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  A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting

Tritschler, F., Eulalio, A., Truffault, V., Hartmann, M., Helms, S., Schmidt, S., et al. (2007). A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. Molecular and Cellular Biology (Washington, DC), 27(24), 8600-8611. doi:10.1128/MCB.01506-07.

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 Creators:
Tritschler, F1, Author           
Eulalio, A1, Author           
Truffault, V2, Author           
Hartmann, MD2, Author           
Helms, S1, Author           
Schmidt, S1, Author           
Coles, M2, Author           
Izaurralde, E1, Author           
Weichenrieder, O1, 3, Author           
Affiliations:
1Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375718              
2Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375791              
3Retrotransposition and Regulatory RNAs Group, Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3490680              

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 Abstract: Members of the (L)Sm (Sm and Sm-like) protein family are found across all kingdoms of life and play crucial roles in RNA metabolism. The P-body component EDC3 (enhancer of decapping 3) is a divergent member of this family that functions in mRNA decapping. EDC3 is composed of a N-terminal LSm domain, a central FDF domain, and a C-terminal YjeF-N domain. We show that this modular architecture enables EDC3 to interact with multiple components of the decapping machinery, including DCP1, DCP2, and Me31B. The LSm domain mediates DCP1 binding and P-body localization. We determined the three-dimensional structures of the LSm domains of Drosophila melanogaster and human EDC3 and show that the domain adopts a divergent Sm fold that lacks the characteristic N-terminal alpha-helix and has a disrupted beta4-strand. This domain remains monomeric in solution and lacks several features that canonical (L)Sm domains require for binding RNA. The structures also revealed a conserved patch of surface residues that are required for the interaction with DCP1 but not for P-body localization. The conservation of surface and of critical structural residues indicates that LSm domains in EDC3 proteins adopt a similar fold that has separable novel functions that are absent in canonical (L)Sm proteins.

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 Dates: 2007-12
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1128/MCB.01506-07
PMID: 17923697
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Title: Molecular and Cellular Biology (Washington, DC)
  Other : Mol Cell Biol
Source Genre: Journal
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Publ. Info: American Society for Microbiology (ASM)
Pages: - Volume / Issue: 27 (24) Sequence Number: - Start / End Page: 8600 - 8611 Identifier: ISSN: 0270-7306
CoNE: https://pure.mpg.de/cone/journals/resource/954925502188