Domains”. Science 1995; 269: 69–72
   PubMed Web of Science ®Google Scholar
• Turgay K., Krause M., Marahiel M. A. “Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes”. Molec. Microbiol. 1992; 6: 529–546
   PubMedGoogle Scholar
• Turgay K., Marahiel M. A. “A General Approach for Identifying and Cloning Peptide Synthetase Genes”. Peptide Research 1994; 7: 238–241
   PubMedGoogle Scholar
• Tymiak A. A., McCormick T. J., Unger S. E. “Structure Determination of Lysobactin, a macrocyclic peptide lactone antibiotic”. J. Org. Chem. 1989; 54: 1149–1157
   Google Scholar
• Weber G., SchÖRgendorfer K., Schneider-Scherzer E., Leitner E. “The peptide synthetase catalyzing cyclosporin production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame”. Curr. Genetics 1994; 26: 120–125
   PubMedGoogle Scholar
• Woese C. R., Weisburg W. G., Hahn C M., Paster B. J., Zablen L. B., Lewis B. J., Macke T. J., Ludwig W., Stackebrandt E. “The phytogeny of purple bacteria: The gamma subdivision”. System. Appl. Microbiol. 1985; 6: 25–33
   Google Scholar