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RNP - 8和GLD - 3在GLD - 2聚腺苷酸聚合酶活性中拮抗作用的结构基础。

Structural basis for the antagonistic roles of RNP-8 and GLD-3 in GLD-2 poly(A)-polymerase activity.

作者信息

Nakel Katharina, Bonneau Fabien, Basquin Claire, Habermann Bianca, Eckmann Christian R, Conti Elena

机构信息

Department of Structural Cell Biology, Max-Planck-Institute of Biochemistry, D-82152 Martinsried, Germany.

Department of Genetics, Martin-Luther-University of Halle-Wittenberg, Institute of Biology, 06120 Halle (Saale), Germany.

出版信息

RNA. 2016 Aug;22(8):1139-45. doi: 10.1261/rna.056598.116. Epub 2016 Jun 10.

DOI:10.1261/rna.056598.116
PMID:27288313
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4931106/
Abstract

Cytoplasmic polyadenylation drives the translational activation of specific mRNAs in early metazoan development and is performed by distinct complexes that share the same catalytic poly(A)-polymerase subunit, GLD-2. The activity and specificity of GLD-2 depend on its binding partners. In Caenorhabditis elegans, GLD-2 promotes spermatogenesis when bound to GLD-3 and oogenesis when bound to RNP-8. GLD-3 and RNP-8 antagonize each other and compete for GLD-2 binding. Following up on our previous mechanistic studies of GLD-2-GLD-3, we report here the 2.5 Å resolution structure and biochemical characterization of a GLD-2-RNP-8 core complex. In the structure, RNP-8 embraces the poly(A)-polymerase, docking onto several conserved hydrophobic hotspots present on the GLD-2 surface. RNP-8 stabilizes GLD-2 and indirectly stimulates polyadenylation. RNP-8 has a different amino-acid sequence and structure as compared to GLD-3. Yet, it binds the same surfaces of GLD-2 by forming alternative interactions, rationalizing the remarkable versatility of GLD-2 complexes.

摘要

细胞质聚腺苷酸化在早期后生动物发育过程中驱动特定mRNA的翻译激活，由具有相同催化性聚（A）聚合酶亚基GLD-2的不同复合物执行。GLD-2的活性和特异性取决于其结合伙伴。在秀丽隐杆线虫中，GLD-2与GLD-3结合时促进精子发生，与RNP-8结合时促进卵子发生。GLD-3和RNP-8相互拮抗并竞争GLD-2的结合。基于我们之前对GLD-2 - GLD-3的机制研究，我们在此报告GLD-2 - RNP-8核心复合物的2.5 Å分辨率结构和生化特征。在该结构中，RNP-8环绕聚（A）聚合酶，停靠在GLD-2表面存在的几个保守疏水热点上。RNP-8稳定GLD-2并间接刺激聚腺苷酸化。与GLD-3相比，RNP-8具有不同的氨基酸序列和结构。然而，它通过形成替代相互作用结合GLD-2的相同表面，解释了GLD-2复合物的显著多功能性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a0f4/4931106/9ba1877c5d54/1139F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a0f4/4931106/a5183119a324/1139F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a0f4/4931106/e4a82f02498a/1139F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a0f4/4931106/9ba1877c5d54/1139F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a0f4/4931106/a5183119a324/1139F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a0f4/4931106/e4a82f02498a/1139F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a0f4/4931106/9ba1877c5d54/1139F3.jpg

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