Department of Biology, Haverford College, Haverford, PA, 19041, USA.
Department of Biology and Center for Computational and Integrative Biology, Rutgers The State University of New Jersey, Camden, NJ, 08102, USA.
Protein J. 2020 Apr;39(2):152-159. doi: 10.1007/s10930-020-09889-x.
The segmented annelid worm, Mesenchytraeus solifugus, is a permanent resident of temperate, maritime glaciers in the Pacific northwestern region of North America, displaying atypically high intracellular ATP levels which have been linked to its unusual ability to thrive in hydrated glacier ice. We have shown previously that ice worms contain a highly basic, carboxy terminal extension on their ATP6 regulatory subunit, likely acquired by horizontal gene transfer from a microbial dietary source. Here we examine the full complement of FF ATP synthase structural subunits with attention to non-conservative, ice worm-specific structural modifications. Our genomics analyses and molecular models identify putative proton shuttling domains on either side of the F hemichannel, which predictably function to enhance proton flow across the mitochondrial membrane. Other components of the ice worm ATP synthase complex have remained largely unchanged in the context of Metazoan evolution.
分段环节蠕虫，Mesenchytraeus solifugus，是北太平洋北美地区温带海洋冰川的永久居民，表现出异常高的细胞内 ATP 水平，这与它在水合冰川冰中茁壮成长的不寻常能力有关。我们之前已经表明，冰蠕虫在其 ATP6 调节亚基上具有高度碱性的羧基末端延伸，可能是通过水平基因从微生物饮食源获得的。在这里，我们检查完整的 FF ATP 合酶结构亚基，特别注意非保守的、冰蠕虫特异性的结构修饰。我们的基因组分析和分子模型确定了 F 半通道两侧的推定质子穿梭结构域，可预测地增强质子穿过线粒体膜的流动。在后生动物进化的背景下，冰蠕虫 ATP 合酶复合物的其他成分基本保持不变。
