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  Molecular Basis for poly(A) RNP Architecture and Recognition by the Pan2-Pan3 Deadenylase

Schäfer, I. B., Yamashita, M., Schuller, J. M., Schüssler, S., Reichelt, P., Strauss, M., et al. (2019). Molecular Basis for poly(A) RNP Architecture and Recognition by the Pan2-Pan3 Deadenylase. Cell, 177(6), 1619-1631.e21. doi:10.1016/j.cell.2019.04.013.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-E98D-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-E98E-7
Genre: Journal Article

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 Creators:
Schäfer, Ingmar B.1, Author              
Yamashita, Masami1, Author              
Schuller, Jan Michael1, Author              
Schüssler, Steffen1, Author              
Reichelt, Peter1, Author              
Strauss, Mike2, Author              
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              

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Free keywords: LABELED POLYRIBOSOMAL RNA; TAIL LENGTH CONTROL; MESSENGER-RNA; POLY(A)-BINDING PROTEIN; BINDING-PROTEIN; CRYO-EM; REPEATING STRUCTURE; CCR4-NOT COMPLEX; ADENYLIC ACID; HELA-CELLSBiochemistry & Molecular Biology; Cell Biology;
 Abstract: The stability of eukaryotic mRNAs is dependent on a ribonucleoprotein (RNP) complex of poly(A)-binding proteins (PABPC1/Pab1) organized on the poly(A) tail. This poly(A) RNP not only protects mRNAs from premature degradation but also stimulates the Pan2-Pan3 deadenylase complex to catalyze the first step of poly(A) tail shortening. We reconstituted this process in vitro using recombinant proteins and show that Pan2-Pan3 associates with and degrades poly(A) RNPs containing two or more Pab1 molecules. The cryo-EM structure of Pan2-Pan3 in complex with a poly(A) RNP composed of 90 adenosines and three Pab1 protomers shows how the oligomerization interfaces of Pab1 are recognized by conserved features of the deadenylase and thread the poly(A) RNA substrate into the nuclease active site. The structure reveals the basis for the periodic repeating architecture at the 3' end of cytoplasmic mRNAs. This illustrates mechanistically how RNA-bound Pab1 oligomers act as rulers for poly(A) tail length over the mRNAs' lifetime.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 34
 Publishing info: -
 Table of Contents: We would like to thank ... the MPIB cryo-EM, and core facilities ...
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Project name : ERC Advanced Investigator Grants DEAD2THEEND and EXORICO
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Funding program : -
Funding organization : European Commission
Project name : DFG SFB1035 and GRK1721
Grant ID : -
Funding program : -
Funding organization : Deutsche Forschungsgemeinschaft

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Title: Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 177 (6) Sequence Number: - Start / End Page: 1619 - 1631.e21 Identifier: ISSN: 0092-8674
CoNE: https://pure.mpg.de/cone/journals/resource/954925463183