A putative RNA binding protein from Plasmodium vivax apicoplast.

A putative RNA binding protein from Plasmodium vivax apicoplast.
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DOI:
10.1002/2211-5463.12351
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发表时间:
2018-03
期刊:
影响因子:
2.6
通讯作者:
Díaz-Moreno I
Díaz-Moreno I
中科院分区:
生物学4区
文献类型:
--
作者:
García-Mauriño SM;Díaz-Quintana A;Rivero-Rodríguez F;Cruz-Gallardo I;Grüttner C;Hernández-Vellisca M;Díaz-Moreno I

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疟疾是由疟原虫属的顶复门原虫通过雌蚊的叮咬进入人类和动物的血液引起的。间日疟原虫基因组的注释揭示了一种推定的RNA结合蛋白(apiRBP),该蛋白被预测将被贩运到顶质体(Apicomplexa原生动物特有的质体细胞器)中。虽然apiRBP的3D结构模型对应于具有额外C末端α螺旋(α3)的非典型RNA识别基序,但初步的蛋白质生产试验仍然不成功。apiRBP模型的理论溶剂化分析突出了聚集α3的暴露疏水区域。因此,我们使用C末端GFP融合嵌合体来稳定高度不溶性的apiRBP,并确定其结合富含U的RNA片段的能力。apiRBP对此类RNA的亲和力高度依赖于离子强度,表明apiRBP-RNA复合物由静电相互作用驱动。总之,apiRBP是一个有吸引力的工具,顶质体转录研究和抗疟药物设计。
Malaria is caused by Apicomplexa protozoans from the Plasmodium genus entering the bloodstream of humans and animals through the bite of the female mosquitoes. The annotation of the Plasmodium vivax genome revealed a putative RNA binding protein (apiRBP) that was predicted to be trafficked into the apicoplast, a plastid organelle unique to Apicomplexa protozoans. Although a 3D structural model of the apiRBP corresponds to a noncanonical RNA recognition motif with an additional C‐terminal α‐helix (α3), preliminary protein production trials were nevertheless unsuccessful. Theoretical solvation analysis of the apiRBP model highlighted an exposed hydrophobic region clustering α3. Hence, we used a C‐terminal GFP‐fused chimera to stabilize the highly insoluble apiRBP and determined its ability to bind U‐rich stretches of RNA. The affinity of apiRBP toward such RNAs is highly dependent on ionic strength, suggesting that the apiRBP–RNA complex is driven by electrostatic interactions. Altogether, apiRBP represents an attractive tool for apicoplast transcriptional studies and for antimalarial drug design.
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