Decelerated degradation of short peptides by the 20S proteasome

被引:52
作者
Dolenc, I
Seemüller, E
Baumeister, W
机构
[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany
[2] Jozef Stefan Inst, Dept Biochem & Mol Biol, Ljubljana, Slovenia
关键词
proteasome; molecular ruler; protein degradation; Thermoplasma acidophilum;
D O I
10.1016/S0014-5793(98)01010-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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, (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:357 / 361
页数:5
相关论文
共 17 条
[1]   Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum [J].
Akopian, TN ;
Kisselev, AF ;
Goldberg, AL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (03) :1791-1798
[2]   The proteasome:: Paradigm of a self-compartmentalizing protease [J].
Baumeister, W ;
Walz, J ;
Zühl, F ;
Seemuller, E .
CELL, 1998, 92 (03) :367-380
[3]   Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes [J].
Bogyo, M ;
Shin, S ;
McMaster, JS ;
Ploegh, HL .
CHEMISTRY & BIOLOGY, 1998, 5 (06) :307-320
[4]   BIOCHEMICAL-PROPERTIES OF THE PROTEASOME FROM THERMOPLASMA-ACIDOPHILUM [J].
DAHLMANN, B ;
KUEHN, L ;
GRZIWA, A ;
ZWICKL, P ;
BAUMEISTER, W .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 208 (03) :789-797
[5]   DEGRADATION OF OXIDIZED INSULIN B-CHAIN BY THE MULTIPROTEINASE COMPLEX MACROPAIN (PROTEASOME) [J].
DICK, LR ;
MOOMAW, CR ;
DEMARTINO, GN ;
SLAUGHTER, CA .
BIOCHEMISTRY, 1991, 30 (10) :2725-2734
[6]   Effects of major-histocompatibility-complex-encoded subunits on the peptidase and proteolytic activities of human 20S proteasomes - Cleavage of proteins and antigenic peptides [J].
Ehring, B ;
Meyer, TH ;
Eckerskorn, C ;
Lottspeich, F ;
Tampe, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 235 (1-2) :404-415
[7]   Functions of the proteasome in antigen presentation [J].
Goldberg, AL ;
Gaczynska, M ;
Grant, E ;
Michalek, M ;
Rock, KL .
COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, 1995, 60 :479-490
[8]   GENERATION, TRANSLOCATION, AND PRESENTATION OF MHC CLASS I-RESTRICTED PEPTIDES [J].
HEEMELS, MT ;
PLOEGH, H .
ANNUAL REVIEW OF BIOCHEMISTRY, 1995, 64 :463-491
[9]   Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes [J].
Kisselev, AF ;
Akopian, TN ;
Goldberg, AL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (04) :1982-1989
[10]   CRYSTAL-STRUCTURE OF THE 20S PROTEASOME FROM THE ARCHAEON T-ACIDOPHILUM AT 3.4-ANGSTROM RESOLUTION [J].
LOWE, J ;
STOCK, D ;
JAP, R ;
ZWICKL, P ;
BAUMEISTER, W ;
HUBER, R .
SCIENCE, 1995, 268 (5210) :533-539