title: The primary structure of DNA binding protein II from the extreme thermophilic bacterium Thermus thermophilus.
abstract: The primary structure of DNA binding protein II (DNA bp II) from the extreme thermophilic bacterium Thermus thermophilus has been established by combination of manual and automated techniques. The protein has 95 residues and a molecular mass of 11,843. Comparison of the primary structure with the known sequence data of DNA bp II from Clostridium pasteurineum, Baccillus stearothermophilus, Escherichia coli, Rhizobium meliloti, Anabena, Thermoplasma acidophilum, Pseudomonas aeruginosa and Bacillus caldolyticus reveals a clear homology among these small basic proteins. In particular, two short sequences in the middle and C-terminal part of the proteins (residues N-Gly-Phe-Gly-X-Phe and Pro-X-Thr at positions 46-51 and 63-65, respectively) are completely conserved.
authors.affiliation: Max Planck Institute for Molecular Genetics, Berlin Dahlem, FRG.
authors.forename: R
authors.initials: R
authors.lastname: Zierer
authors.forename: D
authors.initials: D
authors.lastname: Choli
mesh_terms: D000595:Amino Acid Sequence; D001419:Bacteria / Q000378:metabolism; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013824:Thermus / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins