The role of the hybrid cluster protein in oxidative stress defense

被引:72
作者
Almeida, Claudia C. [1 ]
Romao, Celia V. [1 ]
Lindley, Peter F. [1 ]
Teixeira, Miguel [1 ]
Saraiva, Ligia M. [1 ]
机构
[1] Univ Nova Lisboa, Inst Tecnol Quim & Biol, P-2780157 Oeiras, Portugal
关键词
D O I
10.1074/jbc.M605888200
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
Hybrid cluster proteins (HCP) contain two types of Fe/S clusters, namely a [4Fe-4S](2+/1+) or [2Fe-2S](2+/1+) cluster and a novel type of hybrid cluster, [4Fe-2S-2O], in the as-isolated state. Although first isolated from anaerobic sulfate-reducing bacteria, the analysis of the genomic sequences reveals that genes encoding putative hybrid cluster proteins are present in a wide range of organisms, aerobic, anaerobic, or facultative, from the Bacteria, Archaea, and Eukarya domains. Despite a detailed spectroscopic and structural characterization, the precise physiological function of these proteins remained unknown. The present work shows that the transcription of the Escherichia coli hcp gene is induced by hydrogen peroxide, and this induction is regulated by the redox-sensitive transcriptional activator, OxyR. The E. coli hcp mutant strain exhibits higher sensitivity to hydrogen peroxide, a behavior that reverts to the wild type phenotype once a plasmid carrying the hcp gene is reintroduced. Furthermore, the purified HCPs from E. coli and Desulfovibrio desulfuricans ATCC 27774 show an alternative enzymatic activity, which under physiological conditions exhibited K-m values for hydrogen peroxide (similar to 0.3 mM) within the range of other peroxidases. Altogether, the results reveal that HCP is involved in oxidative stress protection.
引用
收藏
页码:32445 / 32450
页数:6
相关论文
共 29 条
[1]   Evolution of four gene families with patchy phylogenetic distributions: influx of genes into protist genomes [J].
Andersson, Jan O. ;
Hirt, Robert P. ;
Foster, Peter G. ;
Roger, Andrew J. .
BMC EVOLUTIONARY BIOLOGY, 2006, 6
[2]   Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough):: X-ray structures at high resolution using synchrotron radiation [J].
Aragao, D ;
Macedo, S ;
Mitchell, EP ;
Romao, CV ;
Liu, MY ;
Frazao, C ;
Saraiva, LM ;
Xavier, AV ;
LeGall, J ;
van Dongen, WMAM ;
Hagen, WR ;
Teixeira, M ;
Carrondo, MA ;
Lindley, P .
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2003, 8 (05) :540-548
[3]  
Ausubel FM, 1995, CURRENT PROTOCOLS MO
[4]   Global transcriptome analysis of Shewanella oneidensis MR-1 exposed to different terminal electron acceptors [J].
Beliaev, AS ;
Klingeman, DM ;
Klappenbach, JA ;
Wu, L ;
Romine, MF ;
Tiedje, JA ;
Nealson, KH ;
Fredrickson, JK ;
Zhou, J .
JOURNAL OF BACTERIOLOGY, 2005, 187 (20) :7138-7145
[5]   The complete genome sequence of Escherichia coli K-12 [J].
Blattner, FR ;
Plunkett, G ;
Bloch, CA ;
Perna, NT ;
Burland, V ;
Riley, M ;
ColladoVides, J ;
Glasner, JD ;
Rode, CK ;
Mayhew, GF ;
Gregor, J ;
Davis, NW ;
Kirkpatrick, HA ;
Goeden, MA ;
Rose, DJ ;
Mau, B ;
Shao, Y .
SCIENCE, 1997, 277 (5331) :1453-+
[6]   Identification of the Clostridium perfringens genes involved in the adaptive response to oxidative stress [J].
Briolat, V ;
Reysset, G .
JOURNAL OF BACTERIOLOGY, 2002, 184 (09) :2333-2343
[7]   Hydroxylamine assimilation by Rhodobacter capsulatus E1F1 -: Requirement of the hcp gene (hybrid cluster protein) located in the nitrate assimilation nas gene region for hydroxylamine reduction [J].
Cabello, P ;
Pino, C ;
Olmo-Mira, MF ;
Castillo, F ;
Roldán, MD ;
Moreno-Vivián, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (44) :45485-45494
[8]   One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products [J].
Datsenko, KA ;
Wanner, BL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (12) :6640-6645
[9]   Transcriptional regulation (prismane) protein of a hybrid cluster [J].
Filenko, NA ;
Browning, DF ;
Cole, JA .
BIOCHEMICAL SOCIETY TRANSACTIONS, 2005, 33 :195-197
[10]   Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis [J].
Flatley, J ;
Barrett, J ;
Pullan, ST ;
Hughes, MN ;
Green, J ;
Poole, RK .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (11) :10065-10072