The chaperones of the archaeon Thermoplasma acidophilum

被引:33
作者
Ruepp, A
Rockel, B
Gutsche, I
Baumeister, W
Lupas, AN
机构
[1] Max Planck Inst Biochem, Dept Mol Struct Biol, D-82152 Martinsried, Germany
[2] GlaxoSmithKline, Prot Bioinformat Grp, Collegeville, PA 19426 USA
关键词
Thermoplasma; archaea; chaperone; thermosome; VAT;
D O I
10.1006/jsbi.2001.4402
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
Chaperones are an essential component of a cell's ability to respond to environmental challenges. Chaperones have been studied primarily in bacteria, but in recent years it has become apparent that some classes of chaperones either are very divergent in bacteria relative to archaea and eukaryotes or are missing entirely. In contrast, a high degree of similarity was found between the chaperonins of archaea and those of the eukaryotic cytosol, which has led to the establishment of archaeal model systems. The archaeon most extensively used for such studies is Thermoplasma acidophilum, which thrives at 59 degreesC and pH 2. Here we review information on its chaperone complement in light of the recently determined genome sequence. (C) 2001 Academic Press.
引用
收藏
页码:126 / 138
页数:13
相关论文
共 102 条
[1]
Polypeptide binding of Escherichia coli FtsH (HflB) [J].
Akiyama, Y ;
Ehrmann, M ;
Kihara, A ;
Ito, K .
MOLECULAR MICROBIOLOGY, 1998, 28 (04) :803-812
[2]
Recurrent paralogy in the evolution of archaeal chaperonins [J].
Archibald, JM ;
Logsdon, JM ;
Doolittle, WF .
CURRENT BIOLOGY, 1999, 9 (18) :1053-1056
[3]
Crystal structure of the Sec18p N-terminal domain [J].
Babor, SM ;
Fass, D .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (26) :14759-14764
[4]
HFLB, A NEW ESCHERICHIA-COLI LOCUS REGULATING LYSOGENY AND THE LEVEL OF BACTERIOPHAGE LAMBDA-CII PROTEIN [J].
BANUETT, F ;
HOYT, MA ;
MCFARLANE, L ;
ECHOLS, H ;
HERSKOWITZ, I .
JOURNAL OF MOLECULAR BIOLOGY, 1986, 187 (02) :213-224
[5]
PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone [J].
Benaroudj, N ;
Goldberg, AL .
NATURE CELL BIOLOGY, 2000, 2 (11) :833-839
[6]
Beyer A, 1997, PROTEIN SCI, V6, P2043
[7]
Crystal structure of the β-apical domain of the thermosome reveals structural plasticity in the protrusion region [J].
Bosch, G ;
Baumeister, W ;
Essen, LO .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 301 (01) :19-25
[8]
The Hsp70 and Hsp60 chaperone machines [J].
Bukau, B ;
Horwich, AL .
CELL, 1998, 92 (03) :351-366
[9]
Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii [J].
Bult, CJ ;
White, O ;
Olsen, GJ ;
Zhou, LX ;
Fleischmann, RD ;
Sutton, GG ;
Blake, JA ;
FitzGerald, LM ;
Clayton, RA ;
Gocayne, JD ;
Kerlavage, AR ;
Dougherty, BA ;
Tomb, JF ;
Adams, MD ;
Reich, CI ;
Overbeek, R ;
Kirkness, EF ;
Weinstock, KG ;
Merrick, JM ;
Glodek, A ;
Scott, JL ;
Geoghagen, NSM ;
Weidman, JF ;
Fuhrmann, JL ;
Nguyen, D ;
Utterback, TR ;
Kelley, JM ;
Peterson, JD ;
Sadow, PW ;
Hanna, MC ;
Cotton, MD ;
Roberts, KM ;
Hurst, MA ;
Kaine, BP ;
Borodovsky, M ;
Klenk, HP ;
Fraser, CM ;
Smith, HO ;
Woese, CR ;
Venter, JC .
SCIENCE, 1996, 273 (5278) :1058-1073
[10]
A six-stranded double-psi β barrel is shared by several protein superfamilies [J].
Castillo, RM ;
Mizuguchi, K ;
Dhanaraj, V ;
Albert, A ;
Blundell, TL ;
Murzin, AG .
STRUCTURE, 1999, 7 (02) :227-236