Acidic pentapeptide phosphorylated in vitro by calf thymus protein kinase NII binds to DNA in the presence of Mg2+ cations

FEBS Letters

Boari, D.⁴  Durban, E.⁵  Miano, A.³  Cardellini, E.⁵  Lugaro, G.⁴  Amici, D.³  Bramucci, M.³  Chillemi, F.²  Gianfranceschi, G.L.¹ 

[1] Institute of Cell Biology, University of Perugia, Perugia, Italy;Department of Organic and Industrial Chemistry, University of Milan, Milan, Italy;Department of Molecular, Cellular and Animal Biology, University of Camerino, Camerino, Italy;Institute of Hormone Chemistry, CNR, Milan, Italy;Department of Pharmacology, Baylor College of Medicine, Houston TX, USA

关键词: Protein kinase NII;    DNA-binding peptide;    Phosphopeptide;   

DOI  :  10.1016/0014-5793(91)81105-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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

【 授权许可】

Unknown