Reference : Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into St...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/6255
Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene
English
Duez, Colette mailto [Université de Liège - ULg > Faculté de médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Fraipont, Claudine mailto [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Joris, Bernard mailto [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Dusart, Jean [Université de Liège - ULg > Faculté de médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Urdea, Mickey S [Chiron Corporation, Emeryville USA > > > >]
Martial, Joseph mailto [Université de Liège - ULg > Faculté de Médecines > Service de Microbiologie appliquée aux sciences pharmaceutiques > > >]
Frère, Jean-Marie [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de médecine > Service de Microbiologie appliquée aux sciences pharmaceutiques > > >]
1987
European Journal of Biochemistry
Blackwell Science
162
509-518
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] Clonage, surexpression ; Séquence ; DD-peptidase ; DNA, Bacterial ; Molecular Sequence Data ; Muramoylpentapeptide Carboxypeptidase/*genetics ; Streptomyces/*enzymology/genetics
[en] An 11450-base DNA fragment containing the gene for the extracellular active-site serine DD-peptidase of Streptomyces R61 was cloned in Streptomyces lividans using the high-copy-number plasmid pIJ702 as vector. Amplified expression of the excreted enzyme was observed. Producing clones were identified with the help of a specific antiserum directed against the pure DD-peptidase. The coding sequence of the gene was then located by hybridization with a specific nucleotide probe and sub-fragments were obtained from which the nucleotide sequence of the structural gene and the putative promoter and terminator regions were determined. The sequence suggests that the gene codes for a 406-amino-acid protein precursor. When compared with the excreted, mature DD-peptidase, this precursor possesses a cleavable 31-amino-acid N-terminal extension which has the characteristics of a signal peptide, and a cleavable 26-amino-acid C-terminal extension. On the basis of the data of Joris et al. (following paper in this journal), the open reading frame coding for the synthesis of the DD-peptidase was established. Comparison of the primary structure of the Streptomyces R61 DD-peptidase with those of several active-site serine β-lactamases and penicillin-binding proteins of Escherichia coli shows homology in those sequences that comprise the active-site serine residue. When the comparison is broadened to the complete amino acid sequences, significant homology is observed only for the pair Streptomyces R61 DD-peptidase/Escherichia coli ampC β-lactamase (class C). Since the Streptomyces R61 DD-peptidase and β-lactamases of class A have very similar three-dimensional structures [Kelly et al. (1986) Science (Wash. DC) 231, 1429–1431; Samraoui et al. (1986) Nature (Lond.) 320, 378–380], it is concluded that these tertiary features are probably also shared by the β-lactamases of class C, i.e. that the Streptomyces R61 DD-peptidase and the β-lactamases of classes A and C are related in an evolutionary sense.
Researchers ; Professionals
http://hdl.handle.net/2268/6255
10.1111/j.1432-1033.1987.tb10669.x

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