5JNB

structure of GLD-2/RNP-8 complex

5JNB の概要

• エントリーDOI: 10.2210/pdb5jnb/pdb
• 分子名称: Poly(A) RNA polymerase gld-2, RNP (RRM RNA binding domain) containing, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: translational control, nucleotidyltransferase poly(a), polymerase, rna binding, c. elegans germline development, transferase
• 由来する生物種: Caenorhabditis elegans; 詳細
• 細胞内の位置: Cytoplasm : O17087
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 189732.41

構造登録者

Nakel, K.,Bonneau, F.,Basquin, C.,Eckmann, C.R.,Conti, E. (登録日: 2016-04-29, 公開日: 2016-06-22, 最終更新日: 2024-01-10)

主引用文献

Nakel, K.,Bonneau, F.,Basquin, C.,Habermann, B.,Eckmann, C.R.,Conti, E.
Structural basis for the antagonistic roles of RNP-8 and GLD-3 in GLD-2 poly(A)-polymerase activity.
Rna, 22:1139-1145, 2016

PubMed 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.

PubMed: 27288313
DOI: 10.1261/rna.056598.116

実験手法

X-RAY DIFFRACTION (2.486 Å)