Characterization of two metagenome-derived esterases that reactivate chloramphenicol by counteracting chloramphenicol acetyltransferase

Journal of Microbiology and Biotechnology

Volumn 21, Issue 12, 2011, Pages 1203-1210

  Tao, Weixin ^a   Lee, Myung Hwan ^a   Yoon, Mi Young ^b   Kim, Jin Cheol ^b   Malhotra, Shweta ^a   Wu, Jing ^a   Hwang, Eul Chul ^a   Lee, Seon Woo ^a  

^a Dong A University   (South Korea)

^b Korea Research Institute of Chemical Technology   (South Korea)

Author keywords

Chloramphenicol acetyltransferase; Chloramphenicol reactivation; Esterase; Metagenomics

Indexed keywords

CHLORAMPHENICOL; CHLORAMPHENICOL ACETATE ESTERASE; CHLORAMPHENICOL ACETYLTRANSFERASE; ESTDL136 PROTEIN; ESTDL26 PROTEIN; ESTERASE; HORMONE SENSITIVE LIPASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DEACETYLATION; ESCHERICHIA COLI; GENETIC VARIABILITY; IN VITRO STUDY; METAGENOMICS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN FAMILY; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BACTERIA; BIOCATALYSIS; CHLORAMPHENICOL; CHLORAMPHENICOL O-ACETYLTRANSFERASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; ESTERASES; METAGENOME; MOLECULAR SEQUENCE DATA; PHYLOGENY; SEQUENCE ALIGNMENT; SOIL MICROBIOLOGY; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 84855237706     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1107.07034     Document Type: Article

References (35)

1. Alexander, N. J., S. P. McCormick, C. Waalwijk, T. van der Lee, and R. H. Proctor. 2011. The genetic basis for 3-ADON and 15-ADON trichothecene chemotypes in Fusarium. Fungal Genet. Biol. 48: 485-495.
2. Amann, R. I., W. Ludwig, and K. H. Schleifer. 1995. Phylogenetic identification and in situ detection of individual microbial cells without cultivation. Microbiol. Rev. 59: 143-169.
3. Arpigny, J. L. and K. E. Jaeger. 1999. Bacterial lipolytic/enzymes: Classification and properties. Biochem. J. 343: 177-183.
4. Bornscheuer, U. T. 2002. Microbial carboxyl esterases: Classification, properties and application in biocatalysis. FEMS. Microbiol. Rev. 26: 73-81.
5. Cundliffe, E. 1989. How antibiotic-producing organisms avoid suicide. Annu. Rev. Microbiol. 43: 207-233.
6. Gross, F., E. A. Lewis, M. Piraee, K. H. Van Pee, L. C. Vining, and R. L. White. 2002. Isolation of 3'-O-acetylchloramphenicol: A possible intermediate in chloramphenicol biosynthesis. Bioorg. Med. Chem. Lett. 12: 283-286.
7. Handelsman, J. 2004. Metagenomics: Application of genomics to uncultured microorganisms. Microbiol. Mol. Biol. Rev. 68: 669-685.
8. He, J., N. Magarvey, M. Piraee, and L. C. Vining. 2001. The gene cluster for chloramphenicol biosynthesis in Streptomyces venezuelae ISP5230 includes novel Shikimate pathway homologues and a monomodular nonribosomal peptide synthetase gene. Microbiology 147: 2817-2829.
9. Henne, A., R. A. Schmitz, M. Bomeke, G. Gottschalk, and R. Daniel. 2000. Screening of environmental DNA libraries for the presence of genes conferring lipolytic activity on Escherichia coli. Appl. Environ. Microbiol. 66: 3113-3116.
10. Hong, K. S., H. K. Lim, E. J. Chung, E. J. Park, M. H. Lee, J. C. Kim, G. J. Choi, K. Y. Cho, and S. W. Lee. 2007. Selection and characterization of forest soil metagenome genes encoding lipolytic enzymes. J. Microbiol. Biotechnol. 17: 1655-1660.
11. Hu, Y., G. Zhang, A. Li, J. Chen, and L. Ma. 2008. Cloning and enzymatic characterization of a xylanase gene from a soilmetagenomic library with an efficient approach. Appl. Microbiol. Biotechnol. 80: 823-830.
12. Jaeger, K. E., B. W. Dijkstra, and M. T. Reetz. 1999. Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu. Rev. Microbiol. 53: 315-351.
13. Jeanmougin, F., J. D. Thompson, M. Gouy, D. G. Higgins, and T. J. Gibson. 1998. Multiple sequence alignment with Clustal X. Trends Biochem. Sci. 23: 403-405.
14. Jeon, J. H., J. T. Kim, S. G. Kang, J. H. Lee, and S. J. Kim. 2009. Characterization and its potential application of two esterases derived from the arctic sediment metagenome. Mar. Biotechnol. (NY) 11: 307-316.
15. Kim, Y. J., G. S. Choi, S. B. Kim, G. S. Yoon, Y. S. Kim, and Y. W. Ryu. 2006. Screening and characterization of a novel esterase from a metagenomic library. Protein Expr. Purif. 45: 315-323.
16. Kimura, M., I. Kaneko, M. Komiyama, A. Takatsuki, H. Koshino, K. Yoneyama, and I. Yamaguchi. 1998. Trichothecene 3-O-acetyltransferase protects both the producing organism and transformed yeast from related mycotoxins. Cloning and characterization of Tri101. J. Biol. Chem. 273: 1654-1661.
17. Kneusel, R. E., E. Schiltz, and U. Matern. 1994. Molecular characterization and cloning of an esterase which inactivates the macrolide toxin brefeldin A. J. Biol. Chem. 269: 3449-3456.
18. Lee, M. H., K. S. Hong, S. Malhotra, J. H. Park, E. C. Hwang, H. K. Choi, Y. S. Kim, W. Tao, and S. W. Lee. 2010. A new esterase EstD2 isolated from plant rhizosphere soil metagenome. Appl. Microbiol. Biotechnol. 88: 1125-1134.
19. Lee, S. W., L. Won, H. K. Lim, J. C. Kim, G. J. Choi, and K. Y. Cho. 2004. Screening for novel lipolytic enzymes from uncultured soil microorganisms. Appl. Microbiol. Biotechnol. 65: 720-726.
20. Lewis, E. A., T. L. Adamek, L. C. Vining, and R. L. White. 2003. Metabolites of a blocked chloramphenicol producer. J. Nat. Prod. 66: 62-66.
21. Lim, H. K., E. J. Chung, J. C. Kim, G. J. Choi, K. S. Jang, Y. R. Chung, K. Y. Cho, and S. W. Lee. 2005. Characterization of a forest soil metagenome clone that confers indirubin and indigo production on Escherichia coli. Appl. Environ. Microbiol. 71: 7768-7777.
22. Mandrich, L., V. Menchise, V. Alterio, G. D. Simone, C. Pedone, M. Rossi, and G. Manco. 2008. Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius. Proteins 71: 1721-1731.
23. McCormick, S. P. and N. J. Alexander. 2002. Fusarium Tri8 encodes a trichothecene C-3 esterase. Appl. Environ. Microbiol. 68: 2959-2964.
24. Nakagawa, Y., Y. Nitahara, and S. Miyamura. 1979. Kinetic studies on enzymatic acetylation of chloramphenicol in Streptococcus faecalis. Antimicrob. Agents Chemother. 16: 719-723.
25. Nakano, H., Y. Matsuhashi, T. Takeuchi, and H. Umezawa. 1977. Distribution of chloramphenicol acetyltransferase and chloramphenicol-3-acetate esterase among Streptomyces and Corynebacterium. J. Antibiot. (Tokyo) 30: 76-82.
26. Ping, L., R. Buchler, A. Mithofer, A. Svatos, D. Spiteller, K. Dettner, et al. 2007. A novel Dps-type protein from insect gut bacteria catalyses hydrolysis and synthesis of N-acyl amino acids. Environ. Microbiol. 9: 1572-1583.
27. Pongs, O. 1979. Chloramphenicol. pp. 26-42. In F. E. Hahn (ed.). Antibiotics: Mechanism of Action of Antibacterial Agents. Springer-Verlag, Berlin.
28. Rhee, J. K., D. G. Ahn, Y. G. Kim, and J. W. Oh. 2005. New thermophilic and thermostable esterase with sequence similarity to the hormone-sensitive lipase family, cloned from a metagenomic library. Appl. Environ. Microbiol. 71: 817-825.
29. Riaz, K., C. Elmerich, D. Moreira, A. Raffoux, Y. Dessaux, and D. Faure. 2008. A metagenomic analysis of soil bacteria extends the diversity of quorum-quenching lactonases. Environ. Microbiol. 10: 560-570.
30. Shaw, W. V. 1983. Chloramphenicol acetyltransferase: Enzymology and molecular biology. Crit. Rev. Biochem. 14: 1-46.
31. Sohaskey, C. D. 2004. Enzymatic inactivation and reactivation of chloramphenicol by Mycobacterium tuberculosis and Mycobacterium bovis. FEMS. Microbiol. Lett. 240: 187-192.
32. Sohaskey, C. D. and A. G. Barbour. 1999. Esterases in serumcontaining growth media counteract chloramphenicol acetyltransferase activity in vitro. Antimicrob. Agents Chemother. 43: 655-660.
33. Sohaskey, C. D. and A. G. Barbour. 2000. Spirochaeta aurantia has diacetyl chloramphenicol esterase activity. J. Bacteriol. 182: 1930-1934.
34. Tamura, K., J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24: 1596-1599.
35. Zhou, J., M. A. Bruns, and J. M. Tiedje. 1996. DNA recovery from soils of diverse composition. Appl. Environ. Microbiol. 62: 316-322.