| Literature DB >> 1936253 |
F Chillemi1, G Lugaro, D Boari, E Cardellini, M Bramucci, A Miano, D Amici, G L Gianfranceschi, E Durban.
Abstract
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+ (lambda 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.Entities:
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Year: 1991 PMID： 1936253 DOI： 10.1016/0014-5793(91)81105-h
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124