The in vitro DNA binding properties of NDP kinase are related to its oligomeric state

FEBS Letters

Agou, Fabrice¹  Véron, Michel¹  Mesnildrey, Sébastien¹ 

[1] Unité de Régulation Enzymatique des Activités Cellulaires, Institut Pasteur, CNRS UMR 321, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France

关键词: Nucleoside diphosphate kinase;    DNA binding protein;    Dimeric mutant;    Filter binding assay;    Development;   

DOI  :  10.1016/S0014-5793(97)01292-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Genetic and biochemical evidences suggest that the enzymatic activity of NDP kinase is necessary but not sufficient for its biological function. While the human NDPK-B binds specifically single-strand polypyrimidines sequences, the hexameric enzyme from Dictyostelium does not. We demonstrated by electrophoretic mobility shift assay and filter binding assay that a dimeric mutant from Dictyostelium binds to an oligodesoxynucleotide while the wild-type does not. These data suggest that the differences in the DNA binding properties of several eucaryotic NDP kinases might be correlated to the differences in the stability of their hexameric structure.

【 授权许可】

Unknown