Cloning, sequencing, and expression of a Thermomonospora fusca protease gene in Streptomyces lividans.
The major Thermomonospora fusca YX extracellular protease gene (tfpA) was cloned into Escherichia coli and Streptomyces lividans and was sequenced. The open reading frame encoded 375 residues, including a 31-residue potential signal sequence, an N-terminal prosequence containing 150 residues, and the 194-residue mature protease that belongs to the chymotrypsin family. The protease was secreted by S. lividans, but evidence suggested that it was bound to an extracellular protease inhibitor. An inhibitor-deficient mutant was selected to produce protease for purification.
Department of Microbiology, Cornell University, Ithaca, New York 14853, USA.
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D000192:Actinomycetales / Q000201:enzymology* / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009154:Mutation; D015345:Oligonucleotide Probes / Q000235:genetics; D016366:Open Reading Frames; D012697:Serine Endopeptidases / Q000235:genetics*; D013302:Streptomyces / Q000235:genetics
D004269:DNA, Bacterial; D015345:Oligonucleotide Probes; D012697:Serine Endopeptidases