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| Souza,André L.F.; Chubatsu,Leda S.; Souza,Emanuel M.; Pedrosa,Fábio O.; Monteiro,Rose A.; Rego,Fabiane G.M.; Rigo,Liu U.. |
| In prokaryotes molybdenum is taken up by a high-affinity ABC-type transporter system encoded by the modABC genes. The endophyte β-Proteobacterium Herbaspirillum seropedicae has two modABC gene clusters and two genes encoding putative Mo-dependent regulator proteins (ModE1 and ModE2). Analysis of the amino acid sequence of the ModE1 protein of H. seropedicae revealed the presence of an N-terminal domain containing a DNA-binding helix-turn-helix motif (HTH) and a C-terminal domain with a molybdate-binding motif. The second putative regulator protein, ModE2, contains only the helix-turn-helix motif, similar to that observed in some sequenced genomes. We cloned the modE1 (810 bp) and modE2 (372 bp) genes and expressed them in Escherichia coli as His-tagged... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Herbaspirillum seropedicae; ModE1 protein; ModE2 protein. |
| Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572008000400022 |
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