Gene of Heat Shock Protein of Sulfur-Dependent Archaeal Hyperthermophile Desulfurococcus

• Published in: Biochemical and biophysical research communications Vol. 214; no. 2; pp. 730 - 736
• Main Authors: Kagawa, Y., Ohta, T., Abe, Y., Endo, H., Yohda, M., Kato, N., Endo, I., Hamamoto, T., Ichida, M., Hoaki, T., Maruyama, T.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 14-09-1995
• Subjects: Amino Acid Sequence; Archaea - genetics; Archaea - metabolism; Bacterial Proteins - biosynthesis; Bacterial Proteins - genetics; Base Sequence; Biological Evolution; Chromosome Mapping; Chromosomes, Bacterial; Cloning, Molecular; DNA, Fungal - chemistry; DNA, Fungal - metabolism; Genes, Fungal; Heat-Shock Proteins - biosynthesis; Heat-Shock Proteins - genetics; Humans; Macromolecular Substances; Molecular Sequence Data; Recombinant Proteins - biosynthesis; Sequence Homology, Amino Acid; Thermoplasma - genetics
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1995.2346

To elucidate thermoresistance, a gene of a hyperthermophilic heat shock protein (HHSP) was isolated from the hyperthermophile
Desulfurococcus strain SY which grows at 95°C. The molecular weight of HHSP deduced from the open reading frame was 59,137 (545 amino acid residues). Sequence alignments of peptides reveal similarities (evolutionary distances) to the α (0.279) and β (0.296) subunits of thermosome, TF55 (0.343) and human t-complex polypeptide 1. The structure of a thermophilic heat shock protein TGroEL (Tamada et al. (1991)
Biochem. Biophys. Res. Commun.
179, 565) was quite different from that of HHSP. TGroEL and HSP60 have sequences identical to HHSP at its equatorial domain, while those identical to the α subunit of F-type ATPase are at its apical domain.