Reference : Transcriptional Analysis of the dd-Peptidase/Penicillin-Binding Protein-Encoding dac Gen...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/76273
Transcriptional Analysis of the dd-Peptidase/Penicillin-Binding Protein-Encoding dac Gene of Streptomyces R61: Use of the Promoter and Signal Sequences in a Secretion Vector
English
Piron-Fraipont, Claudine [Université de Liège - ULg > Institut de Chimie > Département de Microbiologie > >]
Lenzini, Mauro V [Université de Liège - ULg > Insitut de Chimie > Département de Microbiologie > >]
Dusart, Jean [Université de Liège - ULg > Institut de Chimie > Département de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Département de Microbiologie > > >]
1-Aug-1990
Molecular & General Genetics
Springer
223
114-120
Yes (verified by ORBi)
International
0026-8925
[en] In vivo promoter probing ; S1 mapping ; Protein secretion ; R-TEM beta-lactamase ; Streptomyces ; R61 DD-peptidase/PBP
[en] The promoter region of the gene encoding the extracellular DD-peptidase/penicillin-binding protein of Streptomyces R61 has been identified by in vivo promoter probing and S1 mapping. A secretion vector, pDML116, was constructed by inserting into the multicopy Streptomyces plasmid pIJ702, a 247 bp DNA sequence that contained the transcriptional, translational and secretory signals and the 12 amino acid N-terminal region-encoding sequence of the mature Streptomyces DD-peptidase/penicillin-binding protein. Insertion, downstream of this 247 bp segment, of the Streptomyces R61 DD-peptidase-encoding gene or the Escherichia coli R-TEM beta-lactamase-encoding gene yielded plasmids pDML120 and pDML128, respectively, which allowed expression and secretion of the relevant enzymes by Streptomyces lividans. The maximal secretion levels obtained were 42 mg protein/ml for the autologous Streptomyces DD-peptidase and 0.9 mg protein/ml for the heterologous E. coli beta-lactamase.
Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/76273
also: http://hdl.handle.net/2268/81266
10.1007/BF00315803

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