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Isolation and characterization of the gene encoding a novel, thermostable serine proteinase from the mould Tritirachium album Limber
Author(s) -
Samal B. B.,
Karan B.,
Boone T. C.,
Osslund T. D.,
Chen K. K.,
Stabinsky Y.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb00558.x
Subject(s) - biology , proteinase 3 , biochemistry , subtilisin , serine , proteinase k , amino acid , serine proteinase inhibitors , microbiology and biotechnology , gene , proteases , complementary dna , cdna library , peptide sequence , protease , enzyme , serine protease , genetics , antibody , autoantibody
Summary A number of proteinases are induced and secreted into the culture medium of Tritirachium album Limber when the nitrogen source is limited to exogenous proteins. We have constructed a cDNA library using the polyadenylated RNA isolated during the nutritional induction with bovine serum albumin. A full‐length clone of a gene for a new proteinase (named proteinase R) was identified from this library. This clone contained sequences coding for the 108‐amino‐acid prepro‐leader as well as for the 279‐amino‐acid mature preoteinase. Proteinase R apparently belongs to the subtilisin group of serine proteases that contains disulphide bonds. Homology between proteinase R and proteinase K was found to be about 87% at the nucleotide as well as at the amino acid level. The Brookhaven Protein Data Base co‐ordinate file of proteinase K was used as a template to study the proteinase R substitutions in three‐dimensional space. The majority of the substitutions of proteinase R with respect to proteinase K were found to be on the exterior of the protein model.