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	Provedor de dados BJMBR (3) Autor Araújo,L.M. (2) Chubatsu,L.S. (2) Monteiro,R.A. (2) Nishikawa,C.Y. (2) Pedrosa,F.O. (2) Souza,E.M. (2) Huergo,L.F. (1) Kadowaki,M.A.S. (1) Passaglia,L.M.P. (1) Schrank,A. (1) Schrank,I.S. (1) Sotomaior,P. (1) Steffens,M.B.R. (1) Van Soom,C. (1) Mais... Palavra-chave Azospirillum brasilense (3) NifA protein (3) Biological nitrogen fixation (1) GAF domain (1) Gel shift assay (1) GlnB protein (1) NifA activity (1) NifA antibodies (1) Nitrogen fixation (1) Upstream activator sequence (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Info:eu-repo/semantics/other (1) Ano 2012 (2) 1998 (1) País Brazil (3) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Effect of ATP and 2-oxoglutarate on the in vitro interaction between the NifA GAF domain and the GlnB protein of Azospirillum brasilense BJMBR Sotomaior,P.; Araújo,L.M.; Nishikawa,C.Y.; Huergo,L.F.; Monteiro,R.A.; Pedrosa,F.O.; Chubatsu,L.S.; Souza,E.M.. Azospirillum brasilense is a diazotroph that associates with important agricultural crops and thus has potential to be a nitrogen biofertilizer. The A. brasilense transcription regulator NifA, which seems to be constitutively expressed, activates the transcription of nitrogen fixation genes. It has been suggested that the nitrogen status-signaling protein GlnB regulates NifA activity by direct interaction with the NifA N-terminal GAF domain, preventing the inhibitory effect of this domain under conditions of nitrogen fixation. In the present study, we show that an N-terminal truncated form of NifA no longer required GlnB for activity and lost regulation by ammonium. On the other hand, in trans co-expression of the N-terminal GAF domain inhibited the... Tipo: Info:eu-repo/semantics/article Palavras-chave: Azospirillum brasilense; NifA protein; GlnB protein; GAF domain; Nitrogen fixation. Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2012001200005 Expression and characterization of an N-truncated form of the NifA protein of Azospirillum brasilense BJMBR Nishikawa,C.Y.; Araújo,L.M.; Kadowaki,M.A.S.; Monteiro,R.A.; Steffens,M.B.R.; Pedrosa,F.O.; Souza,E.M.; Chubatsu,L.S.. Azospirillum brasilense is a nitrogen-fixing bacterium associated with important agricultural crops such as rice, wheat and maize. The expression of genes responsible for nitrogen fixation (nif genes) in this bacterium is dependent on the transcriptional activator NifA. This protein contains three structural domains: the N-terminal domain is responsible for the negative control by fixed nitrogen; the central domain interacts with the RNA polymerase σ54 co-factor and the C-terminal domain is involved in DNA binding. The central and C-terminal domains are linked by the interdomain linker (IDL). A conserved four-cysteine motif encompassing the end of the central domain and the IDL is probably involved in the oxygen-sensitivity of NifA. In the present study,... Tipo: Info:eu-repo/semantics/other Palavras-chave: Biological nitrogen fixation; Azospirillum brasilense; NifA protein. Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2012000200004 Purification and binding analysis of the nitrogen fixation regulatory NifA protein from Azospirillum brasilense BJMBR Passaglia,L.M.P.; Van Soom,C.; Schrank,A.; Schrank,I.S.. NifA protein activates transcription of nitrogen fixation operons by the alternative sigma54 holoenzyme form of RNA polymerase. This protein binds to a well-defined upstream activator sequence (UAS) located at the -200/-100 position of nif promoters with the consensus motif TGT-N10-ACA. NifA of Azospirillum brasilense was purified in the form of a glutathione-S-transferase (GST)-NifA fusion protein and proteolytic release of GST yielded inactive and partially soluble NifA. However, the purified NifA was able to induce the production of specific anti-A. brasilense NifA-antiserum that recognized NifA from A. brasilense but not from K. pneumoniae. Both GST-NifA and NifA expressed from the E. coli tac promoter are able to activate transcription from the nifHDK... Tipo: Info:eu-repo/semantics/article Palavras-chave: NifA protein; NifA antibodies; Azospirillum brasilense; Gel shift assay; NifA activity; Upstream activator sequence. Ano: 1998 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998001100001 Registros recuperados: 3 Primeira ... 1 ... Última

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