2',3'‐Dialdehyde of GTP blocks regulatory functions of adenylate cyclase Ns protein

FEBS Letters

Bulargina, Tamara V.¹  Skurat, Alexander V.¹  Yurkova, Maria S.¹  Severin, Eugene S.¹  Khropov, Yuri V.¹ 

[1] Department of Biochemistry, Moscow State University, Moscow 119899, USSR

关键词: GTP 2';    3'-dialdehyde;    Adenylate cyclase;    Ns;    protein;    Caudate nucleus;    Forskolin;    Reconstitution;   

DOI  :  10.1016/0014-5793(85)80893-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Preincubation of bovine caudate nucleus membranes with the 2',3'-dialdehyde of GTP (oGTP) reduces adenylate cyclase activation by guanylyl imidodiphosphate (GppNHp) in a time-dependent fashion. A slower rate of inhibition is observed if membranes are treated with both GTP and oGTP. The efficacy of oGTP action is enhanced by raising the Mg²⁺ concentration. Reduction of adenylate cyclase sensitivity to GppNHp is followed by an irreversible decrease of enzyme stimulation by forskolin. Addition of a Lubrol soluble preparation from guinea pig lung membranes to oGTP-treated caudate nucleus membranes causes restoration of the adenylate cyclase sensitivity to GppNHp. These data suggest that oGTP blocks the GTP-binding site of the adenylate cyclase system localized on the N_s protein. Such modification leads to the elimination of the N_s-mediated regulation of the enzyme.

【 授权许可】

Unknown