Amylocyclicin, a novel circular bacteriocin produced by Bacillus amyloliquefaciens FZB42

Journal of Bacteriology

Volumn 196, Issue 10, 2014, Pages 1842-1852

  Scholz, Romy ^a   Vater, Joachim ^b   Budiharjo, Anto ^a,f   Wang, Zhiyuan ^a,c   He, Yueqiu ^c   Dietel, Kristin ^d   Schwecke, Torsten ^e   Herfort, Stefanie ^e   Lasch, Peter ^e   Borriss, Rainer ^a,d  

^a HUMBOLDT UNIVERSITY   (Germany)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^c YUNNAN AGRICULTURAL UNIVERSITY   (China)

^d ABITEP GMBH   (Germany)

^e ROBERT KOCH INSTITUTE   (Germany)

^f DIPONEGORO UNIVERSITY   (Indonesia)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOCYCLICIN; BACTERIOCIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SIGW; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANTIBACTERIAL ACTIVITY; ARTICLE; BACILLUS AMYLOLIQUEFACIENS; BACILLUS SUBTILIS; BACTERIAL GENE; BACTERIAL IMMUNITY; BACTERIAL STRAIN; BIOSYNTHESIS; CONTROLLED STUDY; GENE CLUSTER; GRAM POSITIVE BACTERIUM; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; MUTAGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; PAENIBACILLUS; PHYLOGENETIC TREE; PRIORITY JOURNAL; PROTEIN PROCESSING; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; TAXON; TRANSPOSON; YDBST GENE;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BACILLUS; BACTERIOCINS; BACTERIOLOGICAL TECHNIQUES; GENE EXPRESSION REGULATION, BACTERIAL; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIA; MUTATION;

EID: 84898879456     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01474-14     Document Type: Article

References (42)

1. Chen XH, Koumoutsi A, Scholz R, Borriss R. 2009. More than anticipated- production of antibiotics and other secondary metabolites by FZB42. J. Mol. Microbiol. Biotechnol. 16:14-24. http://dx.doi.org/10.1159/000142891.
2. Chen XH, Vater J, Piel J, Franke P, Scholz R, Schneider K, Koumoutsi A, Hitzeroth G, Grammel N, Strittmatter AW, Gottschalk G, Süssmuth RD, Borriss R. 2006. Structural and functional characterization of three polyketide synthase gene clusters in Bacillus amyloliquefaciens FZB 42. J. Bacteriol. 188:4024-4036. http://dx.doi.org/10.1128/JB.00052-06.
3. Schneider K, Chen XH, Vater J, Franke P, Nicholson G, Borriss R, Süssmuth RD. 2007. Macrolactin is the polyketide biosynthesis product of the pks2 cluster of Bacillus amyloliquefaciens FZB42. J. Nat. Prod. 70: 1417-1423. http://dx.doi.org/10.1021/np070070k.
4. Koumoutsi A, Chen XH, Henne A, Liesegang H, Hitzeroth G, Franke P, Vater J, Borriss R. 2004. Structural and functional characterization of gene clusters directing nonribosomal synthesis of bioactive cyclic lipopeptides in Bacillus amyloliquefaciens strain FZB42. J. Bacteriol. 186:1084-1096. http://dx.doi.org/10.1128/JB.186.4.1084-1096.2004.
5. Chen XH, Koumoutsi A, Scholz R, Eisenreich A, Schneider K, Heinemeyer I, Morgenstern B, Voss B, Hess WR, Reva O, Junge H, Voigt B, Jungblut PR, Vater J, Süssmuth R, Liesegang H, Strittmatter A, Gottschalk G, Borriss R. 2007. Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42. Nat. Biotechnol. 25:1007-1014. http://dx.doi.org/10.1038/nbt1325.
6. Chen XH, Scholz R, Borriss M, Junge H, Mogel G, Kunz S, Borriss R. 2009. Difficidin and bacilysin produced by plant-associated Bacillus amyloliquefaciens are efficient in controlling fire blight disease. J. Biotechnol. 140:38-44. http://dx.doi.org/10.1016/j.jbiotec.2008.10.015.
7. Chen XH, Koumoutsi A, Scholz R, Schneider K, Vater J, Süssmuth RD, Piel J, Borriss R. 2009. Genome analysis of Bacillus amyloliquefaciens FZB42 reveals its potential for biocontrol of plant pathogens. J. Biotechnol. 140:27-37. http://dx.doi.org/10.1016/j.jbiotec.2008.10.011.
8. Butcher BG, Helmann JD. 2006. Identification of Bacillus subtilis sigmadependent genes that provide intrinsic resistance to antimicrobial compounds produced by bacilli. Mol. Microbiol. 60:765-782. http://dx.doi.org/10.1111/j.1365-2958.2006.05131.x.
9. Scholz R, Molohon KJ, Nachtigall J, Vater J, Markley AL, Süssmuth RD, Mitchell DA, Borriss R. 2011. Plantazolicin, a novel microcin B17/streptolysin S-like natural product from Bacillus amyloliquefaciens FZB42. J. Bacteriol. 193:215-224. http://dx.doi.org/10.1128/JB.00784-10.
10. Haft DH, Basu MK, Mitchell DA. 2010. Expansion of ribosomally produced natural products: a nitrile hydratase-and Nif11-related precursor family. BMC Biol. 8:70. http://dx.doi.org/10.1186/1741-7007-8-70.
11. Lee SW, Mitchell DA, Markley AL, Hensler ME, Gonzalez D, Wohlrab A, Dorrestein PC, Nizet V, Dixon JE. 2008. Discovery of a widely distributed toxin biosynthetic gene cluster. Proc. Natl. Acad. Sci. U. S. A. 105:5879-5884. http://dx.doi.org/10.1073/pnas.0801338105.
12. Kalyon B, Helaly SE, Scholz R, Nachtigall J, Vater J, Borriss R, Süssmuth RD. 2011. Plantazolicin A and B: structure elucidation of ribosomally synthesized thiazole/oxazole peptides from Bacillus amyloliquefaciens FZB42. Org. Lett. 13:2996-2999. http://dx.doi.org/10.1021/ol200809m.
13. Molohon KJ, Melby JO, Lee J, Evans BS, Dunbar KL, Bumpus SB, Kelleher NL, Mitchell DA. 2011. Structure determination and interception of biosynthetic intermediates for the plantazolicin class of highly discriminating antibiotics. ACS Chem. Biol. 16:1307-1313. http://dx.doi.org/10.1021/cb200339d.
14. Liu Z, Budiharjo A, Wang P, Shi H, Fang J, Borriss R, Zhang K, Huang X. 2013. The highly modified microcin peptide plantazolicin is associated with nematicidal activity of Bacillus amyloliquefaciens FZB42. Appl. Microbiol. Biotechnol. 97:10081-10090. http://dx.doi.org/10.1007/s00253-013-5247-5.
15. Van Belkum MJ, Martin-Visscher LA, Vederas JC. 2011. Structure and genetics of circular bacteriocins. Trends Microbiol. 19:411-418. http://dx.doi.org/10.1016/j.tim.2011.04.004.
16. Kunst F, Rapoport G. 1995. Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis. J. Bacteriol. 177: 2403-2407.
17. Idris ESE, Iglesias DJ, Talon M, Borriss R. 2007. Tryptophan-dependent production of indole-3-acetic acid (IAA) affects level of plant growth promotion by Bacillus amyloliquefaciens FZB42. Mol. Plant Microbe Interact. 20:619-626. http://dx.doi.org/10.1094/MPMI-20-6-0619.
18. Horton RM, Cai ZL, Ho SN, Pease LR. 1990. Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction. Biotechniques 8:528-535.
19. Le Breton Y, Mohapatra NP, Haldenwang WG. 2006. In vivo random mutagenesis of Bacillus subtilis by use of TnYLB-1, a mariner-based transposon. Appl. Environ. Microbiol. 72:327-333. http://dx.doi.org/10.1128/AEM.72.1.327-333.2006.
20. Vater J, Kablitz B, Wilde C, Franke P, Mehta N, Cameotra SS. 2002. Matrix-assisted laser desorption ionization-time of flight mass spectrometry of lipopeptide biosurfactants in whole cells and culture filtrates of Bacillus subtilis C-1 isolated from petroleum sludge. Appl. Environ. Microbiol. 68:6210-6219. http://dx.doi.org/10.1128/AEM.68.12.6210-6219.2002.
21. Suckau D, Resemann A, Schuerenberg M, Hufnagel P, Franzen J, Holle A. 2003. A novel MALDI LIFT-TOF/TOF mass spectrometer for proteomics. Anal. Bioanal. Chem. 376:952-965. http://dx.doi.org/10.1007/s00216-003-2057-0.
22. Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680. http://dx.doi.org/10.1093/nar/22.22.4673.
23. Koumoutsi A, Chen XH, Vater J, Borriss R. 2007. DegU and YczE positively regulate the synthesis of bacillomycin D by Bacillus amyloliquefaciens strain FZB42. Appl. Environ. Microbiol. 73:6953-6964. http://dx.doi.org/10.1128/AEM.00565-07.
24. Mariappan A, Makarewicz O, Chen XH, Borriss R. 2012. Twocomponent response regulator degU controls the expression of bacilysin in plant-growth-promoting bacterium Bacillus amyloliquefaciens FZB42. J. Mol. Microbiol. Biotechnol. 22:114-125. http://dx.doi.org/10.1159/000338804.
25. Martinez-Bueno M, Maqueda M, Galvet A, Samyn B, van Beeumen J, Coyette J, Valdivia E. 1994. Determination of the gene sequence and the molecular structure of the enterococcal peptide antibiotic AS-48. J. Bacteriol. 176:6334-6339.
26. Kemperman R, Kuipers A, Karsens H, Nauta A, Kuipers O, Kok J. 2003. Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574. Appl. Environ. Microbiol. 69:1589-1597. http://dx.doi.org/10.1128/AEM.69.3.1589-1597.2003.
27. Martin-Visscher LA, Gong X, Duszyk M, Vederas JC. 2009. The threedimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif. J. Biol. Chem. 284:28674-28681. http://dx.doi.org/10.1074/jbc.M109.036459.
28. Wirawan RE, Swanson KM, Kleffmann T, Jack RW, Tagg JR. 2007. Uberolysin: a novel cyclic bacteriocin produced by Streptococcus uberis. Microbiology 153:1619-1630. http://dx.doi.org/10.1099/mic.0.2006/005967-0.
29. Kalmokoff ML, Cyr TD, Hefford MA, Whitford MF, Teather RM. 2003. Butyrivibriocin AR10, a new cyclic bacteriocin produced by the ruminal anaerobe Butyrivibrio fibrisolvens AR10: characterization of the gene and peptide. Can. J. Microbiol. 49:763-773. http://dx.doi.org/10.1139/w03-101.
30. Kawai Y, Saito T, Kitazawa H, Itoh T. 1998. Gassericin A; an uncommon cyclic bacteriocin produced by Lactobacillus gasseri LA39 linked at N-and C-terminal ends. Biosci. Biotechnol. Biochem. 62:2438-2440. http://dx.doi.org/10.1271/bbb.62.2438.
31. Sawa N, Zendo T, Kiyofuji J, Fujita K, Himeno K, Nakayama J, Sonomoto K. 2009. Identification and characterization of lactocyclicin Q, a novel cyclic bacteriocin produced by Lactococcus sp. strain QU 12. Appl. Environ. Microbiol. 75:1552-1558. http://dx.doi.org/10.1128/AEM.02299-08.
32. Sedgley CM, Clewell DB, Flannagan SE. 2009. Plasmid pAMS1-encoded, bacteriocin-related "Siblicide" in Enterococcus faecalis. J. Bacteriol. 191: 3183-3188. http://dx.doi.org/10.1128/JB.00147-09.
33. Maqueda M, Sanchez-Hidalgo M, Fernandez M, Montalban-Lopez M, Valdivia E, Martinez-Bueno M. 2008. Genetic features of circular bacteriocins produced by Gram-positive bacteria. FEMS Microbiol. Rev. 32:2-http://dx.doi.org/10.1111/j.1574-6976.2007.00087.x.
34. Coelho MLV, Coutinho BG, Cabral da Silva Santos O, Nes IF, Bastos MCF. 2014. Immunity to the Staphylococcus aureus leaderless fourpeptide bacteriocin aureocin A70 is conferred by AurI, an integral membrane protein. Res. Microbiol. 165:50-59. http://dx.doi.org/10.1016/j.resmic.2013.11.001.
35. Roberts AA, Sharma SV, Strankman AW, Duran SR, Rawat M, Hamilton JC. 2013. Mechanistic studies of FosB: a divalent-metaldependent bacillithiol-S-transferase that mediates fosfomycin resistance in Staphylococcus aureus. Biochem. J. 451:69-79. http://dx.doi.org/10.1042/BJ20121541.
36. Martin-Visscher LA, van Belkum MJ, Garneau-Tsodikova S, Whittal RM, Zheng J, McMullen LM, Vederas JC. 2008. Isolation and characterization of carnocyclin a, a novel circular bacteriocin produced by Carnobacterium maltaromaticum UAL307. Appl. Environ. Microbiol. 74: 4756-4763. http://dx.doi.org/10.1128/AEM.00817-08.
37. Masuda Y, Ono H, Kitagawa H, Ito H, Mu F, Sawa N, Zendo T. 2011. Identification and characterization of leucocyclicin Q, a novel cyclic bacteriocin produced by Leuconostoc mesenteroides TK41401. Appl. Environ. Microbiol. 77:8164-8170. http://dx.doi.org/10.1128/AEM.06348-11.
38. Borrero J, Brede DA, Skaugen M, Diep DB, Herranz C, Nes IF, Cintas LM, Hernández PE. 2011. Characterization of garvicin ML, a novel circular bacteriocin produced by Lactococcus garvieae DCC43, isolated from mallard ducks (Anas platyrhynchos). Appl. Environ. Microbiol. 77:369-373. http://dx.doi.org/10.1128/AEM.01173-10.
39. Maqueda M, Galvez A, Bueno MM, Sanchez-Barrena MJ, Gonzalez C, Albert A, Rico M, Valdivia E. 2004. Peptide AS-48: prototype of a new class of cyclic bacteriocins. Curr. Protein Pept. Sci. 5:399-416. http://dx.doi.org/10.2174/1389203043379567.
40. Leer RJ, van der Vossen JM, van Giezen M, van Noort JM, Pouwels PH. 1995. Genetic analysis of acidocin B, a novel bacteriocin produced by Lactobacillus acidophilus. Microbiology 141:1629-1635. http://dx.doi.org/10.1099/13500872-141-7-1629.
41. Kawulka K, Sprules T, McKay RT, Mercier P, Diaper CM, Zuber P, Vederas JC. 2003. Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine. J. Am. Chem. Soc. 125:4726-4727. http://dx.doi.org/10.1021/ja029654t.
42. Montalban-Lopez M, Sanchez-Hidalgo M, Cebrian R, Maqueda M. 2012. Discovering the bacterial circular proteins: bacteriocins, cyanobactins, and pilins. J. Biol. Chem. 287:27007-27013. http://dx.doi.org/10.1074/jbc.R112.354688.