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Cloning and sequence analysis of pituitary cDNA encoding the β‐subunit of Xenopus proteasome
Author(s) -
van Riel Maarten C.H.M.,
Martens Gerard J.M.
Publication year - 1991
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(91)81098-s
Subject(s) - protein subunit , complementary dna , xenopus , proteasome , open reading frame , peptide sequence , amino acid , biochemistry , cloning (programming) , biology , microbiology and biotechnology , chemistry , gene , computer science , programming language
The proteasome is a multicatalytic proteinase composed of a number of non‐identical subunits. A Xenopus pituitary cDNA was isolated and found to code for the β‐subunit of proteasome. The amino acid sequence deduced from the open reading frame consisted of 215 amino acid residues with a calculated molecular weight of 23 979. A comparative structural analysis indicated that the proteasome subunits can be divided into two groups with the same evolutionary origin. One group consists of subunits with an N‐terminally blocked residue and includes components C2, C3, C8 and C9, while the second group of non‐blocked proteins includes components C5 and the β‐subunit.