Naoko Imokawa

Naoko Imokawa

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Appl Environ Microbiol

v.76(17); 2010 Sep

PMC2935060

Appl Environ Microbiol. 2010 Sep; 76(17): 5669–5675.
Published online 2010 Jul 2. doi: 10.1128/AEM.00853-10
Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan, 1 Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan 2
* Corresponding author. Mailing address: Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Fukui 910-1195, Japan. Phone: 81 776 61 6000. Fax: 81 776 61 6015. E-mail: pj.ca.upf@onamah
Received 2010 Apr 8; Accepted 2010 Jun 19.
Copyright © 2010, American Society for Microbiology
This article has been cited by other articles in PMC.
a Tsp r , thiostrepton resistant; Apm r , apramycin resistant; Tet r , tetracycline resistant; Neo r , neomycin resistant.
1. Bagnara, A. S., and Finch, L. R. 1972. Quantitative extraction and estimation of intracellular nucleoside triphosphates of Escherichia coli . Anal. Biochem. 45 : 24-34. [ PubMed ] [ Google Scholar ]
2. Hamano, Y., T. Dairi, M. Yamamoto, T. Kuzuyama, N. Itoh, and H. Seto. 2002. Growth-phase dependent expression of the mevalonate pathway in a terpenoid antibiotic-producing Streptomyces strain. Biosci. Biotechnol. Biochem. 66 : 808-819. [ PubMed ] [ Google Scholar ]
3. Hamano, Y., I. Nicchu, Y. Hoshino, T. Kawai, S. Nakamori, and H. Takagi. 2005. Development of gene delivery systems for the ɛ-poly-L-lysine producer, Streptomyces albulus . J. Biosci. Bioeng. 99 : 636-641. [ PubMed ] [ Google Scholar ]
4. Hamano, Y., C. Maruyama, and H. Kimoto. 2006. Construction of a knockout mutant of the streptothricin-resistance gene in Streptomyces albulus by electroporation. Actinomycetologica 20 : 35-41. [ Google Scholar ]
5. Hamano, Y., T. Yoshida, M. Kito, S. Nakamori, T. Nagasawa, and H. Takagi. 2006. Biological function of the pld gene product that degrades ɛ-poly-l-lysine in Streptomyces albulus . Appl. Microbiol. Biotechnol. 72 : 173-181. [ PubMed ] [ Google Scholar ]
6. Hamano, Y., I. Nicchu, T. Shimizu, Y. Onji, J. Hiraki, and H. Takagi. 2007. ɛ-Poly-l-lysine producer, Streptomyces albulus , has feedback-inhibition resistant aspartokinase. Appl. Microbiol. Biotechnol. 76 : 873-882. [ PubMed ] [ Google Scholar ]
7. Hiraki, J., M. Hatakeyama, H. Morita, and Y. Izumi. 1998. Improved ɛ-poly-l-lysine production of an S-(2-aminoethyl)-l-cysteine resistant mutant of Streptomyces albulus . Seibutu Kougaku Kaishi 76 : 487-493. (In Japanese.) [ Google Scholar ]
8. Itzhaki, R. F. 1972. Colorimetric method for estimating polylysine and polyarginine. Anal. Biochem. 50 : 569-574. [ PubMed ] [ Google Scholar ]
9. Kahar, P., T. Iwata, J. Hiraki, E. Y. Park, and M. Okabe. 2001. Enhancement of ɛ-polylysine production by Streptomyces albulus strain 410 using pH control. J. Biosci. Bioeng. 91 : 190-194. [ PubMed ] [ Google Scholar ]
10. Kito, M., R. Takimoto, T. Yoshida, and T. Nagasawa. 2002. Purification and characterization of an ɛ-poly-l-lysine-degrading enzyme from an ɛ-poly-l-lysine-producing strain of Streptomyces albulus . Arch. Microbiol. 178 : 325-330. [ PubMed ] [ Google Scholar ]
11. Marahiel, M. A., T. Stachelhaus, and H. D. Mootz. 1997. Modular peptide synthases involved in nonribosomal peptide synthesis. Chem. Rev. 97 : 2651-2673. [ PubMed ] [ Google Scholar ]
12. Mootz, H. D., D. Schwarzer, and M. A. Marahiel. 2002. Ways of assembling complex natural products on modular nonribosomal peptide synthetases. Chembiochem 3 : 490-504. [ PubMed ] [ Google Scholar ]
13. Oppermann-Sanio, F. B., and A. Steinbüchel. 2002. Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production. Naturwissenschaften 89 : 11-22. [ PubMed ] [ Google Scholar ]
14. Sambrook, J., and D. W. Russell. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
15. Schwarzer, D., R. Finking, and M. A. Marahiel. 2003. Nonribosomal peptides: from genes to products. Nat. Prod. Rep. 20 : 275-287. [ PubMed ] [ Google Scholar ]
16. Shima, S., and H. Sakai. 1977. Polylysine produced by Streptomyces . Agric. Biol. Chem. 41 : 1807-1809. [ Google Scholar ]
17. Shima, S., and H. Sakai. 1981. Poly-l-lysine produced by Streptomyces . II. Taxonomy and fermentation studies. Agric. Biol. Chem. 45 : 2497-2502. [ Google Scholar ]
18. Shima, S., and H. Sakai. 1981. Poly-l-lysine produced by Streptomyces . III. Chemical studies. Agric. Biol. Chem. 45 : 2503-2508. [ Google Scholar ]
19. Shima, S., S. Oshima, and H. Sakai. 1983. Biosynthesis of ɛ-poly-l-lysine by washed mycelium of Streptomyces albulus no. 346. Nippon Nogeikagaku Kaishi 57 : 221-226. [ Google Scholar ]
20. Shima, S., H. Matsuoka, T. Iwamoto, and H. Sakai. 1984. Antimicrobial action of ɛ-poly-l-lysine. J. Antibiot. (Tokyo) 37 : 1449-1455. [ PubMed ] [ Google Scholar ]
21. Walsh, C. 2003. Antibiotics: action, origins, resistance. ASM Press, Washington, DC.
22. Yamanaka, K., C. Maruyama, H. Takagi, and Y. Hamano. 2008. Epsilon-poly-l-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase. Nat. Chem. Biol. 4 : 766-772. [ PubMed ] [ Google Scholar ]
Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)
13. Oppermann-Sanio, F. B., and A. Steinbüchel. 2002. Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production. Naturwissenschaften 89 : 11-22. [ PubMed ] [ Google Scholar ] [ Ref list ]
16. Shima, S., and H. Sakai. 1977. Polylysine produced by Streptomyces . Agric. Biol. Chem. 41 : 1807-1809. [ Google Scholar ] [ Ref list ]
20. Shima, S., H. Matsuoka, T. Iwamoto, and H. Sakai. 1984. Antimicrobial action of ɛ-poly-l-lysine. J. Antibiot. (Tokyo) 37 : 1449-1455. [ PubMed ] [ Google Scholar ] [ Ref list ]
7. Hiraki, J., M. Hatakeyama, H. Morita, and Y. Izumi. 1998. Improved ɛ-poly-l-lysine production of an S-(2-aminoethyl)-l-cysteine resistant mutant of Streptomyces albulus . Seibutu Kougaku Kaishi 76 : 487-493. (In Japanese.) [ Google Scholar ] [ Ref list ]
22. Yamanaka, K., C. Maruyama, H. Takagi, and Y. Hamano. 2008. Epsilon-poly-l-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase. Nat. Chem. Biol. 4 : 766-772. [ PubMed ] [ Google Scholar ] [ Ref list ]
11. Marahiel, M. A., T. Stachelhaus, and H. D. Mootz. 1997. Modular peptide synthases involved in nonribosomal peptide synthesis. Chem. Rev. 97 : 2651-2673. [ PubMed ] [ Google Scholar ] [ Ref list ]
12. Mootz, H. D., D. Schwarzer, and M. A. Marahiel. 2002. Ways of assembling complex natural products on modular nonribosomal peptide synthetases. Chembiochem 3 : 490-504. [ PubMed ] [ Google Scholar ] [ Ref list ]
15. Schwarzer, D., R. Finking, and M. A. Marahiel. 2003. Nonribosomal peptides: from genes to products. Nat. Prod. Rep. 20 : 275-287. [ PubMed ] [ Google Scholar ] [ Ref list ]
21. Walsh, C. 2003. Antibiotics: action, origins, resistance. ASM Press, Washington, DC. [ Ref list ]
9. Kahar, P., T. Iwata, J. Hiraki, E. Y. Park, and M. Okabe. 2001. Enhancement of ɛ-polylysine production by Streptomyces albulus strain 410 using pH control. J. Biosci. Bioeng. 91 : 190-194. [ PubMed ] [ Google Scholar ] [ Ref list ]
10. Kito, M., R. Takimoto, T. Yoshida, and T. Nagasawa. 2002. Purification and characterization of an ɛ-poly-l-lysine-degrading enzyme from an ɛ-poly-l-lysine-producing strain of Streptomyces albulus . Arch. Microbiol. 178 : 325-330. [ PubMed ] [ Google Scholar ] [ Ref list ]
5. Hamano, Y., T. Yoshida, M. Kito, S. Nakamori, T. Nagasawa, and H. Takagi. 2006. Biological function of the pld gene product that degrades ɛ-poly-l-lysine in Streptomyces albulus . Appl. Microbiol. Biotechnol. 72 : 173-181. [ PubMed ] [ Google Scholar ] [ Ref list ]
3. Hamano, Y., I. Nicchu, Y. Hoshino, T. Kawai, S. Nakamori, and H. Takagi. 2005. Development of gene delivery systems for the ɛ-poly-L-lysine producer, Streptomyces albulus . J. Biosci. Bioeng. 99 : 636-641. [ PubMed ] [ Google Scholar ] [ Ref list ]
14. Sambrook, J., and D. W. Russell. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. [ Ref list ]
4. Hamano, Y., C. Maruyama, and H. Kimoto. 2006. Construction of a knockout mutant of the streptothricin-resistance gene in Streptomyces albulus by electroporation. Actinomycetologica 20 : 35-41. [ Google Scholar ] [ Ref list ]
6. Hamano, Y., I. Nicchu, T. Shimizu, Y. Onji, J. Hiraki, and H. Takagi. 2007. ɛ-Poly-l-lysine producer, Streptomyces albulus , has feedback-inhibition resistant aspartokinase. Appl. Microbiol. Biotechnol. 76 : 873-882. [ PubMed ] [ Google Scholar ] [ Ref list ]
8. Itzhaki, R. F. 1972. Colorimetric method for estimating polylysine and polyarginine. Anal. Biochem. 50 : 569-574. [ PubMed ] [ Google Scholar ] [ Ref list ]
2. Hamano, Y., T. Dairi, M. Yamamoto, T. Kuzuyama, N. Itoh, and H. Seto. 2002. Growth-phase dependent expression of the mevalonate pathway in a terpenoid antibiotic-producing Streptomyces strain. Biosci. Biotechnol. Biochem. 66 : 808-819. [ PubMed ] [ Google Scholar ] [ Ref list ]
1. Bagnara, A. S., and Finch, L. R. 1972. Quantitative extraction and estimation of intracellular nucleoside triphosphates of Escherichia coli . Anal. Biochem. 45 : 24-34. [ PubMed ] [ Google Scholar ] [ Ref list ]

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Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan, 1 Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan 2
Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan, 1 Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan 2
Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan, 1 Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan 2
Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan, 1 Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan 2
Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan, 1 Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan 2
Yokohama Research Center, Chisso Corporation, 5-1 Ookawa, Kanazawa-Ku, Yokohama 236-8605, Japan, 1 Department of Bioscience, Fukui Prefectural University, 4-1-1 Matsuoka-Kenjojima, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan 2
ɛ-Poly- l -lysine (ɛ-PL) is produced by Streptomyces albulus NBRC14147 as a secondary metabolite and can be detected only when the fermentation broth has an acidic pH during the stationary growth phase. Since strain NBRC14147 produces ɛ-PL-degrading enzymes, the original chain length of the ɛ-PL polymer product synthesized by ɛ-PL synthetase (Pls) is unclear. Here, we report on the identification of the gene encoding the ɛ-PL-degrading enzyme (PldII), which plays a central role in ɛ-PL degradation in this strain. A knockout mutant of the pldII gene was found to produce an ɛ-PL of unchanged polymer chain length, demonstrating that the length is not determined by ɛ-PL-degrading enzymes but rather by Pls itself and that the 25 to 35 l -lysine residues of ɛ-PL represent the original chain length of the polymer product synthesized by Pls in vivo . Transcriptional analysis of pls and a kinetic study of Pls further suggested that the Pls catalytic function is regulated by intracellular ATP, high levels of which are required for full enzymatic activity. Furthermore, it was found that acidic pH conditions during ɛ-PL fermentation, rather than the inhibition of the ɛ-PL-degrading enzyme, are necessary for the accumulation of intracellular ATP.
Two amino acid homopolymers comprising a single type of amino acid are known in nature ( 13 ): poly-γ-glutamic acid (γ-PGA) and ɛ-poly- l -lysine (ɛ-PL). The latter consists of 25 to 35 l -lysine residues with linkages between α-carboxyl groups and ɛ-amino groups (Fig. (Fig.1). 1 ). ɛ-PL exhibits antimicrobial activity against a spectrum of microorganisms including bacteria and fungi ( 16 - 20 ). Because of its high levels of safety and biodegradability ( 7 ), ɛ-PL is used as a food preservative in several countries.
The biological activity of ɛ-PL is dependent on its molecular size. Shima and coworkers investigated this relationship in Escherichia coli K-12 ( 20 ) and showed that ɛ-PL with more than nine l -lysine residues severely inhibited microbial growth; however, the l -lysine octamer demonstrated negligible antimicrobial activity. In contrast, chemically synthesized α-poly- l -lysine with a chain of 50 l -lysine residues and linkages between the α-carboxyl and α-amino groups demonstrated a lower level of activity than ɛ-PL. Thus, polymerization of l -lysine via an isopeptide bond is required to exert its biological activity, and the polymerization mechanisms involved in the chain length and the diversity of ɛ-PL are of particular interest.
We recently reported on the purification of an ɛ-PL synthetase (Pls) and the cloning of its gene (accession number {"type":"entrez-nucleotide","attrs":{"text":"AB385841","term_id":"197116282"}} AB385841 ) from Streptomyces albulus NBRC14147, which is an ɛ-PL-producing strain ( 22 ). Pls was found to be a membrane protein with adenylation and thiolation domains characteristic of the nonribosomal peptide synthetases (NRPSs) ( 11 , 12 , 15 , 21 ). In vitro , Pls produced ɛ-PL with chain lengths ranging from 3 to 17 residues, demonstrating that the chain length diversity of ɛ-PL is directly generated by the synthetase rather than via the differential degradation of a uniform polymer by ɛ-PL-degrading enzymes ( 22 ). However, in vivo , it is still unclear whether the 25 to 35 l -lysine residues of ɛ-PL represent the original chain length of the polymer product synthesized by Pls as strain NBRC14147 produces ɛ-PL-degrading enzymes ( 9 ).
During ɛ-PL fermentation, its production and accumulation are detected when the pH value of the fermentation broth decreases from approximately 7.0 to the self-stabilized final value of approximately 3.2 ( 9 ). After fermentation is complete, ɛ-PL is enzymatically degraded by increasing the pH value to approximately 7.0 ( 9 ). Such degradation is also observed using washed mycelium at pH 7.0. In fact, Kito and coworkers successfully purified the ɛ-PL-degrading enzyme Pld from S. albulus ( 10 ). Pld was classified as a type of Zn 2+ -containing aminopeptidase that is tightly bound to the cell membrane and that releases amino (N)-terminal l -lysines one at a time; the mode of ɛ-PL degradation with Pld is an exo-type action. Its highest activity was observed at pH 7.0, which was in good agreement with the observation that the ɛ-PL produced was degraded at a neutral pH
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