title: The amino acid sequence of a small DNA binding protein from the archaebacterium Sulfolobus solfataricus.
abstract: The thermoacidophilic archaebacterium Sulfolobus solfataricus possesses several DNA binding proteins which may have a histone-like function. Two particularly dominant species have molecular masses of 7 and 10 kDa, respectively. We have purified one of the small proteins which occurs in relatively large amount and have determined its amino acid sequence. The protein is characterized by a high lysine content; in the N-terminal region the lysine residues occur in an alternating order: X-K-X-K-X-K-X-K. The amino acid sequence does not indicate any obvious homology to those DNA binding proteins whose sequences have been determined.
mesh_terms: D000595:Amino Acid Sequence; D001105:Archaea / Q000032:analysis*; D001419:Bacteria / Q000032:analysis*; D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification*; D003488:Cyanogen Bromide; D004269:DNA, Bacterial / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004926:Escherichia coli; D010446:Peptide Fragments; D010957:Plasmids
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D003488:Cyanogen Bromide