Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium Sulfolobus acidocaldarius.
DNA-binding proteins in eubacteria, such as Escherichia coli NS1 and NS2, are generally small basic molecules. In contrast, the archaebacterium Sulfolobus acidocaldarius contains three groups of DNA-binding proteins which have molecular masses of 7, 8, and 10 kDa. In the first group, five proteins (7a-7e) have been identified, while in the second and third group only two proteins each are present, denoted 8a and 8b and 10a and 10b, respectively. In this paper, we present the primary structures of proteins 7a, 7b, and 7e from the first group. All three proteins contain lysyl residues which are monomethylated to different extents. The modified lysines are found in the NH2-terminal regions of all 7-kDa proteins and in the COOH-terminal part of protein 7e. The sequences of the 7-kDa group are highly similar to each other. All of these macromolecules have been shown to interact specifically with DNA. Protein 7e of the 7-kDa group shows the tightest binding to DNA.
D000595:Amino Acid Sequence; D001105:Archaea / Q000032:analysis*; D001419:Bacteria / Q000032:analysis*; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D004268:DNA-Binding Proteins / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation
D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D002918:Chymotrypsin; D003488:Cyanogen Bromide