Cloning, Nucleotide Sequence and Amplified Expression of the Gene Encoding the Extracellular Metallo (Zn) Dd-Peptidase of Streptomyces Albus G

The gene encoding the extracellular metallo (Zn) dd‐peptidase of Streptomyces albus G has been cloned in Escherichia coli DH5αMCR via pBR322 or 325, and then transferred into Streptomyces lividans TK24 via pIJ486, with substantial amplification of the expressed dd‐peptidase. The gene has the informa...

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Bibliographic Details
Published in:FEMS microbiology letters 1990-09, Vol.71 (1‐2), p.215-219
Main Authors: Duez, Colette, Lakaye, Bernard, Houba, Simone, Dusart, Jean, Ghuysen, Jean-Marie
Format: Article
Language:English
Subjects:
active sites
cloning
Cloning of methylated DNA
DD-peptidase
Escherichia coli
gene expression
Microbiology
nucleotide sequence
Streptomyces lividans
Streptomyces plasmid
Streptomyces signal peptides
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Summary:The gene encoding the extracellular metallo (Zn) dd‐peptidase of Streptomyces albus G has been cloned in Escherichia coli DH5αMCR via pBR322 or 325, and then transferred into Streptomyces lividans TK24 via pIJ486, with substantial amplification of the expressed dd‐peptidase. The gene has the information for the synthesis of a 255 amino acid precursor, the amino terminal region of which has the characteristic features of a signal peptide. The primary structure as deduced from nucleotide sequencing confirms that previously determined by chemical methods except for the occurrence of an Asp instead of Asn at position 1 and an additional Ala immediately downstream of Pro67.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1990.tb03825.x