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Cluster exchange reactivity of [2Fe‐2S]‐bridged heterodimeric BOLA1‐GLRX5
The FEBS Journal ( IF 5.5 ) Pub Date : 2020-06-15 , DOI: 10.1111/febs.15452 Sambuddha Sen 1 , Amber L Hendricks 1 , James A Cowan 1
The FEBS Journal ( IF 5.5 ) Pub Date : 2020-06-15 , DOI: 10.1111/febs.15452 Sambuddha Sen 1 , Amber L Hendricks 1 , James A Cowan 1
Affiliation
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Mitochondrial BOLA1 is known to form a [2Fe‐2S] cluster‐bridged heterodimeric complex with mitochondrial monothiol glutaredoxin GLRX5; however, the function of this heterodimeric complex is unclear. Some reports suggest redundant roles for BOLA1 and a related protein, BOLA3, with both involved in the maturation of [4Fe‐4S] clusters in a subset of mitochondrial proteins. However, a later report on the structure of BOLA1‐GLRX5 heterodimeric complex demonstrated a buried cluster environment and predicted a redox role instead of the cluster trafficking role suggested for the BOLA3‐GLRX5 heterodimeric complex. Herein, we describe a detailed kinetic study of relative cluster exchange reactivity involving heterodimeric complex of BOLA1 with GLRX5. By the use of CD spectroscopy, it is demonstrated that [2Fe‐2S]‐bridged BOLA1‐GLRX5 can be readily formed by cluster uptake from donors such as ISCU or [2Fe‐2S](GS)4 complex, but not from ISCA1 or ISCA2. Rapid holo‐formation following delivery from [2Fe‐2S](GS)4 supports possible physiological relevance in the cellular labile iron pool. Holo [2Fe‐2S] BOLA1‐GLRX5 heterodimeric complex is incapable of donating cluster to apo protein acceptors, providing experimental support for a nontrafficking role. Finally, we report the formation and reactivity of the holo [2Fe‐2S]‐bridged BOLA1 homodimer (lacking a partner GLRX). While the holo‐heterodimer is thermodynamically more stable, by contrast the holo BOLA1 homodimer does demonstrate facile cluster exchange reactivity.
中文翻译：
[2Fe-2S]-桥接的异二聚体BOLA1-GLRX5的簇交换反应性
已知线粒体BOLA1与线粒体单硫醇戊二糖谷氨酸毒素GLRX5形成[2Fe-2S]簇桥杂二聚体。然而，该异二聚体复合物的功能尚不清楚。一些报告表明BOLA1和相关蛋白BOLA3的冗余作用，都参与了线粒体蛋白子集中[4Fe-4S]簇的成熟。但是，后来有关BOLA1-GLRX5异二聚体结构的报告证明了埋藏的簇状环境，并预测了氧化还原作用，而不是建议的BOLA3-GLRX5异二聚体复合物的贩运作用。在这里，我们描述了涉及BOLA1与GLRX5的异二聚体复合物的相对簇交换反应性的详细动力学研究。通过CD光谱学，4复杂，但不是来自ISCA1或ISCA2。从[2Fe-2S]（GS）4释放后快速形成全铁，支持细胞不稳定铁池中可能的生理相关性。Holo [2Fe-2S] BOLA1-GLRX5异二聚体复合物无法将簇捐赠给载脂蛋白受体，从而为非贩运角色提供实验支持。最后，我们报告了[2Fe-2S]桥连的BOLA1同型二聚体（缺少伴侣GLRX）的形成和反应性。虽然全异源二聚体在热力学上更稳定，但相比之下，全质BOLA1同型二聚体确实显示出容易的簇交换反应性。
更新日期：2020-06-15
中文翻译：
[2Fe-2S]-桥接的异二聚体BOLA1-GLRX5的簇交换反应性
已知线粒体BOLA1与线粒体单硫醇戊二糖谷氨酸毒素GLRX5形成[2Fe-2S]簇桥杂二聚体。然而，该异二聚体复合物的功能尚不清楚。一些报告表明BOLA1和相关蛋白BOLA3的冗余作用，都参与了线粒体蛋白子集中[4Fe-4S]簇的成熟。但是，后来有关BOLA1-GLRX5异二聚体结构的报告证明了埋藏的簇状环境，并预测了氧化还原作用，而不是建议的BOLA3-GLRX5异二聚体复合物的贩运作用。在这里，我们描述了涉及BOLA1与GLRX5的异二聚体复合物的相对簇交换反应性的详细动力学研究。通过CD光谱学，4复杂，但不是来自ISCA1或ISCA2。从[2Fe-2S]（GS）4释放后快速形成全铁，支持细胞不稳定铁池中可能的生理相关性。Holo [2Fe-2S] BOLA1-GLRX5异二聚体复合物无法将簇捐赠给载脂蛋白受体，从而为非贩运角色提供实验支持。最后，我们报告了[2Fe-2S]桥连的BOLA1同型二聚体（缺少伴侣GLRX）的形成和反应性。虽然全异源二聚体在热力学上更稳定，但相比之下，全质BOLA1同型二聚体确实显示出容易的簇交换反应性。
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