Acidic pentapeptide phosphorylated in vitro by calf thymus protein kinase NII binds to DNA in the presence of Mg2+cations
| Autor: | Francesco Chillemi, G. L. Gianfranceschi, D. Boari, Domenico Amici, Massimo Bramucci, Egon Durban, Elena Cardellini, Antonino Miano, Lugaro G |
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| Rok vydání: | 1991 |
| Předmět: |
Molecular Sequence Data
Biophysics Peptide Biology Biochemistry Pentapeptide repeat DNA-binding protein Serine chemistry.chemical_compound Non-histone protein Structural Biology Genetics Animals Magnesium Amino Acid Sequence Phosphorylation Phosphopeptide Protein kinase A Molecular Biology chemistry.chemical_classification DNA Cell Biology Hydrogen-Ion Concentration Molecular biology Chromatin Kinetics chemistry DNA-binding peptide Cattle Electrophoresis Polyacrylamide Gel Chromatography Thin Layer Peptides Oligopeptides Protein Kinases Protein kinase NII |
| Zdroj: | FEBS Letters. 291:67-70 |
| ISSN: | 0014-5793 |
| Popis: | The pentapeptide pyroGlu-Ala-Glu-Ser-Asn has been synthetized and phosphorylated in vitro at level of serine by protein kinase NII isolated from calf thymus chromatin. It is noteworthy that the calf thymus kinase NII shows a remarkable affinity for this peptide. The [32P]peptide is able to bind to several DNAs in the presence of Mg2+ (λ phage, calf thymus, pBR540 plasmid). This binding appears not specific with regard to the type of DNA and its base sequence. These data support the hypothesis that phosphorylated acidic domains of nuclear nonhistone proteins could bind directly to DNA in the presence of Mg2+ cations |
| Databáze: | OpenAIRE |
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