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The thermostable histone-like protein Sso7c (Sso for Sulfolobus solfataricus) from the archaeon Sulfolobus solfataricus was purified from the supernatant of acid-soluble cell lysates. Reverse phase HPLC of an apparently homogeneous Sso7c protein fraction from Mono S chromatography resulted in resolution of three further peaks. Sequence analysis revealed one of these components to be bovine RNase A, originating from the culture medium and explaining the RNA hydrolyzing activities of Sso7 preparations previously described. Sequence analysis of pure Sso7c showed an epsilon-Lys methylation pattern identical to that of Sso7d and a single Gln --> Glu mutational difference at position 13. The remaining two proteins obtained after HPLC separation were identified as homologues of bacterial repressor-like proteins. Thus, the existence of repressor-like proteins was demonstrated at the protein level in archaea, raising the question of structural and functional consequences of these proteins on the otherwise eukaryotic-like basal transcriptional machinery in archaea.

Original publication




Journal article


Febs lett

Publication Date





141 - 144


Amino Acid Sequence, Archaeal Proteins, DNA-Binding Proteins, Databases, Factual, Hydrogen-Ion Concentration, Molecular Sequence Data, Repressor Proteins, Ribonuclease, Pancreatic, Sequence Alignment, Sequence Analysis, Sequence Homology, Amino Acid, Sulfolobus