Characterization of the respiration-induced yeast mitochondrial permeability transition pore.
Characterization of the respiration-induced yeast mitochondrial permeability transition pore.
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DOI：
10.1002/yea.2984
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发表时间：
2013-12
期刊：
影响因子：
2.6
通讯作者：
Pfeiffer, Douglas R.
中科院分区：
文献类型：
--
作者：
Bradshaw, Patrick C.;Pfeiffer, Douglas R.
当从酿酒酵母中分离出的线粒体在没有磷和ADP的情况下氧化呼吸底物时，酵母线粒体非选择性通道，也被称为酵母通透性转换孔(YPTP)，在内膜打开，消散电化学梯度。ATP还能诱导yPTP开放。YPTP的开放允许甘露醇运输到实验室酵母菌株的分离线粒体中，但在工业酵母菌株酵母泡沫中，甘露醇不容易通过yPTP渗透。三磷酸腺苷合成酶的抑制剂寡霉素的存在允许呼吸诱导的甘露醇在该菌株的线粒体中渗透。钾(K+)对呼吸诱导的yPTP的影响因呼吸底物浓度的不同而不同。呼吸底物浓度低时，K+抑制呼吸诱导的yPTP开放，而高底物浓度时，这种作用减弱。然而，在较高的呼吸底物浓度下，K+的存在部分阻止了磷酸盐对yPTP开放的抑制。磷酸盐被发现通过结合内膜基质空间侧的一个位点来抑制呼吸诱导的yPTP开放，此外，它还通过向基质空间赠送质子来防止yPTP开放所需的pH变化的已知抑制作用。呼吸诱导的yPTP也被NAD、Mg2+、NH4+或聚合成十钒酸根的氧阴离子所抑制。结果表明，呼吸诱导的yPTP的效应器与先前描述的ATP诱导的yPTP的效应器相似，并协调了先前菌株对yPTP溶质选择性的差异。
When isolated mitochondria from the yeast Saccharomyces cerevisiae oxidize respiratory substrates in the absence of phosphate and ADP, the yeast mitochondrial unselective channel, also called the yeast permeability transition pore (yPTP), opens in the inner membrane dissipating the electrochemical gradient. ATP also induces yPTP opening. yPTP opening allows mannitol transport into isolated mitochondria of laboratory yeast strains, but mannitol is not readily permeable through the yPTP in an industrial yeast strain, Yeast Foam. The presence of oligomycin, an inhibitor of ATP synthase, allowed for respiration-induced mannitol permeability in mitochondria from this strain. Potassium (K+) had varied effects on the respiration-induced yPTP depending on the concentration of the respiratory substrate added. At low respiratory substrate concentrations K+ inhibited respiration-induced yPTP opening, while at high substrate concentrations this effect diminished. However, at the high respiratory substrate concentrations, the presence of K+ partially prevented phosphate inhibition of yPTP opening. Phosphate was found to inhibit respiration-induced yPTP opening by binding a site on the matrix space side of the inner membrane in addition to its known inhibitory effect of donating protons to the matrix space to prevent the pH change necessary for yPTP opening. The respiration-induced yPTP was also inhibited by NAD, Mg2+, NH4+, or the oxyanion vanadate polymerized to decavanadate. The results demonstrate similar effectors of the respiration-induced yPTP as those previously described for the ATP-induced yPTP and reconcile previous strain-dependent differences in yPTP solute selectivity.
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