A highly thermostable ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus

A ferritin from the obligate anaerobe and hyperthermophilic archaeon Pyrococcus furiosus (optimal growth at 100 degrees C) has been cloned and overproduced in Escherichia coli to one-fourth of total cell-free extract protein, and has been purified in one step to homogeneity. The ferritin (PfFtn) is...

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Veröffentlicht in:	Extremophiles : life under extreme conditions 2006-04, Vol.10 (2), p.139-148
Hauptverfasser:	TATUR, Jana, HAGEDOORN, Peter-Leon, OVEREIJNDER, Marieke L, HAGEN, Wilfred R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anaerobiosis Archaeal Proteins - chemistry Archaeal Proteins - isolation & purification Bacteria Bacteriology Biological and medical sciences Biotechnology E coli Escherichia coli Ferritins - chemistry Ferritins - isolation & purification Fundamental and applied biological sciences. Psychology Hot Temperature Isoelectric Focusing Microbiology Miscellaneous Molecular Sequence Data Protein Structure, Quaternary Pyrococcus furiosus Pyrococcus furiosus - chemistry Pyrococcus furiosus - genetics Sequence Alignment Space life sciences Spectrum Analysis
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Zusammenfassung:	A ferritin from the obligate anaerobe and hyperthermophilic archaeon Pyrococcus furiosus (optimal growth at 100 degrees C) has been cloned and overproduced in Escherichia coli to one-fourth of total cell-free extract protein, and has been purified in one step to homogeneity. The ferritin (PfFtn) is structurally similar to known bacterial and eukaryal ferritins; it is a 24-mer of 20 kDa subunits, which add up to a total Mr 480 kDa. The protein belongs to the non-heme type of ferritins. The 24-mer contains approximately 17 Fe (as isolated), 2,700 Fe (fully loaded), or
ISSN:	1431-0651 1433-4909
DOI:	10.1007/s00792-005-0484-x