PMID:8168477
| Citation |
Darimont, B and Sterner, R (1994) Sequence, assembly and evolution of a primordial ferredoxin from Thermotoga maritima. EMBO J. 13:1772-81 |
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| Abstract |
A gene coding for the ferredoxin of the primordial, strictly anaerobic and hyperthermophilic bacterium Thermotoga maritima was cloned, sequenced and expressed in Escherichia coli. The ferredoxin gene encodes a polypeptide of 60 amino acids that incorporates a single 4Fe-4S cluster. T. maritima ferredoxin expressed in E. coli is a heat-stable, monomeric protein, the spectroscopic properties of which show that its 4Fe-4S cluster is correctly assembled within the mesophilic host, and that it remains stable during purification under aerobic conditions. Removal of the iron-sulfur cluster results in an apo-ferredoxin that has no detectable secondary structure. This observation indicates that in vivo formation of the ferredoxin structure is coupled to the insertion of the iron-sulfur cluster into the polypeptide chain. Sequence comparison of T. maritima ferredoxin with other 4Fe-4S ferredoxins revealed high sequence identities (75% and 50% respectively) to the ferredoxins from the hyperthermophilic members of the Archaea, Thermococcus litoralis and Pyrococcus furiosus. The high sequence similarity supports a close relationship between these extreme thermophilic organisms from different phylogenetic domains and suggests that ferredoxins with a single 4Fe-4S cluster are the primordial representatives of the whole protein family. This observation suggests a new model for the evolution of ferredoxins. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Biological Evolution; Circular Dichroism; Cloning, Molecular; Escherichia coli/genetics; Ferredoxins/genetics; Ferredoxins/metabolism; Genes, Bacterial/genetics; Gram-Negative Anaerobic Bacteria/genetics; Iron/metabolism; Models, Genetic; Models, Molecular; Molecular Sequence Data; Protein Conformation; Recombinant Proteins/biosynthesis; Sequence Homology, Amino Acid; Spectrophotometry, Ultraviolet; Sulfur/metabolism |
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