Deterre P, Bigay J, Robert M, Pfister C, Kühn H, Chabre M
Laboratoire de Biophysique Moléculaire et Cellulaire (Unité Associée 520 du CNRS), DRF-CEN Grenoble, France.
Proteins. 1986 Oct;1(2):188-93. doi: 10.1002/prot.340010210.
The GTP-binding subunit of transducin (T alpha) activates the cGMP phosphodiesterase (PDE) of bovine retinal rods by relieving the constraint imposed by the inhibitory subunit PDE gamma. We have isolated and characterized the complex T alpha.GTP gamma S-PDE gamma formed when T alpha is activated by the nonhydrolyzable analog GTP gamma S. Sedimentation and light-scattering techniques demonstrate that, in contrast to free T alpha.GTP gamma S, which is soluble, the T alpha.GTP gamma S-PDE gamma complex, as well as T alpha.GTP-PDE gamma, is membrane bound at cytosolic ionic strength. It is eluted from the membrane at low ionic strength as a monomeric and 1:1 stoichiometric complex. The relative affinities of PDE gamma for PDE alpha beta and for T alpha.GTP are discussed.
转导素的GTP结合亚基(Tα)通过解除抑制性亚基PDEγ所施加的限制,激活牛视网膜杆细胞的cGMP磷酸二酯酶(PDE)。我们已经分离并鉴定了Tα被不可水解类似物GTPγS激活时形成的复合物Tα.GTPγS-PDEγ。沉降和光散射技术表明,与可溶的游离Tα.GTPγS不同,Tα.GTPγS-PDEγ复合物以及Tα.GTP-PDEγ在胞质离子强度下与膜结合。在低离子强度下,它以单体和1:1化学计量比的复合物形式从膜上洗脱下来。讨论了PDEγ对PDEαβ和Tα.GTP的相对亲和力。