Two bifunctional enzymes with ferric reduction ability play complementary roles during magnetosome synthesis in Magnetospirillum gryphiswaldense MSR-1

Journal of Bacteriology

Volumn 195, Issue 4, 2013, Pages 876-885

  Zhang, Chan ^a,c   Meng, Xia ^a,b   Li, Ningxiao ^a,c   Wang, Wei ^a,c   Sun, Yuan ^a,c   Jiang, Wei ^a,c   Guan, Guohua ^a,c   Li, Ying ^a,c  

^a CHINA AGRICULTURAL UNIVERSITY   (China)

^b YANGZHOU UNIVERSITY   (China)

^c France China Biomineralization and Nano structure Laboratory   (China)

Author keywords

[No Author keywords available]

Indexed keywords

FERRIC ION; FERRIC REDUCTASE 5; FERRIC REDUCTASE 6; OXIDOREDUCTASE; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; BACTERIUM MUTANT; CELL GROWTH; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE DELETION; GENE EXPRESSION; GENETIC COMPLEMENTATION; GENETIC TRANSCRIPTION; IN VITRO STUDY; IN VIVO STUDY; IRON ABSORPTION; IRON RESTRICTION; MAGNETOSOME; MAGNETOSPIRILLUM GRYPHISWALDENSE; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; QUANTITATIVE ANALYSIS; REAL TIME POLYMERASE CHAIN REACTION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; FERRIC COMPOUNDS; GENE DELETION; GENE EXPRESSION REGULATION, BACTERIAL; MAGNETOSOMES; MAGNETOSPIRILLUM; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PLASMIDS; SPRAINS AND STRAINS;

EID: 84873551358     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01750-12     Document Type: Article

References (42)

1. Neilands JB. 1981. Microbial iron compounds. Annu. Rev. Biochem. 50:715-731.
2. Andrews SC, Robinson AK, Rodriguez-Quinones F. 2003. Bacterial iron homeostasis. FEMS Microbiol. Rev. 27:215-237.
3. Guerinot ML. 1994. Microbial iron transport. Annu. Rev. Microbiol. 48:743-772.
4. Dailey HA, Jr, Lascelles J. 1977. Reduction of iron and synthesis of protoheme by Spirillum itersonii and other organisms. J. Bacteriol. 129: 815-820.
5. Vrzheshch PV. 2007. Steady-state kinetics of bifunctional enzymes: taking into account kinetic hierarchy of fast and slow catalytic cycles in a generalized model. Biochemistry 72:936-943.
6. Sutay Kocabas D, Bakir U, Phillips SE, McPherson MJ, Ogel ZB. 2008. Purification, characterization, and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum. Appl. Microbiol. Biotechnol. 79:407-415.
7. Schneider TR, Gerhardt E, Lee M, Liang PH, Anderson KS, Schlichting I. 1998. Loop closure and intersubunit communication in tryptophan synthase. Biochemistry 37:5394-5406.
8. Gehring AM, Lees WJ, Mindiola DJ, Walsh CT, Brown ED. 1996. Acetyltransfer precedes uridylyltransfer in the formation of UDP-Nacetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry 35:579-585.
9. Fontecave M, Coves J, Pierre JL. 1994. Ferric reductases or flavin reductases. Biometals 7:3-8.
10. Schröder I, Johnson E, de Vries S. 2003. Microbial ferric iron reductases. FEMS Microbiol. Rev. 27:427-447.
11. Petrat F, Paluch S, Dogruoz E, Dorfler P, Kirsch M, Korth HG, Sustmann R, de Groot H. 2003. Reduction of Fe(III) ions complexed to physiological ligands by lipoyl dehydrogenase and other flavoenzymes in vitro: implications for an enzymatic reduction of Fe(III) ions of the labile iron pool. J. Biol. Chem. 278:46403-46413.
12. Blakemore RP, Maratea D, Wolfe RS. 1979. Isolation and pure culture of a freshwater magnetic spirillum in chemically defined medium. J. Bacteriol. 140:720-729.
13. Andrews SC, Smith JM, Hawkins C, Williams JM, Harrison PM, Guest JR. 1993. Overproduction, purification and characterization of the bacterioferritin of Escherichia coli and a C-terminally extended variant. Eur. J. Biochem. 213:329-338.
14. Hartmann A, Braun V. 1981. Iron uptake and iron limited growth of Escherichia coli K-12. Arch. Microbiol. 130:353-356.
15. Matzanke BF, Muller GI, Bill E, Trautwein AX. 1989. Iron metabolism of Escherichia coli studied by Mossbauer spectroscopy and biochemical methods. Eur. J. Biochem. 183:371-379.
16. Schüler D, Baeuerlein E. 1996. Iron-limited growth and kinetics of iron uptake in Magnetospirillum gryphiswaldense. Arch. Microbiol. 166:301-307.
17. Rong C, Huang Y, Zhang W, Jiang W, Li Y, Li J. 2008. Ferrous iron transport protein B gene (feoB1) plays an accessory role in magnetosome formation in Magnetospirillum gryphiswaldense strain MSR-1. Res. Microbiol. 159:530-536.
18. Rong C, Zhang C, Zhang Y, Qi L, Yang J, Guan G, Li Y, Li J. 2012. FeoB2 functions in magnetosome formation and oxidative stress protection in Magnetospirillum gryphiswaldense strain MSR-1. J. Bacteriol. 194: 3972-3976.
19. Sali A, Blundell TL. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
20. Ding Y, Li J, Liu J, Yang J, Jiang W, Tian J, Li Y, Pan Y. 2010. Deletion of the ftsZ-like gene results in the production of superparamagnetic magnetite magnetosomes in Magnetospirillum gryphiswaldense. J. Bacteriol. 192:1097-1105.
21. Hefti MH, Van Vuqt-Van der Toorn CJ, Dixon R, Vervoort J. 2001. A novel purification method for histidine-tagged proteins containing a thrombin cleavage site. Anal. Biochem. 295:180-185.
22. Noguchi Y, Fujiwara T, Yoshimatsu K, Fukumori Y. 1999. Iron reductase for magnetite synthesis in the magnetotactic bacterium Magnetospirillum magnetotacticum. J. Bacteriol. 181:2142-2147.
23. Ohshiro T, Aoi Y, Torii K, Izumi Y. 2002. Flavin reductase coupling with two monooxygenases involved in dibenzothiophene desulfurization: purification and characterization from a non-desulfurizing bacterium, Paenibacillus polymyxa A-1. Appl. Microbiol. Biotechnol. 59:649-657.
24. Zhao L, Wu D, Wu LF, Song T. 2007. A simple and accurate method for quantification of magnetosomes in magnetotactic bacteria by common spectrophotometer. J. Biochem. Biophys. Methods 70:377-383.
25. Huang Y, Zhang W, Jiang W, Rong C, Li Y. 2007. Disruption of a fur-like gene inhibits magnetosome formation in Magnetospirillum gryphiswaldense MSR-1. Biochemistry (Mosc.) 72:1247-1253.
26. França A, Freitas AI, Henriques AF, Cerca N. 2012. Optimizing a qPCR gene expression quantification assay for S. epidermidis biofilms: a comparison between commercial kits and a customized protocol. PLoS One 7:e37480. doi:10.1371/journal.pone.0037480.
27. Franca A, Melo LD, Cerca N. 2011. Comparison of RNA extraction methods from biofilm samples of Staphylococcus epidermidis. BMC Res. Notes 4:572. doi:10.1186/1756-0500-4-572.
28. Lee C, Kim J, Shin SG, Hwang S. 2006. Absolute and relative QPCR quantification of plasmid copy number in Escherichia coli. J. Biotechnol. 123:273-280.
29. Paakkanen R, Vauhkonen H, Eronen KT, Jarvinen A, Seppanen M, Lokki ML. 2012. Copy number analysis of complement C4A, C4B and C4A silencing mutation by real-time quantitative polymerase chain reaction. PLoS One 7:e38813. doi:10.1371/journal.pone.0038813.
30. Webb BN, Ballinger JW, Kim E, Belchik SM, Lam KS, Youn B, Nissen MS, Xun L, Kang C. 2010. Characterization of chlorophenol 4-monooxygenase (Tftc) of Burkholderia cepacia AC1100. J. Biol. Chem. 285:2014-2027.
31. Xia M, Wei J, Lei Y, Ying L. 2007. A novel ferric reductase purified from Magnetospirillum gryphiswaldense MSR-1. Curr. Microbiol. 55:71-75.
32. Russel M, Model P. 1988. Sequence of thioredoxin reductase from Escherichia coli: relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 263:9015-9019.
33. Bester PA, Litthauer D, Piater LA, van Heerden E. 2010. A thioredoxin reductase-like protein from the thermophile, Thermus scotoductus SA-01, displaying iron reductase activity. FEMS Microbiol. Lett. 302:182-188.
34. +. Structure 9:311-319.
35. Shibata N, Ueda Y, Takeuchi D, Haruyama Y, Kojima S, Sato J, Niimura Y, Kitamura M, Higuchi Y. 2009. Structure analysis of the flavoredoxin from Desulfovibrio vulgaris Miyazaki F reveals key residues that discriminate the functions and properties of the flavin reductase family. FEBS J. 276:4840-4853.
36. Mo H, Chen Q, Du J, Tang L, Qin F, Miao B, Wu X, Zeng J. 2011. Ferric reductase activity of the ArsH protein from Acidithiobacillus ferrooxidans. J. Microbiol. Biotechnol. 21:464-469.
37. Hanahan D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
38. Simon R, Priefer U, Pühler A. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Nat. Biotechnol. 1:784-791.
39. Taylor LA, Rose RE. 1988. A correction in the nucleotide sequence of the Tn903 kanamycin resistance determinant in pUC4K. Nucleic Acids Res. 16:358.
40. Schweizer HP. 1993. Small broad-host-range gentamycin resistance gene cassettes for site specific insertion and deletion mutagenesis. Biotechniques 15:831-834.
41. Li L, Rock JL, Nelson DR. 2008. Identification and characterization of a repeat-in-toxin gene cluster in Vibrio anguillarum. Infect. Immun. 76: 2620-2632.
42. Santos PM, Bartolo ID, Blatny JM, Zennaro E, Valla S. 2001. New broad-host-range promoter probe vectors based on the plasmid RK2 replicon. FEMS Microbiol. Lett. 195:91-96.