Molecular cloning and comparative analysis of four beta-galactosidase genes from Bifidobacterium bifidum NCIMB41171

Goulas, T.K., Goulas, A.K., Tzortzis, G. and Gibson, G.R. ORCID: https://orcid.org/0000-0002-0566-0476 (2007) Molecular cloning and comparative analysis of four beta-galactosidase genes from Bifidobacterium bifidum NCIMB41171. Applied Microbiology and Biotechnology, 76 (6). pp. 1365-1372. ISSN 0175-7598 doi: 10.1007/s00253-007-1099-1

Abstract/Summary

Bifidobacterium bifidum NCIMB41171 carries four genes encoding different beta-galactosidases. One of them, named bbgIII, consisted of an open reading frame of 1,935 amino acid (a.a.) residues encoding a protein with a multidomain structure, commonly identified on cell wall bound enzymes, having a signal peptide, a membrane anchor, FIVAR domains, immunoglobulin Ig-like and discoidin-like domains. The other three genes, termed bbgI, bbgII and bbgIV, encoded proteins of 1,291, 689 and 1,052 a.a. residues, respectively, which were most probably intracellularly located. Two cases of protein evolution between strains of the same species were identified when the a.a. sequences of the BbgI and BbgIII were compared with homologous proteins from B. bifidum DSM20215. The homologous proteins were found to be differentiated at the C-terminal a.a. part either due to a single nucleotide insertion or to a whole DNA sequence insertion, respectively. The bbgIV gene was located in a gene organisation surrounded by divergently transcribed genes putatively for sugar transport (galactoside-symporter) and gene regulation (LacI-transcriptional regulator), a structure that was found to be highly conserved in B. longum, B. adolescentis and B. infantis, suggesting optimal organisation shared amongst those species.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/13352
Item Type	Article
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
Uncontrolled Keywords	B. bifidum, bifidobacteria, galactosidase, beta-galactosidase, protein, evolution, HUMAN GASTROINTESTINAL-TRACT, GLYCOSIDE HYDROLASE FAMILY, LONGUM, IDENTIFICATION, PREDICTION, SEQUENCE, GENOME, PHOSPHORYLASE, PURIFICATION, EXPRESSION
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