Cloning and characterization of a gene encoding extracellular metalloprotease from Streptomyces lividans

• Published in: Gene Vol. 111; no. 1; p. 125
• Main Authors: Lichenstein, H S, Busse, L A, Smith, G A, Narhi, L O, McGinley, M O, Rohde, M F, Katzowitz, J L, Zukowski, M M
• Format: Journal Article
• Language: English
• Published: Netherlands 01-02-1992
• Subjects: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Cloning, Molecular; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; Genes, Bacterial; Genomic Library; Hydrogen-Ion Concentration; Metalloendopeptidases - genetics; Metalloendopeptidases - metabolism; Molecular Sequence Data; Restriction Mapping; Sequence Alignment; Streptomyces - enzymology; Streptomyces - genetics; Temperature
• DOI: 10.1016/0378-1119(92)90613-t
• ISSN: 0378-1119

The prt gene, encoding a protease (Prt) from Streptomyces lividans TK24, was cloned and sequenced. An S. lividans host with plasmid-borne prt secreted 200 micrograms/ml of a 22-kDa Prt into the culture medium. Prt is classified as a metalloprotease since its activity is significantly inhibited by 1,10-phenanthroline or EDTA. The region upstream from prt codes for an incomplete open reading frame (ORF) oriented opposite to prt. This ORF has a strong similarity to a gene family (lysR) whose members regulate the transcription of structural genes required for either biosynthesis or degradation.