Decelerated degradation of short peptides by the 20S proteasome

FEBS Letters

Dolenc, Iztok¹  Baumeister, Wolfgang¹  Seemüller, Erika¹ 

[1] Max-Planck-Institut fur Biochemie, Am Klopferspitz 18a, Martinsried D-82152, Germany

关键词: Proteasome;    Molecular ruler;    Protein degradation;    Thermoplasma acidophilum;    AMC;    7-amino-4-methylcoumarin;    HPLC;    high performance liquid chromatography;    IPTG;    isopropyl-1-thio-β-d-galactopyranoside;    Ni-NTA;    nickel-nitrilotriacetic acid;    RP;    reverse phase;    Suc;    succinyl;   

DOI  :  10.1016/S0014-5793(98)01010-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown