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Identification, molecular cloning, and characterization of subunit 11 of the human 26S proteasome
Author(s) -
Hoffman Laura,
Gorbea Carlos,
Rechsteiner Martin
Publication year - 1999
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/s0014-5793(99)00403-2
Subject(s) - proteasome , protein subunit , cloning (programming) , identification (biology) , characterization (materials science) , molecular cloning , computational biology , biochemistry , chemistry , biology , gene , peptide sequence , nanotechnology , materials science , computer science , botany , programming language
We sequenced five peptides from subunit 11 (S11), a 43 kDa protein of the human 26S proteasome, and used this information to clone its cDNA. The S11 cDNA encodes a 376 amino acid protein with a p I of 5.6 and a molecular mass of 42.9 kDa. Translation of S11 RNA in the presence of [ 35 S]methionine produces a radiolabeled protein that co‐migrates with S11 of the human 26S proteasome on SDS‐PAGE. Polyclonal antiserum made against recombinant S11 recognizes a protein of the same size in extracts of bacteria expressing S11 and in purified 26S proteasomes from human red blood cells or rabbit reticulocytes. The S11 sequence does not contain motifs that suggest a biological function. S11 is, however, the human homolog of Rpn9, a recently identified subunit of the yeast 26S proteasome.