Cloning and characterization of nif structural and regulatory genes in the purple sulfur bacterium, Halorhodospira halophila

Journal of Bioscience and Bioengineering

Volumn 101, Issue 3, 2006, Pages 263-270

  Tsuihiji, Hisayoshi ^a   Yamazaki, Yoichi ^a   Kamikubo, Hironari ^a   Imamoto, Yasushi ^a   Kataoka, Mikio ^a  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

Halorhodospira halophila; nifA; nifD; nifH; nitrogenase; photobiological hydrogen generation; purple sulfur bacteria

Indexed keywords

AMINO ACIDS; BACTERIA; GENES; HYDROGEN; NITROGEN; PHOTOSYNTHESIS; PROTEINS;

HALORHODOSPIRA HALOPHILA; NIFA; NIFH; NITROGENASE; PHOTOBIOLOGICAL HYDROGEN GENERATION; PURPLE SULFUR BACTERIA;

CLONING;

BACTERIAL PROTEIN; HYDROGEN; IRON; NITROGENASE; PROTEIN NIF; PROTEIN NIFA; PROTEIN NIFD; PROTEIN NIFH; PROTEIN NIFL; UNCLASSIFIED DRUG; NITROGENASE REDUCTASE; OXIDOREDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; CORRELATION ANALYSIS; GENE INTERACTION; GENETIC CONSERVATION; GENETIC IDENTIFICATION; HALORHODOSPIRA HALOPHILA; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; REGULATOR GENE; REGULATORY MECHANISM; SALT STRESS; SALT TOLERANCE; STRUCTURAL GENE; SULFUR BACTERIUM; BIOLOGICAL MODEL; BIOTECHNOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; CHROMATIACEAE; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; NITROGEN FIXATION; PHYLOGENY; SEQUENCE HOMOLOGY;

BACTERIA (MICROORGANISMS); CHROMATIACEAE; HALORHODOSPIRA HALOPHILA; PHOTOBACTERIA;

AMINO ACID SEQUENCE; BASE SEQUENCE; BIOTECHNOLOGY; CHROMATIACEAE; CLONING, MOLECULAR; GENE EXPRESSION REGULATION, BACTERIAL; GENES, REGULATOR; HALORHODOSPIRA HALOPHILA; HYDROGEN; MODELS, GENETIC; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITROGEN FIXATION; OXIDOREDUCTASES; PHYLOGENY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 33745727506     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.101.263     Document Type: Article

References (30)

1. Wakayama T., Nakada E., Asada Y., and Miyake J. Effect of light/dark cycle on bacterial hydrogen production by Rhodobacter sphaeroides. RV. Appl. Biochem. Biotechnol. (2000) 84-86 431-440
2. Oelze J., and Klein G. Control of nitrogen fixation by oxygen in purple nonsulfur bacteria. Arch. Microbiol. 165 (1996) 219-225
3. Raymond J.C., and Sistrom W.R. Ectothiorhodospira halophila: a new species of the genus Ectothiorhodospira. Arch. Mikrobiol. 69 (1969) 121-126
4. Orme-Johnson W.E. Molecular basis of biological nitrogen fixaton. Annu. Rev. Biophys. Biophys. Chem. 14 (1985) 419-459
5. Emerich D.W., Hageman R.V., and Burris R.H. Interactions of dinitrogenase and dinitrogenase reductase. Adv. Enzymol. Relat. Areas. Mol. Biol. 52 (1981) 1-22
6. Martinez-Argudo I., Little R., Shearer N., Johnson P., and Dixon R. The NifL-NifA system: a multidomain transcriptional regulatory complex that integrates environmental signals. J. Bacteriol. 186 (2004) 601-610
7. Cullen P.J., Bowman W.C., and Kranz R.G. In vitro reconstitution and characterization of the Rhodobacter capsulatus NtrB and NtrC two-component system. J. Biol. Chem. 271 (1996) 6530-6536
8. Imhoff J.F., and Suling J. The phylogenic relationship among Ectothiorhodospiraceae: a reevaluation of their taxonomy on the basis of 16SrRNA analyses. Arch. Microbiol. 165 (1996) 106-113
9. Kondo T., Arakawa M., Hirai T., Wakayama T., Hara M., and Miyake J. Enhancement of hydrogen production by a photosynthetic bacterium mutant with reduced pigment. J. Biosci. Bioeng. 93 (2002) 145-150
10. Sambrook J., and Russell D.W. Molecular cloning: a laboratory manual. 3rd ed. 1 (2001), Cold Spring Harbor Laboratory Press, New York 6.4-6.11
11. Thompson J.D., Higgins D.G., and Gibson T.J. 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 (1994) 4673-4680
12. Koku H., Eroglu I., Gündüz U., Yücel M., and Türker L. Aspects of the metabolism of hydrogen production by Rhodobacter sphaeroides. Int. J. Hydrogen Energ. 27 (2002) 1315-1329
13. Woese C.R., Stackebrandt E., Macke T.J., and Fox G.E. A phylogenetic definition of the major eubacterial taxa. Syst. Appl. Microbiol. 6 (1985) 143-151
14. Georgiadis M.M., Komiya H., Chakrabarti P., Woo D., Kornuc J.J., and Rees D.C. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257 (1992) 1653-1659
15. Kim J., and Rees D.C. Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii. Nature 360 (1992) 553-560
16. Madern D., Pfister C., and Zaccai G. Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts. Eur. J. Biochem. 230 (1995) 1088-1095
17. Buck M., Cannon W., and Woodcock J. Mutational analysis of upstream sequences required for transcriptional activation of the Klebsiella pneumoniae nifH promoter. Nucleic Acids Res. 15 (1987) 9945-9956
18. Barrios H., Valderrama B., and Morett E. Compilation and analysis of sigma (54)-dependent promoter sequences. Nucleic Acids Res. 27 (1999) 4305-4313
19. Dixon R. The oxygen-responsive NifL-NifA complex: a novel two-component regulatory system controlling nitrogenase synthesis in γ-proteobacteria. Arch. Microbiol. 169 (1998) 371-380
20. Siddavattam D., Steibl H.-D., Kreutzer R., and Klingmüller W. Regulation of nif gene expression in Enterobacter agglomerans: nucleotide sequence of the nifLA operon and influence of temperature and ammonium on its transcription. Mol. Gen. Genet. 249 (1995) 629-636
21. Morett E., and Segovia L. The sigma 54 bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of their functional domains. J. Bacteriol. 175 (1993) 6067-6074
22. Gonzalez V., Olvera L., Soberon X., and Morett E. In vivo studies on the positive control function of NifA: a conserved hydrophobic amino acid patch at the central domain involved in transcriptional activation. Mol. Microbiol. 28 (1998) 55-67
23. Walker J.E., Saraste M., Runswick M.J., and Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1 (1982) 945-951
24. Reyes-Ramirez F., Little R., and Dixon R. Mutant forms of the Azotobacter vinelandii transcriptional activator NifA resistant to inhibition by the NifL regulatory protein. J. Bacteriol. 184 (2002) 6777-6785
25. Fischer H.M., Bruderer T., and Hennecke H. Essential and non-essential domains in the Bradyrhizobium japonicum NifA protein: identification of indispensable cysteine residues potentially involved in redox reactivity and/or metal binding. Nucleic Acids Res. 16 (1988) 2207-2224
26. Husimi Y., Nishigaki K., Kinoshita Y., and Tanaka T. Cellstat - a continuous culture system of a bacteriophage for the study of the mutation rate and the selection process of the DNA level. Rev. Sci. Instrum. 53 (1982) 517-522
27. Egener T., Sarkar A., Martin D.E., and Reinhold-Hurek B. Identification of NifL-like protein in a diazotroph of the β-subgroup of the Proteobacteria, Azoarcus sp. strain BH72. Microbiology 148 Pt 10 (2002) 3203-3212
28. Zehr J.P., Mellon M.T., and Zani S. New nitrogen-fixing microorganisms detected in oligotrophic oceans by amplification of Nitrogenase (nifH) genes. Appl. Environ. Microbiol. 64 (1998) 3444-3450
29. Grunwald S.K., Lies D.P., Roberts G.P., and Ludden P.W. Posttranslational regulation of nitrogenase in Rhodospirillum rubrum strains overexpressing the regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase reductase activating glycohydrolase. J. Bacteriol. 177 (1995) 628-635
30. Maeda I., Mizoguchi T., Miura Y., Yagi K., Shioji N., and Miyasaka H. Influence of sulfate-reducing bacteria on outdoor hydrogen production by photosynthetic bacterium with seawater. Curr. Microbiol. 40 (2000) 210-213