Homologous expression of aspartokinase (ask) gene in Streptomyces clavuligerus and its hom-deleted mutant: Effects on cephamycin C production

Bioengineered Bugs

Volumn 1, Issue 3, 2010, Pages 191-197

  Özcengiz, Gülay ^a   Okay, Sezer ^a   Ünsaldi, Eser ^a   Taşkin, Bilgin ^a   Liras, Paloma ^b   Piret, Jacqueline ^c  

^a MIDDLE EAST TECHNICAL UNIVERSITY   (Turkey)

^b UNIVERSITY OF LEÓN   (Spain)

^c NORTHEASTERN UNIVERSITY   (United States)

Author keywords

Aspartate pathway; Aspartokinase; Cephamycin C; Homologous expression; Streptomyces clavuligerusis

Indexed keywords

AMINO ACID; ASPARTATE KINASE; BACTERIAL VECTOR; BETA LACTAM ANTIBIOTIC; CEPHAMYCIN C;

ARTICLE; BACTERIAL CELL; BACTERIAL GENETICS; BACTERIAL STRAIN; BACTERIUM MUTANT; CELL GROWTH; CONTROLLED STUDY; CULTURE MEDIUM; DRUG SYNTHESIS; ENZYME ACTIVITY; ENZYME DEGRADATION; GENE AMPLIFICATION; GENE DOSAGE; GENE INSERTION; GENE POOL; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FOLDING; STREPTOMYCES CLAVULIGERUS; WILD TYPE;

ASPARTATE KINASE; BACTERIAL PROTEINS; BIOENGINEERING; CEPHAMYCINS; CULTURE MEDIA; GENE DOSAGE; GENE EXPRESSION; HOMOSERINE DEHYDROGENASE; SEQUENCE DELETION; STREPTOMYCES;

STREPTOMYCES; STREPTOMYCES CLAVULIGERUS;

EID: 79851474936     PISSN: 19491018     EISSN: 19491026     Source Type: Journal    
DOI: 10.4161/bbug.1.3.11244     Document Type: Article

References (35)

1. Zhang J, Wolfe S, Demain AL. Biochemical studies on the activity of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Streptomyces clavuligerus. Biochem J 1992; 283:691-8.
2. Kern BA, Hendlin D, Inamine E. L-lysine-ε-aminotransferase involved in cephamycin C synthesis in Streptomyces lactamdurans. Antimicrob Agents Chemother 1980; 17:679-85.
3. Malmberg LH, Hu WS, Sherman DH. Effects of enhanced lysine ε-aminotransferase activity on cephamycin biosynthesis in Streptomyces clavuligerus. Appl Microbiol Biotechnol 1995; 44:198-205.
4. Rius N, Maeda K, Demain AL. Induction of L-lysine-ε-aminotransferase by L-lysine in Streptomyces clavuligerus, producer of cephalosporins. FEMS Microbiol Lett 1996; 144:207-11.
5. Malumbres M, Martin JF. Molecular control mechanisms of lysine and threonine biosynthesis in amino acid-producing corynebacteria: redirecting carbon flow. FEMS Microbiol Lett 1996; 143:103-14.
6. Kalinowski J, Bachmann B, Thierbach G, Puhler A. Aspartokinase genes lysCα and lysCβ overlap and are adjacent to the aspartate β-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum. Mol Gen Genet 1990; 224:317-24.
7. Chen NY, Jiang SQ, Klein DA, Paulus H. Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. J Biol Chem 1993; 268:9448-65.
8. Cirillo JD, Weisbrod TR, Pascopella L, Bloom BR, Jacobs WR Jr. Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria. Mol Microbiol 1994; 11:629-39.
9. Zhang W, Jiang W, Zhao G, Yang Y, Chiao J. Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV-producing Amycolatopsis mediterranei. Gene 1999; 237:413-9.
10. Hernando-Rico V, Martin JF, Santamarta I, Liras P. Structure of the ask-asd operon and formation of aspartokinase subunits in the cephamycin producer "Amycolatopsis lactamdurans". Microbiology 2001; 147:1547-55.
11. Tunca S, Yilmaz EI, Piret J, Liras P, Ozcengiz G. Cloning, characterization and heterologous expression of the aspartokinase and aspartate semialdehyde dehydrogenase genes of cephamycin C-producer Streptomyces clavuligerus. Res Microbiol 2004; 155:525-34.
12. Le Y, He J, Vining LC. Streptomyces akiyoshiensis differs from other gram-positive bacteria in the organization of a core biosynthetic pathway gene for aspartate family amino acids. Microbiology 1996; 142:791-8.
13. Theze J, Margarita D, Cohen GN, Borne F, Patte JC. Mapping of the structural genes of three aspartokinases and of the two homoserine dehydrogenases of Escherichia coli K12. J Bacteriol 1974; 117:133-43.
14. Zhang JJ, Hu FM, Chen NY, Paulus H. Comparison of the three aspartokinase isoenzymes in Bacillus subtilis Marburg and 168. J Bacteriol 1990; 172:701-8.
15. Zhang WW, Jiang WH, Zhao GP, Yang YL, Chiao JS. Expression in Escherichia coli, purification and kinetic analysis of the aspartokinase and aspartate semialdehyde dehydrogenase from the rifamycin SV-producing Amycolatopsis mediterranei U32. Appl Microbiol Biotechnol 2000; 54:52-8.
16. Mendelovitz S, Aharonowitz Y. Regulation of cephamycin C synthesis, aspartokinase, dihydrodipicolinic acid synthetase and homoserine dehydrogenase by aspartic acid family amino acids in Streptomyces clavuligerus. Antimicrob Agents Chemother 1982; 21:74-84.
17. Yi{dotless}lmaz EI, Çaydasi AK, Özcengiz G. Targeted disruption of homoserine dehydrogenase gene and its effect on cephamycin C production in Streptomyces clavuligerus. J Ind Microbiol Biotechnol 2008; 35:1-7.
18. Aharonowitz Y, Demain AL. Carbon catabolite regulation of cephalosporin production in Streptomyces clavuligerus. Antimicrob Agents Chemother 1978; 14:159-64.
19. Saudagar PS, Singhal RS. Optimization of nutritional requirements and feeding strategies for clavulanic acid production by Streptomyces clavuligerus. Bioresource Technol 2007; 98:2010-7.
20. Chmiel A, Brzeszczynska A, Kabza B. Biosynthesis of cephamycin by resting cells of Streptomyces lactamdurans L 2/6. Acta Microbiol Pol 1986; 35:251-7.
21. Khaoua S, Lebrihi A, Germain P, Lefebvre G. Cephamycin C biosynthesis in Streptomyces cattleya: nitrogen source regulation. Appl Microbiol Biotechnol 1991; 35:253-7.
22. Çakar ZP, Sauer U, Bailey JE. Metabolic engineering of yeast: the perils of auxotrophic hosts. Biotechnol Lett 1999; 21:611-6.
23. Hopwood DA, Merrick MJ. Genetics of antibiotic production. Bacteriol Rev 1977; 41:595-635.
24. Malmberg LH, Hu WS, Sherman DH. Precursor flux control through targeted chromosomal insertion of the lysine epsilon-aminotransferase (lat) gene in cephamycin C biosynthesis. J Bacteriol 1993; 175:6916-24.
25. Perez-Llarena FJ, Liras P, Rodriguez-Garcia A, Martin JF. A regulatory gene (ccaR) required for cephamycin and clavulanic acid production in Streptomyces clavuligerus: amplification results in overproduction of both β-lactam compounds. J Bacteriol 1997; 179:2053-9.
26. Santamarta I, López-García MT, Pérez-Redondo R, Koekman B, Martín JF, Liras P. Connecting primary and secondary metabolism: AreB, an IclR-like protein, binds the ARE(ccaR) sequence of S. clavuligerus and modulates leucine biosynthesis and cephamycin C and clavulanic acid production. Mol Microbiol 2007; 66:511-24.
27. Aharonowitz Y, Mendelovitz S, Kirenberg F, Kuper V. Regulatory mutants of Streptomyces clavuligerus affected in free diaminopimelic acid content and antibiotic biosynthesis. J Bacteriol 1984; 157:337-40.
28. Nüesch J, Heim J, Treichler HJ. The biosynthesis of sulfur-containing β-lactam antibiotics. Ann Rev Microbiol 1987; 41:51-75.
29. Martin JF. New aspects of genes and enzymes for β-lactam antibiotic biosynthesis. Appl Microbiol Biotechnol 1998; 50:1-15.
30. Öster LM, Lester DR, van Scheltinga AT, Svenda M, van Lun M, Généreux C, et al. Insights into cephamycin biosynthesis: the crystal structure of CmcI from Streptomyces clavuligerus. J Mol Biol 2006; 358:546-58.
31. Kieser T, Bibb MJ, Buttner MJ, Chater KF, Hopwood DA. Practical Streptomyces Genetics. Norwich: The John Innes Foundation 2000.
32. Higgins CE, Kastner RE. Streptomyces clavuligerus sp. nov., a β-lactam antibiotic producer. Int J Syst Bacteriol 1971; 21:326-31.
33. nd ed. New York: Cold Spring Harbor Laboratory Press 1989.
34. Follettie MT, Peoples OP, Agoropoulou C, Sinskey AJ. Gene structure and expression of the Corynebacterium flavum N13 ask-asd operon. J Bacteriol 1993; 175:4096-103.
35. Burton K. Determination of DNA concentration with diphenylamine. In: Grossman L, Moldave K, eds. Methods in Enzymology Vol. 12B. New York: Academic Press 1968; 163-6.