A rubrerythrin-like oxidative stress protein of Clostridium acetobutylicum is encoded by a duplicated gene and identical to the heat shock protein Hsp21

被引:30
作者
May, A [1 ]
Hillmann, F [1 ]
Riebe, O [1 ]
Fischer, RM [1 ]
Bahl, H [1 ]
机构
[1] Univ Rostock, Inst Biol Sci, Div Microbiol, D-18051 Rostock, Germany
关键词
oxidative stress; heat shock; anaerobic; Clostridium; flavoprotein;
D O I
10.1016/j.femsle.2004.07.042
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Comparison of the N-terminus of the heat shock protein Hsp21 of Clostridium acetobutylicum with proteins predicted to be encoded by the genome of this bacterium revealed that this stress protein is encoded by two almost identical open reading frames CAC3597 and CAC3598. These genes encode a rubrerythrin-like protein with the rubredoxin-like FeS4 domain at the N-terminus and the ferritin-like diiron domain (rubrerythrin domain) at the C-terminus. Thus, the order of the two putative functional domains is reversed compared to "normal" rubrerythrins. This protein is proposed to be involved in the oxidative stress response of strict anaerobic bacteria. Northern blot analysis indicated that hsp21 is induced by heat and oxidative stress (air, H2O2). Hsp21 of C acetobutylicum can be considered as a "reverse" rubrerythrin and a role of this stress protein, which is conserved among clostridia and other strict anaerobic bacteria, in the heat and oxidative stress response is proposed. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:249 / 254
页数:6
相关论文
共 16 条
[1]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[2]  
BAHL H, 1995, FEMS MICROBIOL REV, V17, P341, DOI 10.1016/0168-6445(95)00007-Y
[3]   The genome sequence of Clostridium tetani, the causative agent of tetanus disease [J].
Brüggemann, H ;
Bäumer, S ;
Fricke, WF ;
Wiezer, A ;
Liesegang, H ;
Decker, I ;
Herzberg, C ;
Martínez-Arias, R ;
Merkl, R ;
Henne, A ;
Gottschalk, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (03) :1316-1321
[4]   NADH peroxidase activity of rubrerythrin [J].
Coulter, ED ;
Shenvi, NV ;
Kurtz, DM .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1999, 255 (02) :317-323
[5]   Rubrerythrin-catalyzed substrate oxidation by dioxygen and hydrogen peroxide [J].
Coulter, ED ;
Shenvi, NV ;
Beharry, ZM ;
Smith, JJ ;
Prickril, BC ;
Kurtz, DM .
INORGANICA CHIMICA ACTA, 2000, 297 (1-2) :231-241
[6]   The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains [J].
deMare, F ;
Kurtz, DM ;
Nordlund, P .
NATURE STRUCTURAL BIOLOGY, 1996, 3 (06) :539-546
[7]  
JOSEPH H, 1993, THESIS U GOTTINGEN
[8]   Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris:: a novel oxidative stress protection system [J].
Lumppio, HL ;
Shenvi, NV ;
Summers, AO ;
Voordouw, G ;
Kurtz, DM .
JOURNAL OF BACTERIOLOGY, 2001, 183 (01) :101-108
[9]   MOLECULAR CHARACTERIZATION OF THE DNAK GENE REGION OF CLOSTRIDIUM-ACETOBUTYLICUM, INCLUDING GRPE, DNAJ, AND A NEW HEAT-SHOCK GENE [J].
NARBERHAUS, F ;
GIEBELER, K ;
BAHL, H .
JOURNAL OF BACTERIOLOGY, 1992, 174 (10) :3290-3299
[10]   SYNTHESIS OF HEAT-SHOCK PROTEINS IN THERMOANAEROBACTERIUM THERMASULFURIGENES EM1 (CLOSTRIDIUM THERMOSULFUROGENES EM1) [J].
NARBERHAUS, F ;
PICH, A ;
BAHL, H .
CURRENT MICROBIOLOGY, 1994, 29 (01) :13-18