Andreini Claudia, Banci Lucia, Bertini Ivano, Rosato Antonio
Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy.
J Proteome Res. 2008 Jan;7(1):209-16. doi: 10.1021/pr070480u. Epub 2007 Nov 8.
In high-throughput genome-level protein investigation efforts, such as Structural Genomics, the systematic experimental characterization of metal-binding properties (i.e., the investigation of the metalloproteome) is not always pursued and remains far from trivial. In the present work, we have applied a bioinformatic approach to investigate the occurrence of (putative) copper-binding proteins in 57 different organisms spanning the entire tree of life. We found that the size of the copper proteome is generally less than 1% of the total proteome of an organism, in both eukaryotes and prokaryotes. The occurrence of copper-binding proteins is relatively scarce when compared to that of zinc-binding proteins and of non-heme iron proteins. This may be due to both poorer bioavailability (in particular with respect to iron in the ancient world) and the complexity of copper chemistry and the risks associated with it, which may have adversely affected natural selection of copper-binding proteins. The present analysis shows that there is a strong relationship between the metal coordination sphere and protein function. A network involving proteins having roles in both copper transport and respiration was identified, parts or all of which are detected in the majority of the organisms examined.
在诸如结构基因组学等高通量基因组水平的蛋白质研究工作中，金属结合特性的系统实验表征（即金属蛋白质组的研究）并非总是被开展，而且仍然远非易事。在本研究中，我们应用了一种生物信息学方法来研究涵盖整个生命树的57种不同生物体中（假定的）铜结合蛋白的存在情况。我们发现，无论是在真核生物还是原核生物中，铜蛋白质组的规模通常都小于生物体总蛋白质组的1%。与锌结合蛋白和非血红素铁蛋白相比，铜结合蛋白的存在相对较少。这可能是由于生物可利用性较差（特别是在古代世界相对于铁而言）以及铜化学的复杂性和与之相关的风险，这些可能对铜结合蛋白的自然选择产生了不利影响。目前的分析表明，金属配位球与蛋白质功能之间存在密切关系。我们识别出了一个涉及在铜运输和呼吸中都起作用的蛋白质的网络，在大多数被检测的生物体中都能检测到该网络的部分或全部。
