Structural organization of the glnBA region of the Azospirillum brasilense genome

European Journal of Soil Biology

Volumn 45, Issue 1, 2009, Pages 100-105

  Castellen, Patrícia ^a   Wassem, Roseli ^a   Monteiro, Rose Adele ^a   Cruz, Leonardo Magalhães ^a   Steffens, Maria Berenice R ^a   Chubatsu, Leda S ^a   Maltempi de Souza, Emanuel ^a   Pedrosa, Fabio de Oliveira ^a  

^a FEDERAL UNIVERSITY OF PARANÁ   (Brazil)

Author keywords

Azospirillum brasilense; Clp proteases; glnBA operon; Nitrogen fixation; pAB441

Indexed keywords

AZOSPIRILLUM BRASILENSE;

EID: 57549088879     PISSN: 11645563     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejsobi.2008.09.010     Document Type: Article

References (46)

1. Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 (1997) 3389-3402
2. Arsene F., Kaminski P.A., and Elmerich C. Modulation of NifA activity by PII in Azospirillum brasilense: evidence for a regulatory role of the NifA N-terminal domain. J. Bacteriol. 178 (1996) 4830-4838
3. Bozouklian H., and Elmerich C. Nucleotide sequence of the Azospirillum brasilense Sp7 glutamine synthetase structural gene. Biochimie 68 (1986) 1181-1187
4. Claret L., and Rouvière-Yaniv J. Regulation of HU beta by CRP and FIS in Escherichia coli. J. Mol. Biol. 25 (1996) 126-139
5. Deuerling E., Schulze-Specking A., Tomoyasu T., Mogk A., and Bukau B. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400 (1999) 693-696
6. Döbereiner J., and Day J.M. Associative symbioses in tropical grasses characterization of micro organisms and dinitrogen-fixing sites. In: Newton W.E., and Nyman C.J. (Eds). Proceedings of the First International Symposium on Nitrogen Fixation (1975), Washington University Press, Pullman 518-538
7. Dodge R.W., and Scheraga H.A. Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A. Biochemistry 35 (1996) 1548-1559
8. Drlica K., and Rouviere-Yaniv J. Histonelike proteins of bacteria. Microbiol. Rev. 51 (1987) 301-319
9. Ewing B., and Green P. Base-calling of automated sequencer using Phred. II. Error probabilities. Genome Res. 8 (1998) 186-194
10. Ewing B., Hillier L., Wendi M.C., and Green P. Base-calling of automated sequencer traces using Phred. I. Accuracy assessment. Genome Res. 8 (1998) 175-185
11. Frydman J., and Hartl F.U. Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science 272 (1996) 1497-1502
12. Gauthier D., and Elmerich C. Relationship between glutamine synthetase and nitrogenase in Spirillum lipoferum. FEMS Microbiol. Lett. 2 (1977) 101-104
13. Giangrossi M., Giuliodori A.M., Gualerzi C.O., and Pon C.L. Selective expression of the β-subunit of nucleoid-associated protein HU during cold shock in Escherichia coli. Mol. Microbiol. 44 (2002) 205-216
14. Gordon D., Abajian C., and Green P. Consed: A graphical tool for sequence finishing. Genome Res. 8 (1998) 195-202
15. Gottesman S., and Maurizi M.R. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol. Rev. 56 (1992) 592-621
16. Gottesman S., and Maurizi M.R. Cell biology. Surviving starvation. Science 293 (2001) 614-615
17. Hesterkamp T., and Bukau B. The Escherichia coli trigger factor. FEBS Lett. 389 (1996) 32-34
18. Hesterkamp T., and Bukau B. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17 (1998) 4818-4828
19. Huergo L.F., Souza E.M., Steffens M.B.R., Yates M.G., Pedrosa F.O., and Chubatsu L.S. Regulation of glnB gene promoter expression in Azospirillum brasilense by the NtrC protein. FEMS Microbiol. Lett. 223 (2003) 33-40
20. Ishikawa J., and Hotta K. FramePlot: a new implementation of the frame analysis for predicting protein-coding regions in bacterial DNA with a high G + C content. FEMS Microbiol. Lett. 15 (1999) 251-253
21. Kano Y., Wada M., and Imamoto F. Genetic characterization of the gene hupA encoding the HU-2 protein of Escherichia coli. Gene 30 (1988) 331-335
22. Kramer G., Ramachandiran V., Horowitz P.M., and Hardesty B. The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor. Arch. Biochem. Biophys. 403 (2002) 63-70
23. Liu C.P., Perrett S., and Zhou J.M. Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding. J. Biol. Chem. 280 (2005) 13315-13320
24. Machado H.B., Funayama S., Rigo L.U., and Pedrosa F.O. Excretion of ammonium by Azospirillum brasilense mutants resistant to ethylenediamine. Can. J. Microbiol. 29 (1991) 549-553
25. Merrick M.J., and Edwards R.A. Nitrogen control in bacteria. Microbiol. Rev. 59 (1995) 604-622
26. Mogk A., Tomoyasu T., Goloubinoff P., Rüdiger S., Röder D., Langen H., and Bukau B. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18 (1999) 6934-6949
27. Mori E., Fulchieri M., Indorato C., Fani R., and Bazzicalupo M. Cloning, nucleotide sequencing, and expression of the Azospirillum brasilense lon gene: involvement in iron uptake. J. Bacteriol. 178 (1996) 3440-3446
28. Oberto J., and Rouviere-Yaniv J. Serratia marcescens contains a heterodimeric HU protein like Escherichia coli and Salmonella typhimurium. J. Bacteriol. 178 (1996) 293-297
29. Patzelt H., Rüdiger S., Brehmer D., Kramer G., Vorderwülbecke S., Schaffitzel E., Waitz A., Hesterkamp T., Dong L., Schneider-Mergener J., Bukau B., and Deuerling E. Binding specificity of Escherichia coli trigger factor. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 14244-14249
30. Rodriguez H., Mendoza A., Antonia Cruz M., Holguin G., Glick B.R., and Bashan Y. Pleiotropic physiological effects in the plant growth-promoting bacterium Azospirillum brasilense following chromosomal labelling in the clpX gene. FEMS Microbiol. Ecol. 57 (2006) 217-225
31. Rouviere-Yaniv J., Yaniv M., and Germonk J.E. Escherichia coli DNA-binding protein HU forms nucleosome-like structure with circular double-stranded DNA. Cell 17 (1979) 265-274
32. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: a Laboratory Manual (1989), Cold Spring Harbour Laboratory Press, New York
33. Scholz C., Stoller G., Zarnt T., Fischer G., and Schmid F.X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16 (1997) 54-58
34. Schröder H., Langer T., Hartl F.U., and Bukau B. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12 (1993) 4137-4144
35. Segal G., and Ron E.Z. Regulation and organization of the groE and dnaK operons in eubacteria. FEMS Microbiol. Lett. 138 (1996) 1-10
36. Steenhoudt O., and Vanderleyden J. Azospirillum, a free-living nitrogen-fixing bacterium closely associated with grasses: genetic, biochemical and ecological aspects. FEMS Microbiol. Rev. 24 (2000) 487-506
37. Su S., Stephens B.B., Alexandre G., and Farrand S.K. Lon protease of the alpha-proteobacterium Agrobacterium tumefaciens is required for normal growth, cellular morphology and full virulence. Microbiology 152 (2006) 1197-1207
38. Van Dommellen A., Keijers V., Wollebrants A., and Vanderleyden J. Phenotypic changes resulting from distinct point mutations in the Azospirillum brasilense glnA gene, encoding glutamine synthetase. Appl. Environ. Microbiol. 69 (2003) 5699-5701
39. Veinger L., Diamant S., Buchner J., and Goloubinoff P. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273 (1998) 11032-11037
40. Vetting M.W., Magnet S., Nieves E., Roderick S.L., and Blanchard J.S. A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones. Chem. Biol. 11 (2004) 565-573
41. Vitorino J.C., Steffens M.B.R., Machado H.B., Yates M.G., Souza E.M., and Pedrosa F.O. Potential roles for the glnB and ntrXY genes in Azospirillum brasilense. FEMS Microbiol. Lett. 201 (2001) 199-204
42. Von Mering C., Huynen M., Jaeggi D., Schmidt S., Bork P., and Snel B. STRING: a database of predicted functional associations between proteins. Nucleic Acids Res. 31 (2003) 258-261
43. Wackwitz B., Bongaerts J., Goodman S.D., and Unden G. Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: upstream binding sites and bioenergetic significance. Mol. Gen. Genet. 262 (1999) 876-883
44. + by Azospirillum brasilense grown under nitrogen limitation and excess. J. Bacteriol. 169 (1987) 4211-4214
45. Yu A.Y., and Houry W.A. ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 581 (2007) 3749-3757
46. de Zamaroczy M., Delorme F., and Elmerich C. Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense. Mol. Gen. Genet. 224 (1990) 421-430