PROTEOLYSIS - THE PROTEASOME - A PROTEIN-DEGRADING ORGANELLE

被引：135
作者：
RUBIN, DM
FINLEY, D
机构：
[1] Department of Cell Biology, Harvard Medical School, Boston, MA 02115
来源：
CURRENT BIOLOGY | 1995年 / 5卷 / 08期
关键词：
D O I：
10.1016/S0960-9822(95)00172-2
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：
The crystal structure of the proteasome suggests that degradation of ubiquitin-protein conjugates is achieved by unfolding the protein substrate and translocating it through a channel into a peptidase-containing chamber.
引用
收藏
页码：854 / 858
页数：5
相关论文
共 32 条
  • [1] THE UBIQUITIN-PROTEASOME PROTEOLYTIC PATHWAY
    CIECHANOVER, A
    [J]. CELL, 1994, 79 (01) : 13 - 21
  • [2] DEMARTINO GN, 1994, J BIOL CHEM, V269, P20878
  • [3] DEVEREAUX O, 1994, J BIOL CHEM, V269, P7059
  • [4] SUBUNITS OF THE REGULATORY COMPLEX OF THE 26S PROTEASE
    DUBIEL, W
    FERRELL, K
    RECHSTEINER, M
    [J]. MOLECULAR BIOLOGY REPORTS, 1995, 21 (01) : 27 - 34
  • [5] ATP-DEPENDENT INCORPORATION OF 20S PROTEASE INTO THE 26S COMPLEX THAT DEGRADES PROTEINS CONJUGATED TO UBIQUITIN - (PROTEIN BREAKDOWN MULTICATALYTIC PROTEINASE COMPLEX)
    EYTAN, E
    GANOTH, D
    ARMON, T
    HERSHKO, A
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1989, 86 (20) : 7751 - 7755
  • [6] MHC CLASS-I EXPRESSION IN MICE LACKING THE PROTEASOME SUBUNIT LMP-7
    FEHLING, HJ
    SWAT, W
    LAPLACE, C
    KUHN, R
    RAJEWSKY, K
    MULLER, U
    VONBOEHMER, H
    [J]. SCIENCE, 1994, 265 (5176) : 1234 - 1237
  • [7] INHIBITION OF PROTEASOME ACTIVITIES AND SUBUNIT-SPECIFIC AMINO-TERMINAL THREONINE MODIFICATION BY LACTACYSTIN
    FENTEANY, G
    STANDAERT, RF
    LANE, WS
    CHOI, S
    COREY, EJ
    SCHREIBER, SL
    [J]. SCIENCE, 1995, 268 (5211) : 726 - 731
  • [8] ROLE OF PROTEASOMES IN ANTIGEN PRESENTATION
    GACZYNSKA, M
    ROCK, KL
    GOLDBERG, AL
    [J]. ENZYME & PROTEIN, 1993, 47 (4-6) : 354 - 369
  • [9] GOLDBERG AL, 1994, METHOD ENZYMOL, V244, P350
  • [10] HEINEMEYER W, 1993, J BIOL CHEM, V268, P5115
1234