Sunderman E R, Zagotta W N
Department of Physiology and Biophysics, Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195-7290, USA.
J Gen Physiol. 1999 May;113(5):601-20. doi: 10.1085/jgp.113.5.601.
The cyclic nucleotide-gated (CNG) channel of retinal rod photoreceptor cells is an allosteric protein whose activation is coupled to a conformational change in the ligand-binding site. The bovine rod CNG channel can be activated by a number of different agonists, including cGMP, cIMP, and cAMP. These agonists span three orders of magnitude in their equilibrium constants for the allosteric transition. We recorded single-channel currents at saturating cyclic nucleotide concentrations from the bovine rod CNG channel expressed in Xenopus oocytes as homomultimers of alpha subunits. The median open probability was 0.93 for cGMP, 0.47 for cIMP, and 0.01 for cAMP. The channels opened to a single conductance level of 26-30 pS at +80 mV. Using signal processing methods based on hidden Markov models, we determined that two closed and one open states are required to explain the gating at saturating ligand concentrations. We determined the maximum likelihood rate constants for two gating schemes containing two closed (denoted C) and one open (denoted O) states. For the C left and right arrow C left and right arrow O scheme, all rate constants were dependent on cyclic nucleotide. For the C left and right arrow O left and right arrow C scheme, the rate constants for only one of the transitions were cyclic nucleotide dependent. The opening rate constant was fastest for cGMP, intermediate for cIMP, and slowest for cAMP, while the closing rate constant was fastest for cAMP, intermediate for cIMP, and slowest for cGMP. We propose that interactions between the purine ring of the cyclic nucleotide and the binding domain are partially formed at the time of the transition state for the allosteric transition and serve to reduce the transition state energy and stabilize the activated conformation of the channel. When 1 microM Ni2+ was applied in addition to cyclic nucleotide, the open time increased markedly, and the closed time decreased slightly. The interactions between H420 and Ni2+ occur primarily after the transition state for the allosteric transition.
视网膜视杆光感受器细胞的环核苷酸门控(CNG)通道是一种别构蛋白,其激活与配体结合位点的构象变化相关联。牛视杆CNG通道可被多种不同的激动剂激活,包括cGMP、cIMP和cAMP。这些激动剂在别构转变的平衡常数上跨越三个数量级。我们在非洲爪蟾卵母细胞中表达的牛视杆CNG通道的α亚基同多聚体上,于饱和环核苷酸浓度下记录单通道电流。cGMP的中位开放概率为0.93,cIMP为0.47,cAMP为0.01。在+80 mV时,通道开放至单一电导水平26 - 30 pS。使用基于隐马尔可夫模型的信号处理方法,我们确定需要两个关闭状态和一个开放状态来解释饱和配体浓度下的门控。我们确定了包含两个关闭状态(记为C)和一个开放状态(记为O)的两种门控方案的最大似然速率常数。对于C⇄C⇄O方案,所有速率常数均依赖于环核苷酸。对于C⇄O⇄C方案,只有一个转变的速率常数依赖于环核苷酸。开放速率常数对于cGMP最快,对于cIMP居中,对于cAMP最慢,而关闭速率常数对于cAMP最快,对于cIMP居中,对于cGMP最慢。我们提出,环核苷酸的嘌呤环与结合结构域之间的相互作用在别构转变的过渡态时部分形成,并有助于降低过渡态能量并稳定通道的激活构象。当除环核苷酸外还施加1 μM Ni2+时,开放时间显著增加,关闭时间略有减少。H420与Ni2+之间的相互作用主要发生在别构转变的过渡态之后。