Sulerythrin, the smallest member of the rubrerythrin family, from a strictly aerobic and thermoacidophilic archaeon, Sulfolobus tokodaii strain 7.
A protein corresponding to the N-terminal domain of rubrerythrin was isolated from a strictly aerobic archaeon, Sulfolobus tokodaii strain 7. The molecular mass was found to be 15.8 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, 16278 Da by time-of-flight mass spectrometry and 34.5 kDa by gel filtration chromatography, suggesting that the protein is dimeric. Two mol iron and 1-2 mol zinc mol(-1) protein were detected. On addition of the azide ion, the absorption spectrum was greatly affected. The far UV circular dichroism spectrum suggested that the protein was mostly composed of alpha-helices. The N-terminal sequence completely matched the open reading frame, st2370, recently found on genome analysis of the organism. The protein was homologous to rubrerythrin but lacked a C-terminal rubredoxin domain. It was found in the genus Sulfolobus and therefore named sulerythrin; it is the smallest and first aerobic member of the rubrerythrin family.
Wakagi
Takayoshi
T
Department of Biotechnology, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan. atwakag@mail.ecc.u-tokyo.ac.jp
D000332:Aerobiosis; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000235:genetics*; D005288:Ferredoxins / Q000235:genetics*; D006422:Hemerythrin; D007501:Iron / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012416:Rubredoxins; D013056:Spectrophotometry, Ultraviolet; D016944:Sulfolobus / Q000235:genetics*; D015032:Zinc / Q000737:chemistry
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D005288:Ferredoxins; D006422:Hemerythrin; D012416:Rubredoxins; C055857:rubrerythrins; D007501:Iron; D015032:Zinc