The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms

被引:39
作者
Bruscella, P
Cassagnaud, L
Ratouchniak, J
Brasseur, G
Lojou, E
Amils, R
Bonnefoy, V
机构
[1] CNRS, IBSM, Chim Bacterienne Lab, F-13402 Marseille, France
[2] CNRS, IBSM, Lab Bioenerget & Ingn Prot, F-13402 Marseille, France
[3] Univ Autonoma Madrid, Ctr Biol Mol, E-28049 Madrid, Spain
来源
MICROBIOLOGY-SGM | 2005年 / 151卷
关键词
D O I
10.1099/mic.0.27476-0
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The gene encoding a putative high-potential iron-sulfur protein (HiPIP) from the strictly acidophilic and chemolithoautotrophic Acidithiobacillus ferrooxidans ATCC 33020 has been cloned and sequenced. This potential HiPIP was overproduced in the periplasm of the neutrophile and heterotroph Escherichia coli. As shown by optical and EPR spectra and by electrochemical studies, the recombinant protein has all the biochemical properties of a HiPIP, indicating that the iron-sulfur cluster was correctly inserted. Translocation of this protein in the periplasm of E coli was not detected in a Delta tatC mutant, indicating that it is dependent on the Tat system. The genetic organization of the iro locus in strains ATCC 23270 and ATCC 33020 is different from that found in strains Fe-1 and BRGM. Indeed, in A. ferrooxidans ATCC 33020 and ATCC 23270 (the type strain), iro was not located downstream from purA but was instead downstream from petC2, encoding cytochrome c(1) from the second A. ferrooxidans cytochrome bc(1), complex. These findings underline the genotypic heterogeneity within the A. ferrooxidans species. The results suggest that Iro transfers electrons from a cytochrome bc(1), complex to a terminal oxidase, as proposed for the HiPIP in photosynthetic bacteria.
引用
收藏
页码:1421 / 1431
页数:11
相关论文
共 67 条
[51]   High-potential iron-sulfur protein (HiPIP) is the major electron donor to the reaction center complex in photosynthetically growing cells of the purple bacterium Rubrivivax gelatinosus [J].
Nagashima, KVP ;
Matsuura, K ;
Shimada, K ;
Verméglio, A .
BIOCHEMISTRY, 2002, 41 (47) :14028-14032
[52]   RAPD genomic fingerprinting differentiates Thiobacillus ferrooxidans strains [J].
Novo, MTM ;
DeSouza, AP ;
Garcia, O ;
Ottoboni, LMM .
SYSTEMATIC AND APPLIED MICROBIOLOGY, 1996, 19 (01) :91-95
[53]  
Ochman H., 1990, PCR PROTOCOLS GUIDE, P219
[54]   Moving folded proteins across the bacterial cell membrane [J].
Palmer, T ;
Berks, BC .
MICROBIOLOGY-SGM, 2003, 149 :547-556
[55]   Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus:: Characterization of the iron-sulfur centers from the dehydrogenases and investigation of the high-potential iron-sulfur protein function by in vitro reconstitution of the respiratory chain [J].
Pereira, MM ;
Carita, JN ;
Teixeira, M .
BIOCHEMISTRY, 1999, 38 (04) :1276-1283
[56]   IN-VIVO PARTICIPATION OF A HIGH-POTENTIAL IRON-SULFUR PROTEIN AS ELECTRON-DONOR TO THE PHOTOCHEMICAL-REACTION CENTER OF RUBRIVIVAX-GELATINOSUS [J].
SCHOEPP, B ;
PAROT, P ;
MENIN, L ;
GAILLARD, J ;
RICHAUD, P ;
VERMEGLIO, A .
BIOCHEMISTRY, 1995, 34 (37) :11736-11742
[57]  
Selenska-Pobell S, 1998, J APPL MICROBIOL, V84, P1085
[58]   A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids [J].
Takahashi, Y ;
Tokumoto, U .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (32) :28380-28383
[59]  
TEDRO SM, 1979, J BIOL CHEM, V254, P1495
[60]   THE AMINO-ACID SEQUENCE OF A HIGH-REDOX-POTENTIAL FERREDOXIN FROM THE PURPLE PHOTOTROPHIC BACTERIUM, RHODOSPIRILLUM-TENUE STRAIN-2761 [J].
TEDRO, SM ;
MEYER, TE ;
KAMEN, M .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1985, 239 (01) :94-101