In the thermophilic archaeon Sulfolobus solfataricus a DNA-binding protein is in vitro (Adpribosyl)ated.
A small protein with high affinity for homologous DNA was isolated from Sulfolobus solfataricus homogenate by mineral acid extraction. It was purified using a two-step procedure including CM-cellulose and RP-HPL chromatographies. The protein was electrophoretically homogeneous, had a molecular weight of 7.147 kDa and an amino acid composition with a high content of lysine and glutamic acid residues. The protein was able to protect DNA against thermal denaturation and DNAse I digestion in a dose-dependent manner. After incubation of the sulfolobal homogenate in the presence of 32P-NAD, followed by the purification steps, the protein was modified by ADPribose, as revealed by reaction product analysis, SDS-PAGE and autoradiography.
Faraone-Mennella
M R
MR
Dipartimento di Chimica Organica e Biologica, Università Federico II, Napoli, Italy.
Farina
B
B
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004269:DNA, Bacterial / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D018698:Glutamic Acid / Q000032:analysis; D006657:Histones; D006358:Hot Temperature; D008239:Lysine / Q000032:analysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism*; D009691:Nucleic Acid Denaturation; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D016944:Sulfolobus / Q000378:metabolism*
D000596:Amino Acids; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D006657:Histones; D010446:Peptide Fragments; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D018698:Glutamic Acid; D008239:Lysine