The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.
The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.
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DOI：
10.1016/j.bbabio.2012.06.621
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发表时间：
2012-11
影响因子：
4.3
通讯作者：
Koch, Hans-Georg
中科院分区：
文献类型：
--
作者：
Lohmeyer, Eva;Schroeder, Sebastian;Pawlik, Grzegorz;Trasnea, Petru-Iulian;Peters, Annette;Daldal, Fevzi;Koch, Hans-Georg
关键词：
Sco蛋白是真核生物和原核生物中广泛存在的aa3型细胞色素氧化酶CuA中心的组装因子。然而，Sco同系物也发现于细菌如荚膜红细菌中，其缺乏aa 3型细胞色素氧化酶，而是使用不具有CuA中心的cbb 3型细胞色素氧化酶（cbb 3考克斯）作为末端氧化酶。在本研究中，我们分析了Sco（SenC）在荚膜红细菌cbb3考克斯组装过程中的作用。与早期的工作一致，我们发现了一个强大的cbb3考克斯缺陷，在SenC的情况下，损害CcoN，CcoO和CcoP核心亚基的稳态稳定性，没有可检测的组装中间体的积累。体内交联结果表明，SenC是在紧密接近的CcoP和CcoH亚基的cbb3考克斯，表明SenC直接相互作用，cbb3考克斯在其组装。SenC结合铜，并且在不存在SenC的情况下，cbb 3考克斯组装缺陷可以通过添加至少0.5 μM Cu来挽救。铜和SenC都不影响cbb3考克斯的ccoNOQP操纵子编码的转录。senC本身的转录也不受铜的影响，除非假定的铜出口ATP酶CcoI是缺席。由于cbb3考克斯组装体特别需要CcoI，因此这些数据提供了cbb3考克斯的Cu输送与SenC功能之间的直接联系。
Sco proteins are widespread assembly factors for the CuA centre of aa3-type cytochrome oxidases in eukaryotic and prokaryotic organisms. However, Sco homologues are also found in bacteria like Rhodobacter capsulatus which lack aa3-type cytochrome oxidases and instead use a cbb3-type cytochrome oxidase (cbb3 Cox) without a CuA centre as a terminal oxidase. In the current study, we have analyzed the role of Sco (SenC) during cbb3 Cox assembly in Rhodobacter capsulatus. In agreement with earlier works, we found a strong cbb3 Cox defect in the absence of SenC that impairs the steady-state stability of the CcoN, CcoO and CcoP core subunits, without the accumulation of detectable assembly intermediates. In vivo cross-linking results demonstrate that SenC is in close proximity to the CcoP and CcoH subunits of cbb3 Cox, suggesting that SenC interacts directly with cbb3 Cox during its assembly. SenC binds copper and the cbb3 Cox assembly defect in the absence of SenC can be rescued by the addition of least 0.5 μM Cu. Neither copper nor SenC influenced the transcription of the ccoNOQP operon encoding for cbb3 Cox. Transcription of senC itself was also not influenced by Cu unless the putative Cu-export ATPase CcoI was absent. As CcoI is specifically required for the cbb3 Cox assembly, these data provide a direct link between Cu delivery to cbb3 Cox and SenC function.
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