Proteasomes and other self-compartmentalizing proteases in prokaryotes

被引：119
作者：
De Mot, R [1 ]
Nagy, I
Walz, J
Baumeister, W
机构：
[1] Katholieke Univ Leuven, Genet Lab, B-3001 Heverlee, Belgium
[2] Max Planck Inst Biochem, Abt Mol Strukturbiol, D-82152 Martinsried, Germany
来源：
TRENDS IN MICROBIOLOGY | 1999年 / 7卷 / 02期
关键词：
D O I：
10.1016/S0966-842X(98)01432-2
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 proteasome represents the major nonlysosomal proteolytic system in eukaryotes. It confines proteolytic activity to an inner compartment that is accessible to unfolded proteins only. The strategy of controlling intracellular breakdown of proteins by self-compartmentalization is also used by different types of prokaryotic energy-dependent proteases. Genomic sequencing data reveal that various combinations of these energy-dependent proteases occur in prokaryotic cells from different lineages.
引用
收藏
页码：88 / 92
页数：5
相关论文
共 33 条
  • [1] Purification and characterization of a proteasome from the hyperthermophilic archaeon Pyrococcus furiosus
    Bauer, MW
    Bauer, SH
    Kelly, RM
    [J]. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1997, 63 (03) : 1160 - 1164
  • [2] The proteasome:: Paradigm of a self-compartmentalizing protease
    Baumeister, W
    Walz, J
    Zühl, F
    Seemuller, E
    [J]. CELL, 1998, 92 (03) : 367 - 380
  • [3] Crystal structure of heat shock locus V (HslV) from Escherichia coli
    Bochtler, M
    Ditzel, L
    Groll, M
    Huber, R
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (12) : 6070 - 6074
  • [4] Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
    Bogyo, M
    McMaster, JS
    Gaczynska, M
    Tortorella, D
    Goldberg, AL
    Ploegh, H
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (13) : 6629 - 6634
  • [5] Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    Cole, ST
    Brosch, R
    Parkhill, J
    Garnier, T
    Churcher, C
    Harris, D
    Gordon, SV
    Eiglmeier, K
    Gas, S
    Barry, CE
    Tekaia, F
    Badcock, K
    Basham, D
    Brown, D
    Chillingworth, T
    Connor, R
    Davies, R
    Devlin, K
    Feltwell, T
    Gentles, S
    Hamlin, N
    Holroyd, S
    Hornby, T
    Jagels, K
    Krogh, A
    McLean, J
    Moule, S
    Murphy, L
    Oliver, K
    Osborne, J
    Quail, MA
    Rajandream, MA
    Rogers, J
    Rutter, S
    Seeger, K
    Skelton, J
    Squares, R
    Squares, S
    Sulston, JE
    Taylor, K
    Whitehead, S
    Barrell, BG
    [J]. NATURE, 1998, 393 (6685) : 537 - +
  • [6] Structure and functions of the 20S and 26S proteasomes
    Coux, O
    Tanaka, K
    Goldberg, AL
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1996, 65 : 801 - 847
  • [7] THE MULTICATALYTIC PROTEINASE (PROSOME) IS UBIQUITOUS FROM EUKARYOTES TO ARCHAEBACTERIA
    DAHLMANN, B
    KOPP, F
    KUEHN, L
    NIEDEL, B
    PFEIFER, G
    HEGERL, R
    BAUMEISTER, W
    [J]. FEBS LETTERS, 1989, 251 (1-2) : 125 - 131
  • [8] Lactacystin, proteasome function, and cell fate
    Fenteany, G
    Schreiber, SL
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (15) : 8545 - 8548
  • [9] Regulatory subunits of energy-dependent proteases
    Gottesman, S
    Maurizi, MR
    Wickner, S
    [J]. CELL, 1997, 91 (04) : 435 - 438
  • [10] The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    Gottesman, S
    Roche, E
    Zhou, YN
    Sauer, RT
    [J]. GENES & DEVELOPMENT, 1998, 12 (09) : 1338 - 1347
1234