In vitro catalytic activity of N-terminal and C-terminal domains in NukM, the post-translational modification enzyme of nukacin ISK-1

Journal of Bioscience and Bioengineering

Volumn 120, Issue 6, 2015, Pages 624-629

  Shimafuji, Chinatsu ^a   Noguchi, Megumi ^a   Nishie, Mami ^a   Nagao, Jun Ichi ^b   Shioya, Kouki ^a   Zendo, Takeshi ^a   Nakayama, Jiro ^a   Sonomoto, Kenji ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b FUKUOKA DENTAL COLLEGE   (Japan)

Author keywords

Lantibiotic; Modification enzyme; Nukacin ISK 1; Peptide engineering; Unusual amino acids

Indexed keywords

AMINO ACIDS; CYCLIZATION; DEHYDRATION; ENZYMES; PEPTIDES; PHOSPHORYLATION; PLANTS (BOTANY); PROTEINS; SURFACE PLASMON RESONANCE;

ANTIBACTERIAL PEPTIDES; CYCLIZATION REACTIONS; INVITRO RECONSTITUTION; LANTIBIOTICS; N-AND C-TERMINAL DOMAINS; NUKACIN ISK-1; PEPTIDE ENGINEERINGS; SUBSTRATE RECOGNITION;

CATALYST ACTIVITY;

BACTERIAL ENZYME; LANTIBIOTIC; NUKACIN ISK 1; UNCLASSIFIED DRUG; ALANINE; BACTERIOCIN; ENZYME; LANTHIONINE; NISIN; NUKACIN ISK-1; PROTEIN BINDING; SULFIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CYCLIZATION; ENZYME STRUCTURE; GENE OVEREXPRESSION; IN VITRO STUDY; MOLECULAR BIOLOGY; NONHUMAN; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; SURFACE PLASMON RESONANCE; ANALOGS AND DERIVATIVES; BIOCATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; METABOLISM; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE; STAPHYLOCOCCUS;

ALANINE; BACTERIOCINS; BIOCATALYSIS; CYCLIZATION; ENZYMES; NISIN; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; STAPHYLOCOCCUS; SUBSTRATE SPECIFICITY; SULFIDES;

EID: 84946471932     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2015.03.020     Document Type: Article

References (27)

1. Nagao J., Asaduzzaman S.M., Aso Y., Okuda K., Nakayama J., Sonomoto K. Lantibiotics: insight and foresight for new paradigm. J. Biosci. Bioeng. 2006, 102:139-149.
2. Rea M.C., Ross R.P., Cotter P.D., Hill C. Classification of bacteriocins from gram-positive bacteria. Prokaryotic antimicrobial peptides, genes to applications 2011, 29-54. Springer, Berlin. D. Drider, S. Rebuffat (Eds.).
3. Patton G.C., van der Donk W.A. New developments in lantibiotic biosynthesis and mode of action. Curr. Opin. Microbiol. 2005, 8:543-551.
4. Khusainov R., Moll G.N., Kuipers O.P. Identification of distinct nisin leader peptide regions that determine interactions with the modification enzymes NisB and NisC. FEBS Open Bio 2013, 3:237-242.
5. van der Meer J.R., Roleema H.S., Siezen R.J., Beerthiyzen M.M., Kuipers O.P., de Vos W.M. Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis. J. Biol. Chem. 1994, 269:3555-3562.
6. Bierbaum G., Sahl H.G. Lantibiotics: mode of action, biosynthesis and Bioengineering. Curr. Pharm. Biotechnol. 2009, 10:2-18.
7. Nagao J., Morinaga Y., Islam M.R., Asaduzzaman S.M., Aso Y., Nakayama J., Sonomoto K. Mapping and identification of the region and secondary structure required for the maturation of the nukacin ISK-1 prepeptide. Peptides 2009, 30:1412-1420.
8. Patton G.C., Paul M., Cooper L.E., Chatterjee C., van der Donk W.A. The importance of the leader sequence for directing lanthionine formation in lacticin 481. Biochemistry 2008, 47:7342-7351.
9. Levengood M.R., Patton G.C., van der Donk W.A. The leader peptide is not required for post-translational modification by lacticin 481 synthetase. J. Am. Chem. Soc. 2007, 129:10314-10315.
10. Uguen P., Le Pennec J.P., Dufour A. Lantibiotic biosynthesis: interactions between prelacticin 481 and its putative modification enzyme, LctM. J. Bacteriol. 2000, 182:5262-5266.
11. You Y.O., van der Donk W.A. Mechanistic investigations of the dehydration reaction of lacticin 481 synthetase. Biochemistry 2007, 46:5991-6000.
12. Paul M., Patton G.C., van der Donk W.A. Mutants of the zinc ligands of lacticin 481 synthetase retain dehydration activity but have impaired cyclization activity. Biochemistry 2007, 46:6268-6276.
13. Levengood M.R., Knerr P.J., Oman T.J., van der Donk W.A. In vitro mutasynthesis of lantibiotic analogues containing nonproteinogenic amino acids. J. Am. Chem. Soc. 2009, 131:12024-12025.
14. Levengood M.R., Kerwood C.C., Chatterjee C., van der Donk W.A. Investigation of the substrate specificity of lacticin 481 synthetase by using nonproteinogenic amino acids. Chembiochem. 2009, 10:911-919.
15. You Y.O., Levengood M.R., Ihnken L.A.F., Knowlton A.K., van der Donk W.A. Lacticin 481 synthetase as a general serine/threonine kinase. ACS Chem. Biol. 2009, 4:379-385.
16. Sashihara T., Kimura H., Higuchi T., Adachi A., Matsusaki H., Sonomoto K., Ishizaki A. A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1: cloning of the structural gene and identification of the structure. Biosci. Biotechnol. Biochem. 2000, 64:2420-2428.
17. Aso Y., Sashihara T., Nagao J., Kanemasa Y., Koga H., Hashimoto T., Higuchi T., Adachi A., Nomiyama H., Ishizaki A., Nakayama J., Sonomoto K. Characterization of a gene cluster of Staphylococcus warneri ISK-1 encoding the biosynthesis of and immunity to the lantibiotic, nukacin ISK-1. Biosci. Biotechnol. Biochem. 2004, 68:1663-1671.
18. Sambrook J., Russel D.W. Molecular cloning: a laboratory manual 2001, Cold Spring Harbour Laboratory, Cold Spring Harbour, NY. 3rd ed.
19. Nagao J., Harada Y., Shioya K., Aso Y., Zendo T., Nakayama J., Sonomoto K. Lanthionine introduction into nukacin ISK-1 prepeptide by co-expression with modification enzyme NukM in Escherichia coli. Biochem. Biophys. Res. Commun. 2005, 336:507-513.
20. Aso Y., Okuda K., Nagao J., Kanemasa Y., Phuong N.T.B., Koga H., Shioya K., Sashihara T., Nakayama J., Sonomoto K. A novel type of immunity protein, NukH, for the lantibiotic nukacin ISK-1 produced by Staphylococcus warneri ISK-1. Biosci. Biotechnol. Biochem. 2005, 69:1403-1410.
21. Shioya K., Harada Y., Nagao J., Nakayama J., Sonomoto K. Characterization of modification enzyme NukM and engineering of a novel thioether bridge in lantibiotic nukacin ISK-1. Appl. Microbiol. Biothechnol. 2010, 86:891-899.
22. Chatterjee C., Miller L.M., Leung Y.L., Xie L., Yi M., Kelleher N.L., van der Donk W.A. Lacticin 481 synthetase phosphorylates its substrate during lantibiotic production. J. Am. Chem. Soc. 2005, 127:15332-15333.
23. Li B., Yu J.P.J., Brunzelle J.S., Moll G.N., van der Donk W.A., Nair S.K. Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis. Science 2006, 311:1464-1467.
24. Rink R., Kluskens L.D., Kuipers A., Driessen A.J.M., Kuipers O.P., Moll G.N. NisC, the cyclase of the lantibiotic nisin, can catalyze cyclization of designed nonlantibiotic peptides. Biochemistry 2007, 46:13179-13189.
25. Mavaro A., Abts A., Bakkes P.J., Moll G.N., Driessen A.J.M., Smits S.H.J., Schmitt L. Substrate recognition and specificity of the NisB protein, the lantibiotic dehydratase involved in nisin biosynthesis. J. Biol. Chem. 2011, 286:30552-30560.
26. Kuipers A., de Boef E., Rink R., Fekken S., Kluskens L.D., Driessen A.J.M., Leenhouts K., Kuipers O.P., Moll G.N. NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides. J. Biol. Chem. 2004, 279:22176-22182.
27. van den Berg van Saparoea H.B., Bakkes P.J., Moll G.N., Driessen A.J.M. Distinct contributions nisin biosynthesis enzymes NisB and NisC transporter NisT prenisin production by Lactococcus lactis. Appl. Environ. Microbiol. 2008, 74:5541-5548.