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Decelerated degradation of short peptides by the 20S proteasome
Author(s) -
Dolenc Iztok,
Seemüller Erika,
Baumeister Wolfgang
Publication year - 1998
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(98)01010-2
Subject(s) - thermoplasma acidophilum , proteasome , cleavage (geology) , peptide , chemistry , residue (chemistry) , degradation (telecommunications) , biochemistry , proteolysis , protein degradation , biophysics , biology , enzyme , paleontology , telecommunications , fracture (geology) , computer science
Based on a twelve residue master peptide comprising all five specific cleavage sites defined for the proteasome, a set of variant peptides was generated in order to probe specificity and to elucidate the mechanism which determines product size. It is shown that the rate of degradation by the 20S proteasome from Thermoplasma acidophilum depends critically on the length of the peptide substrate. Peptides of 14 residues and longer are degraded much faster than shorter peptides although the sites of cleavage remain unchanged. The decelerated degradation of peptides shorter than 14 residues explains the accumulation of products with an average length of seven to nine residues.