Premium
Cloning and expression of a human pro(tea)some β‐subunit cDNA: A homologue of the yeast PRE4‐subunit essential for peptidylglutamyl‐peptide hydrolase activity
Author(s) -
Will L.H. Gerards,
Frank W.H. Hop,
Ine L.A.M. Hendriks,
H. Bloemendal
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00454-4
Subject(s) - complementary dna , protein subunit , biology , microbiology and biotechnology , open reading frame , cdna library , biochemistry , xenopus , peptide sequence , yeast , peptide , molecular cloning , gene
The cDNA encoding a human prosome β‐subunit (HSBpros26) was isolated from a lymphoma library using the cDNA of the Xenopus homologue as a probe. The cDNA contains an open reading frame encoding a protein of 233 amino acids and a calculated molecular weight of 25,909. Comparison with interspecies homologues of HSBpros26 from Xenopus (XLB), rat (RN3) and yeast (PRE4) reveals a high degree of identity between the β‐subunits except for the N‐terminal end, which is probably cleaved post‐translationally. The complete coding sequence of HSBpros26 has been expressed in E. coli . The produced protein of about 27 kDa reacts with the prosomal monoclonal antibody MCP205, kindly provided by Dr. K. Hendil. The molecular weight of the native protein is about 28 kDa indicating that the protein is present as monomers. Finally partially purified HSBpros26 preparations do not contain any proteolytical activity.