Mendes Andreia V, Grou Cláudia P, Azevedo Jorge E, Pinto Manuel P
Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, Rua Alfredo Allen 208, 4200-135 Porto, Portugal; Organelle Biogenesis and Function Group, Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal.
Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, Rua Alfredo Allen 208, 4200-135 Porto, Portugal; Organelle Biogenesis and Function Group, Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; Instituto de Ciências Biomédicas Abel Salazar (ICBAS), Universidade do Porto, Rua de Jorge Viterbo Ferreira 228, 4050-313 Porto, Portugal.
Biochim Biophys Acta. 2016 Jan;1863(1):139-47. doi: 10.1016/j.bbamcr.2015.10.020. Epub 2015 Oct 30.
Protein modification with the small ubiquitin-like modifier (SUMO) is a reversible process regulating many central biological pathways. The reversibility of SUMOylation is ensured by SUMO proteases many of which belong to the sentrin/SUMO-specific protease (SENP) family. In recent years, many advances have been made in allocating SENPs to specific biological pathways. However, due to difficulties in obtaining recombinant full-length active SENPs for thorough enzymatic characterization, our knowledge on these proteases is still limited. In this work, we used in vitro synthesized full-length human SENPs to perform a side-by-side comparison of their activities and substrate specificities. ProSUMO1/2/3, RanGAP1-SUMO1/2/3 and polySUMO2/3 chains were used as substrates in these analyses. We found that SENP1 is by far the most versatile and active SENP whereas SENP3 stands out as the least active of these enzymes. Finally, a comparison between the activities of full-length SENPs and their catalytic domains suggests that in some cases their non-catalytic regions influence their activity.
用小泛素样修饰物（SUMO）进行蛋白质修饰是一个调节许多核心生物途径的可逆过程。SUMO化的可逆性由SUMO蛋白酶确保，其中许多属于sentrin/SUMO特异性蛋白酶（SENP）家族。近年来，在将SENP分配到特定生物途径方面取得了许多进展。然而，由于难以获得用于全面酶学表征的重组全长活性SENP，我们对这些蛋白酶的了解仍然有限。在这项工作中，我们使用体外合成的全长人SENP对它们的活性和底物特异性进行了并排比较。在这些分析中，ProSUMO1/2/3、RanGAP1-SUMO1/2/3和多聚SUMO2/3链用作底物。我们发现，SENP1是迄今为止最通用且活性最高的SENP，而SENP3是这些酶中活性最低的。最后，全长SENP与其催化结构域活性之间的比较表明，在某些情况下，它们的非催化区域会影响其活性。
