Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis

Mugridge, Jeffrey S.; Tibble, Ryan W.; Ziemniak, Marcin; Jemielity, Jacek; Gross, John D.

doi:10.1038/s41467-018-03536-x

Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis

Journal Article · Tue Mar 20 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-03536-x· OSTI ID:1624082

Mugridge, Jeffrey S. ^[1]; Tibble, Ryan W. ^[2]; Ziemniak, Marcin ^[3]; Jemielity, Jacek ^[4]; ^[2]

Univ. of California, San Francisco, CA (United States). Dept. of Pharmaceutical Chemistry; DOE/OSTI
Univ. of California, San Francisco, CA (United States). Dept. of Pharmaceutical Chemistry; Univ. of California, San Francisco, CA (United States). Dept. of Program in Chemistry and Chemical Biology
Univ. of Warsaw (Poland). Division of Biophysics, Inst. of Experimental Physics; Univ. of Warsaw (Poland). Centre of New Technologies
Univ. of Warsaw (Poland). Centre of New Technologies

The conserved decapping enzyme Dcp2 recognizes and removes the 5' eukaryotic cap from mRNA transcripts in a critical step of many cellular RNA decay pathways. Dcp2 is a dynamic enzyme that functions in concert with the essential activator Dcp1 and a diverse set of coactivators to selectively and efficiently decap target mRNAs in the cell. Here we present a 2.84 Å crystal structure of K. lactis Dcp1–Dcp2 in complex with coactivators Edc1 and Edc3, and with substrate analog bound to the Dcp2 active site. Our structure shows how Dcp2 recognizes cap substrate in the catalytically active conformation of the enzyme, and how coactivator Edc1 forms a three-way interface that bridges the domains of Dcp2 to consolidate the active conformation. Kinetic data reveal Dcp2 has selectivity for the first transcribed nucleotide during the catalytic step. The heterotetrameric Edc1–Dcp1–Dcp2–Edc3 structure shows how coactivators Edc1 and Edc3 can act simultaneously to activate decapping catalysis.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1624082

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 9; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

References (75)

Nonsense-mediated mRNA decay: novel mechanistic insights and biological impact: Nonsense-mediated mRNA decay Karousis, Evangelos D.; Nasif, Sofia; Mühlemann, Oliver Wiley Interdisciplinary Reviews: RNA, Vol. 7, Issue 5 https://doi.org/10.1002/wrna.1357	journal	May 2016
Regulation of mRNA decapping Li, You; Kiledjian, Megerditch Wiley Interdisciplinary Reviews: RNA, Vol. 1, Issue 2 https://doi.org/10.1002/wrna.15	journal	May 2010
Structures and mechanisms of Nudix hydrolases Mildvan, A. S.; Xia, Z.; Azurmendi, H. F. Archives of Biochemistry and Biophysics, Vol. 433, Issue 1 https://doi.org/10.1016/j.abb.2004.08.017	journal	January 2005
XRN 5′→3′ exoribonucleases: Structure, mechanisms and functions Nagarajan, Vinay K.; Jones, Christopher I.; Newbury, Sarah F. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, Vol. 1829, Issue 6-7 https://doi.org/10.1016/j.bbagrm.2013.03.005	journal	June 2013
Phosphate-modified analogues of m 7 GTP and m 7 Gppppm 7 G—Synthesis and biochemical properties Ziemniak, Marcin; Kowalska, Joanna; Lukaszewicz, Maciej Bioorganic & Medicinal Chemistry, Vol. 23, Issue 17 https://doi.org/10.1016/j.bmc.2015.07.052	journal	September 2015
Codon Optimality Is a Major Determinant of mRNA Stability Presnyak, Vladimir; Alhusaini, Najwa; Chen, Ying-Hsin Cell, Vol. 160, Issue 6 https://doi.org/10.1016/j.cell.2015.02.029	journal	March 2015
mRNA Decapping Is Promoted by an RNA-Binding Channel in Dcp2 Deshmukh, Mandar V.; Jones, Brittnee N.; Quang-Dang, Duc-Uy Molecular Cell, Vol. 29, Issue 3 https://doi.org/10.1016/j.molcel.2007.11.027	journal	February 2008
Structural Basis of Dcp2 Recognition and Activation by Dcp1 She, Meipei; Decker, Carolyn J.; Svergun, Dmitri I. Molecular Cell, Vol. 29, Issue 3 https://doi.org/10.1016/j.molcel.2008.01.002	journal	February 2008
Human Proline-Rich Nuclear Receptor Coregulatory Protein 2 Mediates an Interaction between mRNA Surveillance Machinery and Decapping Complex Cho, Hana; Kim, Kyoung Mi; Kim, Yoon Ki Molecular Cell, Vol. 33, Issue 1 https://doi.org/10.1016/j.molcel.2008.11.022	journal	January 2009
Mille viae in eukaryotic mRNA decapping Valkov, Eugene; Jonas, Stefanie; Weichenrieder, Oliver Current Opinion in Structural Biology, Vol. 47 https://doi.org/10.1016/j.sbi.2017.05.009	journal	December 2017
Structural Basis of the PNRC2-Mediated Link between mRNA Surveillance and Decapping Lai, Tingfeng; Cho, Hana; Liu, Zhou Structure, Vol. 20, Issue 12 https://doi.org/10.1016/j.str.2012.09.009	journal	December 2012
Functional organization of the yeast proteome by systematic analysis of protein complexes Gavin, Anne-Claude; Bösche, Markus; Krause, Roland Nature, Vol. 415, Issue 6868 https://doi.org/10.1038/415141a	journal	January 2002
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae Krogan, Nevan J.; Cagney, Gerard; Yu, Haiyuan Nature, Vol. 440, Issue 7084 https://doi.org/10.1038/nature04670	journal	March 2006
Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map Collins, Sean R.; Miller, Kyle M.; Maas, Nancy L. Nature, Vol. 446, Issue 7137 https://doi.org/10.1038/nature05649	journal	February 2007
Reversible methylation of m6Am in the 5′ cap controls mRNA stability Mauer, Jan; Luo, Xiaobing; Blanjoie, Alexandre Nature, Vol. 541, Issue 7637 https://doi.org/10.1038/nature21022	journal	December 2016
Structure and function of the bacterial decapping enzyme NudC Höfer, Katharina; Li, Sisi; Abele, Florian Nature Chemical Biology, Vol. 12, Issue 9 https://doi.org/10.1038/nchembio.2132	journal	July 2016
NMD: a multifaceted response to premature translational termination Kervestin, Stephanie; Jacobson, Allan Nature Reviews Molecular Cell Biology, Vol. 13, Issue 11 https://doi.org/10.1038/nrm3454	journal	October 2012
A split active site couples cap recognition by Dcp2 to activation Floor, Stephen N.; Jones, Brittnee N.; Hernandez, Gail A. Nature Structural & Molecular Biology, Vol. 17, Issue 9 https://doi.org/10.1038/nsmb.1879	journal	August 2010
Structural basis of mRNA-cap recognition by Dcp1–Dcp2 Mugridge, Jeffrey S.; Ziemniak, Marcin; Jemielity, Jacek Nature Structural & Molecular Biology, Vol. 23, Issue 11 https://doi.org/10.1038/nsmb.3301	journal	October 2016
mRNA decapping in 3D Coller, Jeff Nature Structural & Molecular Biology, Vol. 23, Issue 11 https://doi.org/10.1038/nsmb.3315	journal	November 2016
Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe She, Meipei; Decker, Carolyn J.; Chen, Nan Nature Structural & Molecular Biology, Vol. 13, Issue 1 https://doi.org/10.1038/nsmb1033	journal	December 2005
Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion Benton, Donald J.; Wrobel, Antoni G.; Xu, Pengqi Nature, Vol. 588, Issue 7837 https://doi.org/10.1038/s41586-020-2772-0	journal	September 2020
Linking functionally related genes by sensitive and quantitative characterization of genetic interaction profiles Decourty, L.; Saveanu, C.; Zemam, K. Proceedings of the National Academy of Sciences, Vol. 105, Issue 15 https://doi.org/10.1073/pnas.0710533105	journal	April 2008
Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme Wurm, Jan Philip; Holdermann, Iris; Overbeck, Jan H. Proceedings of the National Academy of Sciences, Vol. 114, Issue 23 https://doi.org/10.1073/pnas.1704496114	journal	May 2017
Genome-wide analysis of core promoter structures in Schizosaccharomyces pombe with DeepCAGE Li, Hua; Hou, Jingyi; Bai, Ling RNA Biology, Vol. 12, Issue 5 https://doi.org/10.1080/15476286.2015.1022704	journal	March 2015
Two Related Proteins, Edc1p and Edc2p, Stimulate mRNA Decapping in Saccharomyces cerevisiae Dunckley, Travis; Tucker, Morgan; Parker, Roy Genetics, Vol. 157, Issue 1 https://doi.org/10.1093/genetics/157.1.27	journal	January 2001
PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations Dolinsky, T. J.; Czodrowski, P.; Li, H. Nucleic Acids Research, Vol. 35, Issue Web Server https://doi.org/10.1093/nar/gkm276	journal	May 2007
Target-specific requirements for enhancers of decapping in miRNA-mediated gene silencing Eulalio, A.; Rehwinkel, J.; Stricker, M. Genes & Development, Vol. 21, Issue 20 https://doi.org/10.1101/gad.443107	journal	October 2007
Phaser crystallographic software McCoy, Airlie J.; Grosse-Kunstleve, Ralf W.; Adams, Paul D. Journal of Applied Crystallography, Vol. 40, Issue 4 https://doi.org/10.1107/s0021889807021206	journal	July 2007
MolProbity : all-atom structure validation for macromolecular crystallography Chen, Vincent B.; Arendall, W. Bryan; Headd, Jeffrey J. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 1 https://doi.org/10.1107/s0907444909042073	journal	December 2009
XDS Kabsch, Wolfgang Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2 https://doi.org/10.1107/s0907444909047337	journal	January 2010
Features and development of Coot Emsley, P.; Lohkamp, B.; Scott, W. G. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 4 https://doi.org/10.1107/s0907444910007493	journal	March 2010
From Birth to Death: The Complex Lives of Eukaryotic mRNAs Moore, M. J. Science, Vol. 309, Issue 5740 https://doi.org/10.1126/science.1111443	journal	September 2005
Identification and Analysis of the Interaction between Edc3 and Dcp2 in Saccharomyces cerevisiae Harigaya, Yuriko; Jones, Brittnee N.; Muhlrad, Denise Molecular and Cellular Biology, Vol. 30, Issue 6 https://doi.org/10.1128/mcb.01305-09	journal	January 2010
Two-headed tetraphosphate cap analogs are inhibitors of the Dcp1/2 RNA decapping complex Ziemniak, Marcin; Mugridge, Jeffrey S.; Kowalska, Joanna RNA, Vol. 22, Issue 4 https://doi.org/10.1261/rna.055152.115	journal	January 2016
The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface Wurm, Jan Philip; Overbeck, Jan; Sprangers, Remco RNA, Vol. 22, Issue 9 https://doi.org/10.1261/rna.057315.116	journal	June 2016
Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body Yu, J. H. RNA, Vol. 11, Issue 12 https://doi.org/10.1261/rna.2142405	journal	December 2005
Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition Borja, M. S.; Piotukh, K.; Freund, C. RNA, Vol. 17, Issue 2 https://doi.org/10.1261/rna.2382011	journal	December 2010
Functional characterization of the mammalian mRNA decapping enzyme hDcp2 Piccirillo, C. RNA, Vol. 9, Issue 9 https://doi.org/10.1261/rna.5690503	journal	September 2003
RNA Degradation in Saccharomyces cerevisae Parker, Roy Genetics, Vol. 191, Issue 3 https://doi.org/10.1534/genetics.111.137265	journal	July 2012
PHENIX: a comprehensive Python-based system for macromolecular structure solution. Adams, Paul D.; Afonine, Pavel V.; Bunkóczi, Gábor Apollo - University of Cambridge Repository https://doi.org/10.17863/cam.45787	text	January 2010
Exploring the gas access routes in a [NiFeSe] hydrogenase using crystals pressurized with krypton and oxygen Zacarias, Sónia; Temporão, Adriana; Carpentier, Philippe JBIC Journal of Biological Inorganic Chemistry, Vol. 25, Issue 6 https://doi.org/10.1007/s00775-020-01814-y	journal	August 2020
Computational studies of polyurethanases from Pseudomonas do Canto, Vanessa Petry; Thompson, Claudia Elizabeth; Netz, Paulo Augusto Journal of Molecular Modeling, Vol. 27, Issue 2 https://doi.org/10.1007/s00894-021-04671-x	journal	January 2021
Inference of Macromolecular Assemblies from Crystalline State Krissinel, Evgeny; Henrick, Kim Journal of Molecular Biology, Vol. 372, Issue 3 https://doi.org/10.1016/j.jmb.2007.05.022	journal	September 2007
Targeted mRNA Degradation by Deadenylation-Independent Decapping Badis, Gwenael; Saveanu, Cosmin; Fromont-Racine, Micheline Molecular Cell, Vol. 15, Issue 1 https://doi.org/10.1016/j.molcel.2004.06.028	journal	July 2004
Multiple Processing Body Factors and the ARE Binding Protein TTP Activate mRNA Decapping Fenger-Grøn, Martin; Fillman, Christy; Norrild, Bodil Molecular Cell, Vol. 20, Issue 6 https://doi.org/10.1016/j.molcel.2005.10.031	journal	December 2005
YRA1 Autoregulation Requires Nuclear Export and Cytoplasmic Edc3p-Mediated Degradation of Its Pre-mRNA Dong, Shuyun; Li, Chunfang; Zenklusen, Daniel Molecular Cell, Vol. 25, Issue 4 https://doi.org/10.1016/j.molcel.2007.01.012	journal	February 2007
Decapping of Long Noncoding RNAs Regulates Inducible Genes Geisler, Sarah; Lojek, Lisa; Khalil, Ahmad M. Molecular Cell, Vol. 45, Issue 3 https://doi.org/10.1016/j.molcel.2011.11.025	journal	February 2012
Active Site Conformational Dynamics Are Coupled to Catalysis in the mRNA Decapping Enzyme Dcp2 Aglietti, Robin A.; Floor, Stephen N.; McClendon, Chris L. Structure, Vol. 21, Issue 9 https://doi.org/10.1016/j.str.2013.06.021	journal	September 2013
Solution Structure of the Quaternary MutT−M ²⁺ −AMPCPP−M ²⁺ Complex and Mechanism of Its Pyrophosphohydrolase Action ^† ^, ^‡ Lin, Jian; Abeygunawardana, Chitrananda; Frick, David N. Biochemistry, Vol. 36, Issue 6 https://doi.org/10.1021/bi962619c	journal	February 1997
The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex: Structure of the Edc3-Dcp2 complex Fromm, Simon A.; Truffault, Vincent; Kamenz, Julia The EMBO Journal, Vol. 31, Issue 2 https://doi.org/10.1038/emboj.2011.408	journal	November 2011
Mammalian microRNAs predominantly act to decrease target mRNA levels Guo, Huili; Ingolia, Nicholas T.; Weissman, Jonathan S. Nature, Vol. 466, Issue 7308 https://doi.org/10.1038/nature09267	journal	August 2010
Genome-wide analysis of mammalian promoter architecture and evolution Carninci, Piero; Sandelin, Albin; Lenhard, Boris Nature Genetics, Vol. 38, Issue 6 https://doi.org/10.1038/ng1789	journal	April 2006
Towards a molecular understanding of microRNA-mediated gene silencing Jonas, Stefanie; Izaurralde, Elisa Nature Reviews Genetics, Vol. 16, Issue 7 https://doi.org/10.1038/nrg3965	journal	June 2015
Structure of the Dcp2–Dcp1 mRNA-decapping complex in the activated conformation Valkov, Eugene; Muthukumar, Sowndarya; Chang, Chung-Te Nature Structural & Molecular Biology, Vol. 23, Issue 6 https://doi.org/10.1038/nsmb.3232	journal	May 2016
Structure of the active form of Dcp1–Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator Charenton, Clément; Taverniti, Valerio; Gaudon-Plesse, Claudine Nature Structural & Molecular Biology, Vol. 23, Issue 11 https://doi.org/10.1038/nsmb.3300	journal	October 2016
PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome Sharma, Deepti; De Falco, Louis; Padavattan, Sivaraman Nature Communications, Vol. 10, Issue 1 https://doi.org/10.1038/s41467-019-13641-0	journal	December 2019
Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation Tillu, Vikas A.; Rae, James; Gao, Ya Nature Communications, Vol. 12, Issue 1 https://doi.org/10.1038/s41467-021-21035-4	journal	February 2021
Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan Floor, S. N.; Borja, M. S.; Gross, J. D. Proceedings of the National Academy of Sciences, Vol. 109, Issue 8 https://doi.org/10.1073/pnas.1113620109	journal	February 2012
Electrostatics of nanosystems: Application to microtubules and the ribosome Baker, N. A.; Sept, D.; Joseph, S. Proceedings of the National Academy of Sciences, Vol. 98, Issue 18, p. 10037-10041 https://doi.org/10.1073/pnas.181342398	journal	August 2001
The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif Dunckley, T. The EMBO Journal, Vol. 18, Issue 19 https://doi.org/10.1093/emboj/18.19.5411	journal	October 1999
Identification of Edc3p as an Enhancer of mRNA Decapping in Saccharomyces cerevisiae Kshirsagar, Meenakshi; Parker, Roy Genetics, Vol. 166, Issue 2 https://doi.org/10.1093/genetics/166.2.729	journal	February 2004
The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1 Chang, Chung-Te; Bercovich, Natalia; Loh, Belinda Nucleic Acids Research, Vol. 42, Issue 8 https://doi.org/10.1093/nar/gku129	journal	February 2014
Control of mRNA decapping by autoinhibition Paquette, David R.; Tibble, Ryan W.; Daifuku, Tristan S. Nucleic Acids Research, Vol. 46, Issue 12 https://doi.org/10.1093/nar/gky233	journal	March 2018
The role of disordered protein regions in the assembly of decapping complexes and RNP granules Jonas, S.; Izaurralde, E. Genes & Development, Vol. 27, Issue 24 https://doi.org/10.1101/gad.227843.113	journal	December 2013
Phaser crystallographic software McCoy, Airlie J.; Grosse-Kunstleve, Ralf W.; Adams, Paul D. Journal of Applied Crystallography, Vol. 40, Issue 4 https://doi.org/10.1107/S0021889807021206	journal	July 2007
MolProbity : all-atom structure validation for macromolecular crystallography Chen, Vincent B.; Arendall, W. Bryan; Headd, Jeffrey J. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 1 https://doi.org/10.1107/S0907444909042073	journal	December 2009
XDS Kabsch, Wolfgang Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2 https://doi.org/10.1107/S0907444909047337	journal	January 2010
PHENIX: a comprehensive Python-based system for macromolecular structure solution Adams, Paul D.; Afonine, Pavel V.; Bunkóczi, Gábor Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2, p. 213-221 https://doi.org/10.1107/S0907444909052925	journal	January 2010
Features and development of Coot Emsley, P.; Lohkamp, B.; Scott, W. G. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 4 https://doi.org/10.1107/S0907444910007493	journal	March 2010
Identification and Analysis of the Interaction between Edc3 and Dcp2 in Saccharomyces cerevisiae Harigaya, Yuriko; Jones, Brittnee N.; Muhlrad, Denise Molecular and Cellular Biology, Vol. 30, Issue 6 https://doi.org/10.1128/MCB.01305-09	journal	January 2010
Organizing Principles of Mammalian Nonsense-Mediated mRNA Decay Popp, Maximilian Wei-Lin; Maquat, Lynne E. Annual Review of Genetics, Vol. 47, Issue 1 https://doi.org/10.1146/annurev-genet-111212-133424	journal	November 2013
Control of mRNA decapping by positive and negative regulatory elements in the Dcp2 C-terminal domain He, Feng; Jacobson, Allan RNA, Vol. 21, Issue 9 https://doi.org/10.1261/rna.052449.115	journal	July 2015
Identification of Edc3p as an Enhancer of mRNA Decapping in Saccharomyces cerevisiae Kshirsagar, Meenakshi; Parker, Roy Genetics, Vol. 166, Issue 2 https://doi.org/10.1534/genetics.166.2.729	journal	February 2004
Nonsense-mediated mRNA decay: novel mechanistic insights and biological impact Karousis, Evangelos; Mühlemann, Oliver; Nasif, Sofia Wiley https://doi.org/10.7892/boris.82540	text	January 2016

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