Comparative genomics and functional roles of the ATP-dependent proteases Lon and Clp during cytosolic protein degradation

被引:54
作者
Chandu, D [1 ]
Nandi, D [1 ]
机构
[1] Indian Inst Sci, Dept Biochem, Bangalore 560012, Karnataka, India
关键词
ATP-dependent proteases; Clp; comparative and functional genomics; cytosolic protein degradation; Lon;
D O I
10.1016/j.resmic.2004.06.003
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The general pathway involving adenosine triphosphate (ATP)-dependent proteases and ATP-independent peptidases during cytosolic protein degradation is conserved, with differences in the enzymes utilized, in organisms from different kingdoms. Lon and caseinolytic protease (Clp) are key enzymes responsible for the ATP-dependent degradation of cytosolic proteins in Escherichia coli. Orthologs of E. coli Lon and Clp were searched for, followed by multiple sequence alignment of active site residues, in genomes from seventeen organisms, including representatives from eubacteria, archaea, and eukaryotes. Lon orthologs, unlike ClpP and ClpQ, are present in most organisms studied. The roles of these proteases as essential enzymes and in the virulence of some organisms are discussed. (C) 2004 Elsevier SAS. All rights reserved.
引用
收藏
页码:710 / 719
页数:10
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  • [1] Control of methionine biosynthesis in Escherichia coli by proteolysis
    Biran, D
    Gur, E
    Gollan, L
    Ron, EZ
    [J]. MOLECULAR MICROBIOLOGY, 2000, 37 (06) : 1436 - 1443
  • [2] A non-canonical Lon proteinase lacking the ATPase domain employs the Ser-Lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus
    Birghan, C
    Mundt, E
    Gorbalenya, AE
    [J]. EMBO JOURNAL, 2000, 19 (01) : 114 - 123
  • [3] Lon protease activity causes down-regulation of Salmonella pathogenicity island 1 invasion gene expression after infection of epithelial cells
    Boddicker, JD
    Jones, BD
    [J]. INFECTION AND IMMUNITY, 2004, 72 (04) : 2002 - 2013
  • [4] The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
    Botos, I
    Melnikov, EE
    Cherry, S
    Tropea, JE
    Khalatova, AG
    Rasulova, F
    Dauter, Z
    Maurizi, MR
    Rotanova, TV
    Wlodawer, A
    Gustchina, A
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (09) : 8140 - 8148
  • [5] CHANDU D, 2002, APPL GENOM PROTEOM, V1, P235
  • [6] Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli:: involvement of the yefM-yoeB toxin-antitoxin system
    Christensen, SK
    Maenhaut-Michel, G
    Mine, N
    Gottesman, S
    Gerdes, K
    Van Melderen, L
    [J]. MOLECULAR MICROBIOLOGY, 2004, 51 (06) : 1705 - 1717
  • [7] Protein folding and degradation in bacteria: To degrade or not to degrade? That is the question
    Dougan, DA
    Mogk, A
    Bukau, B
    [J]. CELLULAR AND MOLECULAR LIFE SCIENCES, 2002, 59 (10) : 1607 - 1616
  • [8] Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    Flynn, JM
    Neher, SB
    Kim, YI
    Sauer, RT
    Baker, TA
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  • [9] A membrane-bound archaeal lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteins
    Fukui, T
    Eguchi, T
    Atomi, H
    Imanaka, T
    [J]. JOURNAL OF BACTERIOLOGY, 2002, 184 (13) : 3689 - 3698
  • [10] The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes
    Gaillot, O
    Pellegrini, E
    Bregenholt, S
    Nair, S
    Berche, P
    [J]. MOLECULAR MICROBIOLOGY, 2000, 35 (06) : 1286 - 1294