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Provedor de dados:  Genet. Mol. Biol.
País:  Brazil
Título:  Structural characterization of the bglH gene encoding a beta-glucosidase-like enzyme in an endophytic Bacillus pumilus strain
Autores:  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.
Data:  2007-01-01
Ano:  2007
Palavras-chave:  Bacillus pumilus
BglH
Glucosidase
Glycosyl hydrolase 1
PTS
Resumo:  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. Over-expression of the B. pumilus bglH gene in E. coli showed a 54 kDa protein whose identity was confirmed by mass spectrometry (MALDI-TOF).
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572007000100018
Editor:  Sociedade Brasileira de Genética
Relação:  10.1590/S1415-47572007000100018
Formato:  text/html
Fonte:  Genetics and Molecular Biology v.30 n.1 2007
Direitos:  info:eu-repo/semantics/openAccess
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