Loftus Samuel J, Crawford Douglas L
Rosenstiel School of Marine and Atmospheric Science, University of Miami, 4600 Rickenbacker Causeway, Miami, FL 33149, USA.
Physiol Biochem Zool. 2013 Jan-Feb;86(1):82-91. doi: 10.1086/668850. Epub 2012 Dec 12.
The first enzyme in the oxidative phosphorylation pathway is Complex I (EC 1.6.5.3). Complex I is a large heteromeric enzyme complex with 45 protein subunits that translocates H(+) ions across the mitochondrial inner membrane. Among northern and southern populations of the teleost fish Fundulus heteroclitus, Complex I subunits have fixed amino acid substitutions. Additionally, there are differences in oxidative phosphorylation activity among populations of F. heteroclitus. To investigate whether these differences are related to Complex I, enzyme activity was measured in 121 individuals from five populations of F. heteroclitus and its sister species Fundulus grandis acclimated to a constant 20°C temperature. Within each population, Complex I activity is highly variable among individuals of F. heteroclitus (coefficient of variation percentage among individuals has a mean of 90% in the five F. heteroclitus populations), and the mean Complex I activity among populations is significantly different at the latitudinal extremes of the range. Importantly, Complex I activity is more similar between F. heteroclitus from the southernmost population and its sister species F. grandis than to the northern populations of F. heteroclitus, suggesting important evolutionary differences. Unexpectedly, the activity is nearly fourfold higher in southern populations than northern populations. Mitochondrial density appears to compensate partially for decreased activity in northern individuals; activity per wet weight is only twofold higher in southern populations. We suggest that some of the variation in Complex I activity is genetically based and thus is being influenced by directional selection. However, this conclusion presents a conundrum: there should not be so much variation in Complex I activity within a population if this variation is biologically important.
氧化磷酸化途径中的首个酶是复合体I(EC 1.6.5.3)。复合体I是一种大型异源酶复合体,含有45个蛋白质亚基,可将氢离子转运穿过线粒体内膜。在硬骨鱼物种——异齿底鳉的北方和南方种群中,复合体I亚基存在固定的氨基酸替换。此外,异齿底鳉不同种群之间的氧化磷酸化活性也存在差异。为了研究这些差异是否与复合体I有关,我们测量了来自异齿底鳉五个种群及其姐妹物种大眼底鳉的121个个体在恒定20°C温度下的酶活性。在每个种群中,异齿底鳉个体间的复合体I活性高度可变(在五个异齿底鳉种群中,个体间变异系数百分比的平均值为90%),并且在该分布范围的纬度极值处,种群间的复合体I平均活性存在显著差异。重要的是,最南端种群的异齿底鳉与它的姐妹物种大眼底鳉之间的复合体I活性,比与异齿底鳉北方种群的复合体I活性更为相似,这表明存在重要的进化差异。出乎意料的是,南方种群的活性几乎是北方种群的四倍。线粒体密度似乎部分补偿了北方个体中降低的活性;按湿重计算,南方种群的活性仅高两倍。我们认为,复合体I活性的一些变异是基于遗传的,因此受到定向选择的影响。然而,这一结论带来了一个难题:如果这种变异具有生物学重要性,那么一个种群内的复合体I活性就不应有如此大的变异。