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cDNA cloning of rat proteasome subunit RC1, a homologue of RING10 located in the human MHC class II region
Author(s) -
Aki Masashi,
Tamura Tomohiro,
Tokunaga Fuminori,
Iwanaga Sadaaki,
Kawamura Yoshihiro,
Shimbara Naoki,
Kagawa Susumu,
Tanaka Keiji,
Ichihara Akira
Publication year - 1992
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(92)80211-x
Subject(s) - complementary dna , open reading frame , peptide sequence , protein subunit , biology , microbiology and biotechnology , mhc class i , nucleic acid sequence , gene , major histocompatibility complex , amino acid , molecular cloning , cloning (programming) , exon , cdna library , protein primary structure , proteasome , mhc class ii , biochemistry , computer science , programming language
The nucleotide sequence of a cDNA that encodes a new subunit, named RC1, of rat proteasomes (multicatalytic proteinase complexes) has been determined. The polypeptide predicted from the open reading frame consisted of 208 amino acid residues with a calculated molecular mass of 23,130, which is consistent with the size obtained by electrophoretic analysis of purified RC1. The partial amino acid sequences of several fragments of RC1, obtained by protein chemical analyses, were found to be in excellent accordance with those deduced from the cDNA sequence. Surprisingly, the overall structure of RC1 was found to be almost identical to that of recently isolated RING10, whose gene is located in the class II region of the human MHC gene cluster. This finding suggests that RC1 is a homologue of human RING10, supporting the proposal that proteasomes are involved in the antigen processing pathway.