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Bogas,Andréa C.; Watanabe,Maria Angelica E.; Barbosa,Aneli; Vilas-Boas,Laurival A.; Bonatto,Ana C.; Dekker,Robert; Souza,Emanuel M.; Fungaro,Maria Helena P.. |
A beta-glucosidase-like enzyme-encoding gene (bglH) of an endophytic Bacillus pumilus strain (CL16) was cloned using a shotgun genomic library constructed in Escherichia coli. The nucleotide sequence of the entire cloned fragment (2484 bp) was determined and characterized. An incomplete open reading frame (ORF) of 534 bp (ORF1) designated bglP and a complete ORF of 1419 bp (ORF2) designated bglH, located in the fragment, are organized in an operon. The protein deduced from 1419 bp (ORF2) had 472 amino acid residues without a characteristic signal peptide sequence, suggesting that the enzyme is localized in the cytoplasm. The amino acid sequence deduced from bglH gene had high similarity with beta-glucosidases from the glycosyl hydrolase family 1.... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bacillus pumilus; BglH; Glucosidase; Glycosyl hydrolase 1; PTS. |
Ano: 2007 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000100018 |
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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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Soares-Ramos,Juliana R.L.; Ramos,Humberto J.O.; Cruz,Leonardo M.; Chubatsu,Leda S.; Pedrosa,Fábio O.; Rigo,Liu U.; Souza,Emanuel M.. |
Herbaspirillum spp. are endophytic diazotrophic bacteria associated with important agricultural crops. In this work, we analyzed six strains of H. seropedicae (Z78, M2, ZA69, ZA95, Z152, and Z67) and one strain of H. rubrisubalbicans (M4) by restriction fragment length polymorphism (RFLP) using HindIII or DraI restriction endonucleases, random amplified polymorphic DNA (RAPD), and partial sequencing of 16S rDNA. The results of these analyses ascribed the strains studied to three distinct groups: group I, consisting of M2 and M4; group II, of ZA69; and group III, of ZA95, Z78, Z67, and Z152. RAPD fingerprinting showed a higher variability than the other methods, and each strain had a unique electrophoretic pattern with five of the six primers used.... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Herbaspirillum; RAPD; RFLP; Phylogeny; 16S rDNA. |
Ano: 2003 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572003000400019 |
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