Reference : Nucleotide sequence of the gene encoding the Streptomyces albus G β-lactamase precursor
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/81288
Nucleotide sequence of the gene encoding the Streptomyces albus G β-lactamase precursor
English
Dehottay, Philippe [Université de Liège - ULg > > Service de Microbiologie > >]
Dusart, Jean [Université de Liège - ULg > > Service de Microbiologie > >]
De Meester, Fabien [Université de Liège - ULg > > Service de Microbiologie > >]
Joris, Bernard mailto [Université de Liège - ULg > > Service de Microbiologie > >]
Van Beeumen, Jozef [Rijksuniversiteit-Gent > > Laboratorium voor Microbiologie > >]
Erpicum, Thomas [Université de Liège - ULg > > Service de Microbiologie > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > > Service de Microbiologie > >]
15-Jul-1987
European Journal of Biochemistry
Blackwell Science
166
2
345-350
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] amino acid sequence ; base sequence ; binding sites ; dna restriction enzymes ; enzyme precursors/*genetics ; genes ; genes, bacterial ; plasmids ; promoter regions, genetic ; streptomyces/enzymology/*genetics ; terminator regions, genetic ; beta-Lactamases/*genetics
[en] A 1400-base DNA fragment, which contains the gene encoding the extracellular active-site serine beta-lactamase of Streptomyces albus G previously cloned into Streptomyces lividans [Dehottay et al. (1986) Gene 42, 31-36], was sequenced. The gene codes for a 314-amino-acid precursor, the N-terminal region of which has the characteristics of a signal peptide. The beta-lactamase as excreted by the host strain S. lividans PD6 has a ragged N-terminus, indicating either the presence of a leader peptidase of poor specificity or the action of an aminopeptidase. The primary structure (as deduced from the nucleotide sequence) was confirmed by amino acid sequencing of a 16-residue stretch at the amino terminus of the protein, a 12-residue stretch containing the active-site serine [De Meester et al. (1987) Biochem. J. 244, 427-432] and a 23-residue stretch obtained by trypsin digestion of the protein. The beta-lactamase belongs to class A, has three half-cystine residues (one of which occurs on the amino side of the active-site serine) and is inactivated by thiol reagents. Putative ribosome binding site and terminator region were identified.
Researchers ; Professionals
http://hdl.handle.net/2268/81288

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