Construction and characterization of tetH overexpression and Knockout strains of Acidithiobacillus ferrooxidans

Journal of Bacteriology

Volumn 196, Issue 12, 2014, Pages 2255-2264

  Yu, Yangyang ^a   Liu, Xiangmei ^a   Wang, Huiyan ^a   Li, Xiuting ^a   Lin, Jianqun ^a  

^a SHANDONG UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HYDROLASE; SULFUR; TETRATHIONATE HYDROLASE; TETRATHIONIC ACID; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

ACIDITHIOBACILLUS FERROOXIDANS; ARTICLE; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL STRAIN; BACTERIUM MUTANT; CONTROLLED STUDY; ENERGY RESOURCE; ENZYME ACTIVITY; ENZYME ANALYSIS; GENE FUNCTION; GENE IDENTIFICATION; GENE INACTIVATION; GENE LOCUS; GENE OVEREXPRESSION; GENE SILENCING; GENETIC ANALYSIS; GENETIC MANIPULATION; HYDROLYSIS; KNOCKOUT GENE; NONHUMAN; OXIDATION KINETICS; PLASMID; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SPONTANEOUS MUTATION; TETH GENE; WILD TYPE; ACIDITHIOBACILLUS; ENERGY METABOLISM; GENE DELETION; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; OXIDATION REDUCTION REACTION; PHYSIOLOGY;

ACIDITHIOBACILLUS; BACTERIAL PROTEINS; ENERGY METABOLISM; GENE DELETION; GENE EXPRESSION REGULATION, BACTERIAL; OXIDATION-REDUCTION; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; TETRATHIONIC ACID;

EID: 84901217771     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01472-13     Document Type: Article

References (44)

1. Bonnefoy V, Holmes DS. 2012. Genomic insights into microbial iron oxidation and iron uptake strategies in extremely acidic environments. Environ. Microbiol. 14:1597-1611. http://dx.doi.org/10.1111/j.1462-2920.2011.02626.x.
2. Bird LJ, Bonnefoy V, Newman DK. 2011. Bioenergetic challenges of microbial iron metabolisms. Trends Microbiol. 19:330-340. http://dx.doi.org/10.1016/j.tim.2011.05.001.
3. Bruscella P, Appia-Ayme C, Levican G, Ratouchniak J, Jedlicki E, Holmes DS, Bonnefoy V. 2007. Differential expression of two bc1 complexes in the strict acidophilic chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans suggests a model for their respective roles in iron or sulfur oxidation. Microbiology 153:102-110. http://dx.doi.org/10.1099/mic.0.2006/000067-0.
4. Quatrini R, Appia-Ayme C, Denis Y, Ratouchniak J, Veloso F, Valdes J, Lefimil C, Silver S, Roberto F, Orellana O, Denizot F, Jedlicki E, Holmes DS, Bonnefoy V. 2006. Insights into the iron and sulfur energetic metabolism of Acidithiobacillus ferrooxidans by microarray transcriptome profiling. Hydrometallurgy 83:263-272. http://dx.doi.org/10.1016/j.hydromet.2006.03.030.
5. Quatrini R, Appia-Ayme C, Denis Y, Jedlicki E, Holmes DS, Bonnefoy V. 2009. Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans. BMC Genomics 10:394. http://dx.doi.org/10.1186/1471-2164-10-394.
6. Valdes J, Pedroso I, Quatrini R, Dodson RJ, Tettelin H, Blake R, II, Eisen JA, Holmes DS. 2008. Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications. BMC Genomics 9:597. http://dx.doi.org/10.1186/1471-2164-9-597.
7. Meulenberg R, Pronk JT, Hazeu W, Bos P, Kuenen JG. 1992. Oxidation of reduced sulfur compounds by intact cells of Thiobacillus acidophilus. Arch. Microbiol. 157:161-168.
8. de Jong GAH, Hazeu W, Bos P, Kuenen JG. 1997. Polythionate degradation by tetrathionate hydrolase of Thiobacillus ferrooxidans. Microbiology 143:499-504. http://dx.doi.org/10.1099/00221287-143-2-499.
9. de Jong GAH, Hazeu W, Bos P, Kuenen JG. 1997. Isolation of tetrathionate hydrolase from Thiobacillus acidophilus. Eur. J. Biochem. 243:678-683. http://dx.doi.org/10.1111/j.1432-1033.1997.00678.x.
10. Bugaytsova Z, Lindstrom EB. 2004. Localization, purification and properties of a tetrathionate hydrolase from Acidithiobacillus caldus. Eur. J. Biochem. 271:272-280. http://dx.doi.org/10.1046/j.1432-1033.2003.03926.x.
11. Rzhepishevska OI, Valdes J, Marcinkeviciene L, Gallardo CA, Meskys R, Bonnefoy V, Holmes DS, Dopson M. 2007. Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds. Appl. Environ. Microbiol. 73:7367-7372. http://dx.doi.org/10.1128/AEM.01497-07.
12. Kanao T, Kamimura K, Sugio T. 2007. Identification of a gene encoding a tetrathionate hydrolase in Acidithiobacillus ferrooxidans. J. Biotechnol. 132:16-22. http://dx.doi.org/10.1016/j.jbiotec.2007.08.030.
13. Kanao T, Matsumoto C, Shiraga K, Yoshida K, Takada J, Kamimura K. 2010. Recombinant tetrathionate hydrolase from Acidithiobacillus ferrooxidans requires exposure to acidic conditions for proper folding. FEMS Microbiol. Lett. 309:43-47. http://dx.doi.org/10.1111/j.1574-6968.2010.02019.x.
14. Sugio T, Taha TM, Takeuchi F. 2009. Ferrous iron production mediated by tetrathionate hydrolase in tetrathionate-, sulfur-, and iron-grown Acidithiobacillus ferrooxidansATCC23270 cells. Biosci. Biotechnol. Biochem. 73:1381-1386. http://dx.doi.org/10.1271/bbb.90036.
15. Beard S, Paradela A, Albar JP, Jerez CA. 2011. Growth of Acidithiobacillus ferrooxidans ATCC 23270 in thiosulfate under oxygen-limiting conditions generates extracellular sulfur globules by means of a secreted tetrathionate hydrolase. Front. Microbiol. 2:79. http://dx.doi.org/10.3389/fmicb.2011.00079.
16. Kanao T, Kosaka M, Yoshida K, Nakayama H, Tamada T, Kuroki R, Yamada H, Takada J, Kamimura K. 2013. Crystallization and preliminary X-ray diffraction analysis of tetrathionate hydrolase from Acidithiobacillus ferrooxidans. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69:692-694. http://dx.doi.org/10.1107/S1744309113013419.
17. Zarschler K, Janesch B, Zayni S, Schaffer C, Messner P. 2009. Construction of a gene knockout system for application in Paenibacillus alvei CCM 2051T, exemplified by the S-layer glycan biosynthesis initiation enzyme Wsfpp. Appl. Environ. Microbiol. 75:3077-3085. http://dx.doi.org/10.1128/AEM.00087-09.
18. Camp S, Zhang L, Krejci E, Dobbertin A, Bernard V, Girard E, Duysen EG, Lockridge O, Jaco AD, Taylor P. 2010. Contributions of selective knockout studies to understanding cholinesterase disposition and function. Chem. Biol. Interact. 187:72-77. http://dx.doi.org/10.1016/j.cbi.2010.02.008.
19. Kumar R, Shimizu K. 2011. Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures. Microb. Cell Fact. 10:3-17. http://dx.doi.org/10.1186/1475-2859-10-3.
20. Liu Z, Guiliani N, Appia-Ayme C, Borne F, Ratouchniak J, Bonnefoy V. 2000. Construction and characterization of a recA mutant of Thiobacillus ferrooxidans by marker exchange. J. Bacteriol. 182:2269-2276. http://dx.doi.org/10.1128/JB.182.8.2269-2276.2000.
21. van Zyl LJ, Munster JM, Rawlings DE. 2008. Construction of arsB and tetH mutants of the sulfur-oxidizing bacterium Acidithiobacillus caldus by marker exchange. Appl. Environ. Microbiol. 74:5686-5694. http://dx.doi.org/10.1128/AEM.01235-08.
22. Wang H, Liu X, Liu S, Yu Y, Lin J, Lin J, Pang X, Zhao J. 2012. Development of a markerless gene replacement system for Acidithiobacillus ferrooxidans and construction of a pfkB mutant. Appl. Environ. Microbiol. 78:1826-1835. http://dx.doi.org/10.1128/AEM.07230-11.
23. Silverman MP, Lundgren DG. 1959. Studies on the chemoautotrophic iron bacterium Ferrobacillus ferrooxidans. J. Bacteriol. 77:642-647.
24. Peng JB, Yan WM, Bao XZ. 1994. Plasmid and transposon transfer to Thiobacillus ferrooxidans. J. Bacteriol. 176:2892-2897.
25. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
26. Herrera L, Ruiz P, Aguillon JC, Fehrmann A. 1989. A new spectrophotometric method for the determination of ferrous iron in the presence of ferric iron. J. Chem. Technol. Biotechnol. 44:171-181.
27. Kelly DP, Chambers LA, Trudinger PA. 1969. Cyanolysis and spectrophotometric estimation of trithionate in mixture with thiosulfate and tetrathionate. Anal. Chem. 41:898-902. http://dx.doi.org/10.1021/ac60276a029.
28. Nor YM, Tabatabai MA. 1975. Colorimetric determination of microgram quantities of thiosulfate and tetrathionate. Anal. Lett. 8:537-547. http://dx.doi.org/10.1080/00032717508058238.
29. Nieto P, Covarrubias P, Jedlicki E, Holmes D, Quatrini R. 2009. Selection and evaluation of reference genes for improved interrogation of microbial transcriptomes: case study with the extremophile Acidithiobacillus ferrooxidans. BMC Mol. Biol. 10:63-73. http://dx.doi.org/10.1186/1471-2199-10-63.
30. PfafflM. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29:e45. http://dx.doi.org/10.1093/nar/29.9.e45.
31. Wakai S, Kikumoto M, Kanao T, Kamimura K. 2004. Involvement of sulfide:quinone oxidoreductase in sulfur oxidation of an acidophilic ironoxidizing bacterium, Acidithiobacillus ferrooxidans NASF-1. Biosci. Biotechnol. Biochem. 68:2519-2528. http://dx.doi.org/10.1271/bbb.68.2519.
32. Wakai S, Tsujita M, Kikumoto M, Manchur MA, Kanao T, Kamimura K. 2007. Purification and characterization of sulfide:quinone oxidoreductase from an acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidans. Biosci. Biotechnol. Biochem. 71:2735-2742. http://dx.doi.org/10.1271/bbb.70332.
33. Zhang Y, Cherney MM, Solomonson M, Liu J, James MN, Weiner JH. 2009. Preliminary X-ray crystallographic analysis of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65:839-842. http://dx.doi.org/10.1107/S1744309109027535.
34. Cherney MM, Zhang Y, Solomonson M, Weiner JH, James MN. 2010. Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: insights into sulfidotrophic respiration and detoxification. J. Mol. Biol. 398:292-305. http://dx.doi.org/10.1016/j.jmb.2010.03.018.
35. Rohwerder T, Sand W. 2003. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149:1699-1709. http://dx.doi.org/10.1099/mic.0.26212-0.
36. Kikumoto M, Nogami S, Kanao T, Takada J, Kamimura K. 2013. Tetrathionate-forming thiosulfate dehydrogenase from the acidophilic, chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans. Appl. Environ. Microbiol. 79:113-120. http://dx.doi.org/10.1128/AEM.02251-12.
37. Holmes D, Bonnefoy V. 2007. Genetic and bioinformatic insights into iron and sulfur oxidation mechanisms of bioleaching organisms, p 281-307. In Rawlings D, Johnson B (ed), Biomining. Springer-Verlag, Berlin, Germany.
38. Valdes J, Pedroso I, Quatrini R, Holmes DS. 2008. Comparative genome analysis of Acidithiobacillus ferrooxidans, A. thiooxidans and A. caldus: insights into their metabolism and ecophysiology. Hydrometallurgy 94: 180-184. http://dx.doi.org/10.1016/j.hydromet.2008.05.039.
39. Nomura CT, Taguchi K, Gan Z, Kuwabara K, Tanaka T, Takase K, Doi Y. 2005. Expression of 3-ketoacyl-acyl carrier protein reductase (fabG) genes enhances production of polyhydroxyalkanoate copolymer from glucose in recombinant Escherichia coli JM109. Appl. Environ. Microbiol. 71:4297-4306. http://dx.doi.org/10.1128/AEM.71.8.4297-4306.2005.
40. Yin X, Wheatcroft R, Chambers JR, Liu B, Zhu J, Gyles CL. 2009. Contributions of O island 48 to adherence of enterohemorrhagic Escherichia coli O157: H7 to epithelial cells in vitro and in ligated pig ileal loops. Appl. Environ. Microbiol. 75:5779-5786. http://dx.doi.org/10.1128/AEM.00507-09.
41. Kienesberger S, Gorkiewicz G, Joainig MM, Scheicher SR, Leitner E, Zechner EL. 2007. Development of experimental genetic tools for Campylobacter fetus. Appl. Environ. Microbiol. 73:4619-4630. http://dx.doi.org/10.1128/AEM.02407-06.
42. Simon R, Priefer U, Puhler A. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Nat. Biotechnol. 1:784-791. http://dx.doi.org/10.1038/nbt1183-784.
43. Meng J, Wang H, Liu X, Lin J, Pang X, Lin J. 2013. Construction of small plasmid vectors for use in genetic improvement of the extremely acidophilic Acidithiobacillus caldus. Microbiol. Res. 168:469-476. http://dx.doi.org/10.1016/j.micres.2013.04.003.
44. Dykxhoorn DM, Pierre RS, Linn T. 1996. A set of compatible tac promoter expression vectors. Gene 177:133-136. http://dx.doi.org/10.1016/0378-1119(96)00289-2.