Genetic design of conditional d-glutamate auxotrophy for Bacillus subtilis: Use of a vector-borne poly-γ-glutamate synthetic system

Biochemical and Biophysical Research Communications

Volumn 362, Issue 3, 2007, Pages 646-650

  Ashiuchi, Makoto ^a   Nishikawa, Yoshito ^a   Matsunaga, Ken'ichiro ^a   Yamamoto, Masayoshi ^a   Shimanouchi, Kazuya ^a   Misono, Haruo ^a  

^a KOCHI UNIVERSITY   (Japan)

Author keywords

Bacillus subtilis; d Glutamate; Genetic design; Glutamate racemase; Poly glutamate

Indexed keywords

DEXTRO GLUTAMIC ACID; POLYGLUTAMIC ACID;

ARTICLE; AUXOTROPHY; BACILLUS SUBTILIS; BACTERIAL GROWTH; BIOSYNTHESIS; CARBOHYDRATE SYNTHESIS; CONTROLLED STUDY; GENE INDUCTION; GENETICS; GROWTH INHIBITION; IN VIVO STUDY; LIQUID CULTURE; MUTANT; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; VECTORCARDIOGRAPHY;

BACILLUS SUBTILIS; BIOCHEMISTRY; GENE EXPRESSION REGULATION, BACTERIAL; GENES, BACTERIAL; GENETIC TECHNIQUES; GENETIC VECTORS; GENOME, BACTERIAL; GLUTAMIC ACID; MODELS, GENETIC; MUTATION; PHENOTYPE; POLYGLUTAMIC ACID; TRANSGENES;

BACILLUS SUBTILIS;

EID: 34548409520     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.08.019     Document Type: Article

References (27)

1. Ashiuchi M., Tani T., Soda K., and Misono H. Properties of glutamate racemase from Bacillus subtilis IFO 3336 producing poly-γ-glutamate. J. Biochem. (Tokyo) 123 (1998) 1156-1163
2. Ashiuchi M., and Misono H. Poly-γ-glutamic acid. In: Fahnestock S.R., and Steinbüchel A. (Eds). Biopolymers vol. 7 (2002), Wiley-VCH, Weinheim 123-174
3. Mengin-lecreulx D., Flouret B., and van Heijenoort J. Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 151 (1982) 1109-1117
4. Dougherty T.J., Thanassi J.A., and Pucci M.J. The Escherichia coli mutant requiring d-glutamic acid is the result of mutations in two distinct genetic loci. J. Bacteriol. 175 (1993) 111-116
5. Yoshimura T., Ashiuchi M., Esaki N., Kobatake C., Choi S.-Y., and Soda K. Expression of glr (murI, dga) gene encoding glutamate racemase in Escherichia coli. J. Biol. Chem. 268 (1993) 24242-24246
6. Wu Q., Xu H., Xu L., and Ouyang P. Biosynthesis of poly(γ-glutamic acid) in Bacillus subtilis NX-2: regulation of stereochemical composition of poly(γ-glutamic acid). Process Biochem. 41 (2006) 1650-1655
7. Shimizu K., Nakamura H., and Ashiuchi M. Salt-inducible bionylon polymer from Bacillus megaterium. Appl. Environ. Microbiol. 73 (2007) 2378-2379
8. Kimura K., Tran L.-S., and Itoh Y. Roles and regulation of the glutamate racemase isogenes, racE and yrpC, in Bacillus subtilis. Microbiology 150 (2004) 2911-2920
9. Kada S., Nanamiya H., Kawamura F., and Horinouchi S. Glr, a glutamate racemase, supplies d-glutamate to both peptidoglycan synthesis and poly-γ-glutamate production in γ-PGA-producing Bacillus subtilis. FEMS Microbiol. Lett. 236 (2004) 13-20
10. Ashiuchi M., Kamei T., Baek D.-H., Shin S.-Y., Sung M.-H., Soda K., Yagi T., and Misono H. Isolation of Bacillus subtilis (chungkookjang), a poly-γ-glutamate producer with high genetic competence. Appl. Microbiol. Biotechnol. 57 (2001) 764-769
11. Ashiuchi M., Soda K., and Misono H. Characterization of yrpC gene product of Bacillus subtilis IFO 3336 as glutamate racemase isozyme. Biosci. Biotechnol. Biochem. 63 (1999) 792-798
12. Kobayashi K., Ehrlich S.D., Albertini A., Amati G., Andersen K.K., Arnaud M., Asai K., Ashikaga S., Aymerich S., Bessieres P., Boland F., Brignell S.C., Bron S., Bunai K., Chapuis J., Christiansen L.C., Danchin A., Debarbouille M., Dervyn E., Deuerling E., Devine K., Devine S.K., Dreesen O., Errington J., Fillinger S., Foster S.J., Fujita Y., Galizzi A., Gardan R., Eschevins C., Fukushima T., Haga K., Harwood C.R., Hecker M., Hosoya D., Hullo M.F., Kakeshita H., Karamata D., Kasahara Y., Kawamura F., Koga K., Koski P., Kuwana R., Imamura D., Ishimaru M., Ishikawa S., Ishio I., LeCoq D., Masson A., Mauel C., Meima R., Mellado R.P., Moir A., Moriya S., Nagakawa E., Nanamiya H., Nakai S., Nygaard P., Ogura M., Ohanan T., O'Reilly M., O'Rourke M., Pragai Z., Pooley H.M., Rapoport G., Rawlins J.P., Rivas L.A., Rivolta C., Sadaie A., Sadaie Y., Sarvas M., Sato T., Saxild H.H., Scanlan E., Schumann W., Seegers J.F., Sekiguchi J., Sekowska A., Seror S.J., Simon M., Stragier P., Studer R., Takamatsu H., Tanaka T., Takeuchi M., Thomaides H.B., Vagner V., van Dijl J.M., Watabe K., Wipat A., Yamamoto H., Yamamoto M., Yamamoto Y., Yamane K., Yata K., Yoshida K., Yoshikawa H., Zuber U., and Ogasawara N. Essential Bacillus subtilis genes. Proc. Natl. Acad. Sci. USA 100 (2003) 4678-4683
13. Bhavsar A.P., Zhao X., and Brown E.D. Development and characterization of a xylose-dependent system for expression of cloned genes in Bacillus subtilis: conditional complementation of a teichoic acid mutant. Appl. Environ. Microbiol. 67 (2001) 403-410
14. Yoshimoto T., Oyama H., Honda T., Tone H., Takeshita T., Kamiyama T., and Tsuru D. Cloning and expression of subtilisin amylosacchariticus gene. J. Biochem. (Tokyo) 103 (1988) 1060-1065
15. Ashiuchi M., Shimanouchi K., Horiuchi T., Kamei T., and Misono H. Genetically engineered poly-γ-glutamate producer from Bacillus subtilis ISW1214. Biosci. Biotechnol. Biochem. 70 (2006) 1794-1797
16. Ashiuchi M., Nawa C., Kamei T., Song J.-J., Hong S.-P., Sung M.-H., Soda K., and Misono H. Physiological and biochemical characteristics of poly γ-glutamate synthetase complex of Bacillus subtilis. Eur. J. Biochem. 268 (2001) 5321-5328
17. Anagostopoulos C., and Spizizen J. Requirement for transformation in Bacillus subtilis. J. Bacteriol. 81 (1961) 741-746
18. Jiang H., Shang L., Yoon S.H., Lee S.Y., and Yu Z. Optimal production of Poly-μ-glutamic acid by metabolically engineered Escherichia coli. Biotechnol. Lett. 28 (2006) 1241-1246
19. Krispin O., and Alimansberger R. The Bacillus subtilis AraE protein displays a broad substrate specificity for several different sugars. J. Bacteriol. 180 (1998) 3250-3252
20. Lundqvist T., Fisher S.L., Kern G., Folmer R.H.A., Xue Y., Newton D.T., Keating T.A., Alm R.A., and de Jonge B.L.M. Exploitation of structural and regulatory diversity in glutamate racemases. Nature 447 (2007) 817-822
21. Ashiuchi M., Shimanouchi K., Nakamura H., Kamei T., Soda K., Park C., Sung M.-H., and Misono H. Enzymatic synthesis of high-molecular-mass poly-γ-glutamate and regulation of its stereochemistry. Appl. Environ. Microbiol. 70 (2004) 4249-4255
22. Candela T., and Fouet A. Poly-γ-glutamate in bacteria. Mol. Microbiol. 60 (2006) 1091-1098
23. Kocianova S., Vuong C., Yao Y., Voyich J.M., Fischer E.R., DeLeo F.R., and Otto M. Key role of poly-γ-dl-glutamic acid in immune evasion and virulence of Staphylococcus epidermidis. J. Clin. Invest. 115 (2005) 688-694
24. Eveland S.S., Pompliano D.L., and Anderson M.S. Conditionally lethal Escherichia coli murein mutants contain point defects that map tp regions conserved among murein and folyl poly-γ-glutamate ligases: identification of a ligase superfamily. Biochemistry 36 (1997) 6223-6229
25. Kleinkauf H., and von Döhren H. A nonribosomal system of peptide biosynthesis. Eur. J. Biochem. 236 (1996) 335-351
26. Nishizawa T., Asayama M., and Shirai M. Cyclic heptapeptide microcystin biosynthesis requires the glutamate racemase gene. Microbiology 147 (2001) 1235-1241
27. Sielaff H., Dittann E., de Marsac N.T., Bouchier C., von Dören H., Börner T., and Schwecke T. The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase. Biochem. J. 373 (2003) 909-916