Ubiquitin found in the archaebacterium Thermoplasma acidophilum

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Abstract
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.