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

Nakel, K., Bonneau, F., Basquin, C., Habermann, B., Eckmann, C. R., & Conti, E. (2016). Structural basis for the antagonistic roles of RNP-8 and GLD-3 in GLD-2 poly(A)-polymerase activity. RNA, 22(8), 1139-1145. doi:10.1261/rna.056598.116.

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RNA-2016-Nakel-1139-45.pdf (Publisher version), 921KB
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© 2016 Nakel et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society
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 Creators:
Nakel, Katharina1, Author              
Bonneau, Fabien1, Author              
Basquin, Claire1, Author              
Habermann, Bianca2, Author              
Eckmann, Christian R.3, Author
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1832284              
3external, ou_persistent22              

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Free keywords: CYTOPLASMIC POLY(A) POLYMERASE; CAENORHABDITIS-ELEGANS GERMLINE; MESSENGER-RNA; MITOSIS/MEIOSIS DECISION; POLYADENYLATION COMPLEX; ACTIVATION; DROSOPHILA; OOGENESIS; TRANSLATION; REGULATORBiochemistry & Molecular Biology; translational regulation; cytoplasmic polyadenylation; nucleotidyl-transferase; germline development; C. elegans;
 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 resolution structure and biochemical characterization of a GLD-2-RNP-8core 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.

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Language(s): eng - English
 Dates: 2016-06-102016-12
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000386679200003
DOI: 10.1261/rna.056598.116
 Degree: -

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Title: RNA
  Subtitle : A Publication of the RNA Society
Source Genre: Journal
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Publ. Info: New York, NY : Cambridge University Press
Pages: - Volume / Issue: 22 (8) Sequence Number: - Start / End Page: 1139 - 1145 Identifier: ISSN: 1355-8382
CoNE: https://pure.mpg.de/cone/journals/resource/954925343776