Molecular Cloning and Heterologous Expression of the Dehydrophos Biosynthetic Gene Cluster

Chemistry and Biology

Volumn 17, Issue 4, 2010, Pages 402-411

  Circello, Benjamin T ^a   Eliot, Andrew C ^a   Lee, Jin Hee ^a   van der Donk, Wilfred A ^a,b   Metcalf, William W ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

CHEMBIO

Indexed keywords

ANTIINFECTIVE AGENT; MUTASE; OLIGOPEPTIDE; PHOSPHOENOLPYRUVATE MUTASE; PHOSPHONIC ACID DERIVATIVE;

ARTICLE; BACTERIAL GENE; GENETICS; GENOMICS; METABOLISM; MOLECULAR CLONING; MULTIGENE FAMILY; MUTATION; STREPTOMYCES;

ANTI-BACTERIAL AGENTS; CLONING, MOLECULAR; GENES, BACTERIAL; GENOMICS; MULTIGENE FAMILY; MUTATION; OLIGOPEPTIDES; PHOSPHONIC ACIDS; PHOSPHOTRANSFERASES (PHOSPHOMUTASES); STREPTOMYCES;

STREPTOMYCES; STREPTOMYCES LIVIDANS; STREPTOMYCES LURIDUS;

EID: 77950960667     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.03.007     Document Type: Article

References (37)

1. Altschul S.F., Gish W., Miller W., Myers E.W., and Lipman D. Basic local alignment search tool. J. Mol. Biol. 215 (1990) 403-410
2. Biarrotte-Sorin S., Maillard A., Delettré J., Sougakoff W., Arthur M., and Mayer C. Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition. Structure 12 (2004) 257-267
3. Blodgett J.A., Zhang J., and Metcalf W. Molecular cloning, sequence analysis, and heterologous expression of the phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces viridochromogenes DSM 40736. Antimicrob. Agents Chemother. 49 (2005) 230-240
4. Blodgett J.A., Thomas P., Li G., Velasquez J.E., van der Donk W., Kelleher N., and Metcalf W. Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide. Nat. Chem. Biol. 3 (2007) 480-485
5. Bowman E., McQueney M., Barry R.J., and Dunawaymariano D. Catalysis and thermodynamics of the phosphoenolpyruvate/phosphonopyruvate rearrangement: entry into the phosphonate class of naturally-occurring organo-phosphorus compounds. J. Am. Chem. Soc. 110 (1988) 5575-5576
6. Cheek S., Ginalski K., Zhang H., and Grishin N. A comprehensive update of the sequence and structure classification of kinases. BMC Struct. Biol. 5 (2005) 6
7. Cicchillo R., Zhang H., Blodgett J., Whitteck J., Li G., Nair S., van der Donk W., and Metcalf W. An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis. Nature 459 (2009) 871-874
8. Datsenko K., and Wanner B. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97 (2000) 6640-6645
9. Diddens H., Zahner H., Kraas E., Gohring W., and Jung G. Transport of tripeptide antibiotics in bacteria. Eur. J. Biochem. 66 (1976) 11-23
10. Eliot A., and Kirsch J. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu. Rev. Biochem. 73 (2004) 383-415
11. Eliot A., Griffin B., Thomas P., Johannes T., Kelleher N., Zhao H., and Metcalf W. Cloning, expression, and biochemical characterization of Streptomyces rubellomurinus genes required for biosynthesis of antimalarial compound FR900098. Chem. Biol. 15 (2008) 765-770
12. Gondry M., Sauguet L., Belin P., Thai R., Amouroux R., Tellier C., Tuphile K., Jacquet M., Braud S., Courçon M., et al. Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes. Nat. Chem. Biol. 5 (2009) 414-420
13. Goward C., and Nicholls D. Malate dehydrogenase: a model for structure, evolution, and catalysis. Protein Sci. 3 (1994) 1883-1888
14. Gregory M., Till R., and Smith M. Integration site for Streptomyces phage phiBT1 and development of site-specific integrating vectors. J. Bacteriol. 185 (2003) 5320-5323
15. Inoue K., Kuramitsu S., Okamoto A., Hirotsu K., Higuchi T., and Kagamiyama H. Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes. Biochemistry 30 (1991) 7796-7801
16. Jia Y., Lu Z., Huang K., Herzberg O., and Dunaway-Mariano D. Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues. Biochemistry 38 (1999) 14165-14173
17. In: Johnson R., Kastner R., Larsen S., and Ose E. (Eds). Antibiotic A53868 and Process for Production Thereof, USPTO (1984), Eli Lilly and Company 14
18. Kieser T., Bibb M., Buttner M., Chater K., and Hopwood D. Practical Streptomyces Genetics (2000), The John Innes Foundation, Norwich, England
19. Kugler M., Loeffler W., Rapp C., Kern A., and Jung G. Rhizocticin A, an antifungal phosphono-oligopeptide of Bacillus subtilis ATCC 6633: biological properties. Arch. Microbiol. 153 (1990) 276-281
20. Lee J., Evans B., Li G., Kelleher N., and van der Donk W. In vitro characterization of a heterologously expressed nonribosomal peptide synthetase involved in phosphinothricin tripeptide biosynthesis. Biochemistry 48 (2009) 5054-5056
21. Liu P., Murakami K., Seki T., He X., Yeung S., Kuzuyama T., Seto H., and Liu H. Protein purification and function assignment of the epoxidase catalyzing the formation of fosfomycin. J. Am. Chem. Soc. 123 (2001) 4619-4620
22. Martinez A., Kolvek S., Yip C., Hopke J., Brown K., MacNeil I., and Osburne M. Genetically modified bacterial strains and novel bacterial artificial chromosome shuttle vectors for constructing environmental libraries and detecting heterologous natural products in multiple expression hosts. Appl. Environ. Microbiol. 70 (2004) 2452-2463
23. Metcalf W., and van der Donk W. Biosynthesis of phosphonic and phosphinic acid natural products. Annu. Rev. Biochem. 78 (2009) 65-94
24. Ntai I., Manier M., Hachey D., and Bachmann B. Biosynthetic origins of C-P bond containing tripeptide K-26. Org. Lett. 7 (2005) 2763-2765
25. O'Brien T., Kluger R., Pike D., and Gennis R. Phosphonate analogues of pyruvate. Probes of substrate binding to pyruvate oxidase and other thiamin pyrophosphate-dependent decarboxylases. Biochim. Biophys. Acta 613 (1980) 10-17
26. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: A Laboratory Manual (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
27. Schwartz D., Berger S., Heinzelmann E., Muschko K., Welzel K., and Wohlleben W. Biosynthetic gene cluster of the herbicide phosphinothricin tripeptide from Streptomyces viridochromogenes Tu494. Appl. Environ. Microbiol. 70 (2004) 7093-7102
28. Schwartz D., Grammel N., Heinzelmann E., Keller U., and Wohlleben W. Phosphinothricin tripeptide synthetases in Streptomyces viridochromogenes Tu494. Antimicrob. Agents Chemother. 49 (2005) 4598-4607
29. Seidel H., Freeman S., Seto H., and Knowles J. Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond. Nature 335 (1988) 457-458
30. Seto H., and Kuzuyama T. Bioactive natural products with carbon-phosphorus bonds and their biosynthesis. Nat. Prod. Rep. 16 (1999) 589-596
31. Shao Z., Blodgett J., Circello B., Eliot A., Woodyer R., Li G., van der Donk W., Metcalf W., and Zhao H. Biosynthesis of 2-hydroxyethylphosphonate, an unexpected intermediate common to multiple phosphonate biosynthetic pathways. J. Biol. Chem. 283 (2008) 23161-23168
32. Vogel H., and Bonner D. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218 (1956) 97-106
33. Whitteck J., Ni W., Griffin B., Eliot A., Thomas P., Kelleher N., Metcalf W., and van der Donk W. Reassignment of the structure of the antibiotic A53868 reveals an unusual amino dehydrophosphonic acid. Angew. Chem. Int. Ed. Engl. 46 (2007) 9089-9092
34. Willey J., and van der Donk W. Lantibiotics: peptides of diverse structure and function. Annu. Rev. Microbiol. 61 (2007) 477-501
35. Woodyer R., Shao Z., Thomas P., Kelleher N., Blodgett J., Metcalf W., van der Donk W., and Zhao H. Heterologous production of fosfomycin and identification of the minimal biosynthetic gene cluster. Chem. Biol. 13 (2006) 1171-1182
36. Zdobnov E., and Apweiler R. InterProScan-an integration platform for the signature-recognition methods in InterPro. Bioinformatics 17 (2001) 847-848
37. Zhang G., Dai J., Lu Z., and Dunaway-Mariano D. The phosphonopyruvate decarboxylase from Bacteroides fragilis. J. Biol. Chem. 278 (2003) 41302-41308