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Ubiquitin found in the archaebacterium Thermoplasma acidophilum
Author(s) -
Wolf Stefan,
Lottspeich Friedrich,
Baumeister Wolfgang
Publication year - 1993
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(93)81757-q
Subject(s) - thermoplasma acidophilum , ubiquitin , proteolysis , biology , biochemistry , proteasome , amino acid , deubiquitinating enzyme , peptide sequence , function (biology) , gel electrophoresis , enzyme , genetics , gene
Systematic N‐terminal sequencing of the low molecular weight proteins from Thermoplasma acidophilum separated by two‐dimensional polyacrylamide get electrophoresis led to the discovery of a polypeptide with an apparent M r of 4.5 kDa identical as its first 18 amino acid residues to human ubiquitin. The occurrence of ubiquitin and proteasomes in an archaebacterium strongly suggests that ATP‐ubiquitin‐dependent proteolysis is a cellular function that developed early in evolution.