title: Studies on S14 protein from Thermus thermophilus possessing zinc finger-like motifs.
abstract: The amino acid sequence of the ribosomal protein S14 of Thermus thermophilus has been determined both by automated sequence analysis of the intact protein as well as by DNA sequence analysis of the gene. The carboxy-terminal region was verified by both amino acid sequence analysis of the carboxy-terminal peptide produced after Glu-C digestion and by DNA sequence analysis. The protein contains 60 amino acid residues with a calculated molecular weight of 7008. The most extensive homology is observed in the carboxy-terminal regions of all S14 proteins compared. Interestingly, the carboxy-terminal region of most S14 proteins of all species studied so far, form zinc-finger domains in the variety of C2-C2 form.
authors.affiliation: Aristotle University of Thessaloniki, School of Chemistry, Laboratory of Biochemistry, Greece.
authors.forename: P
authors.initials: P
authors.lastname: Tsiboli
authors.forename: T
authors.initials: T
authors.lastname: Choli
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D004269:DNA, Bacterial / Q000032:analysis; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012269:Ribosomal Proteins / Q000737:chemistry*; D016963:Thermus thermophilus / Q000737:chemistry*; D014157:Transcription Factors; D016335:Zinc Fingers
chemical_list: D004269:DNA, Bacterial; D009687:Nuclear Proteins; D011506:Proteins; D012269:Ribosomal Proteins; C051065:THRSP protein, human; D014157:Transcription Factors