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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

DOI

10.1016/s0014-5793(98)00848-5

Type

Journal article

Journal

FEBS letters

Publication Date

08/1998

Volume

432

Pages

141 - 144

Addresses

Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden. udo.oppermann@mbb.ki.se

Keywords

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