Transducin‐mediated, isoform‐specific interaction of recombinant rat nucleoside diphosphate kinases with bleached bovine retinal rod outer segment membranes

FEBS Letters

Kimura, Narimichi³  Hanai, Nobuo¹  Nomura, Koji²  Orlov, Nicolay Ya.³  Orlova, Tatiana G.³ 

[1] Tokyo Research Laboratories, Kyowa Hakko Kogyo Co. Ltd., Tokyo, Japan;Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, 35-2, Sakaecho, Itabashi-ku, Tokyo-173, Japan;Department of Molecular Biology, Tokyo Metropolitan Institute of Gerontology, 35-2, Sakaecho, Itabashi-ku, Tokyo-173, Japan

关键词: Nucleoside diphosphate kinase;    Isoform;    Retinal rod outer segment membrane;    G-protein;    Transducin;   

DOI  :  10.1016/0014-5793(96)00575-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The properties of the binding of recombinant rat nucleoside diphosphate (NDP) kinase isoforms a and β (NDP kinase α and β respectively) to bleached bovine retinal rod outer segment (ROS) membranes were investigated. It was found that: (1) both NDP kinase isoforms interacted with ROS membranes in a pH-, cation- and GTPγS-dependent manner; (2) the retinal G-protein transducin was an obligatory factor for the interaction; (3) the apparent affinity of NDP kinase a for ROS membranes was about 100-fold higher than that of NDP kinase β; and (4) an α-isoform-specific peptide, corresponding to the sequence of the N-terminal third (variable region), had the ability to displace bovine NDP kinase from ROS membranes. The results suggest the possible involvement of NDP kinases in cellular regulation via interaction with G-proteins and provide a structural basis for the possible differential roles of mammalian NDP kinase isoforms in the cell.

【 授权许可】

Unknown