4nkt Citations

A critical switch in the enzymatic properties of the Cid1 protein deciphered from its product-bound crystal structure.

OpenAccess logo Nucleic Acids Res. (2013)
Cited: 13 times
EuropePMC logo PMID: 24322298


The addition of uridine nucleotide by the poly(U) polymerase (PUP) enzymes has a demonstrated impact on various classes of RNAs such as microRNAs (miRNAs), histone-encoding RNAs and messenger RNAs. Cid1 protein is a member of the PUP family. We solved the crystal structure of Cid1 in complex with non-hydrolyzable UMPNPP and a short dinucleotide compound ApU. These structures revealed new residues involved in substrate/product stabilization. In particular, one of the three catalytic aspartate residues explains the RNA dependence of its PUP activity. Moreover, other residues such as residue N165 or the β-trapdoor are shown to be critical for Cid1 activity. We finally suggest that the length and sequence of Cid1 substrate RNA influence the balance between Cid1's processive and distributive activities. We propose that particular processes regulated by PUPs require the enzymes to switch between the two types of activity as shown for the miRNA biogenesis where PUPs can either promote DICER cleavage via short U-tail or trigger miRNA degradation by adding longer poly(U) tail. The enzymatic properties of these enzymes may be critical for determining their particular function in vivo.

Articles - 4nkt mentioned but not cited (2)

  1. A critical switch in the enzymatic properties of the Cid1 protein deciphered from its product-bound crystal structure. Munoz-Tello P, Gabus C, Thore S. Nucleic Acids Res. 42 3372-3380 (2014)
  2. Structural insights into a unique preference for 3' terminal guanine of mirtron in Drosophila TUTase tailor. Cheng L, Li F, Jiang Y, Yu H, Xie C, Shi Y, Gong Q. Nucleic Acids Res. 47 495-508 (2019)

Reviews citing this publication (1)

  1. Function and Regulation of Human Terminal Uridylyltransferases. Yashiro Y, Tomita K. Front Genet 9 538 (2018)

Articles citing this publication (10)

  1. Structural plasticity of Cid1 provides a basis for its distributive RNA terminal uridylyl transferase activity. Yates LA, Durrant BP, Fleurdépine S, Harlos K, Norbury CJ, Gilbert RJ. Nucleic Acids Res. 43 2968-2979 (2015)
  2. Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis. Faehnle CR, Walleshauser J, Joshua-Tor L. Nat. Struct. Mol. Biol. 24 658-665 (2017)
  3. Crystal structures of U6 snRNA-specific terminal uridylyltransferase. Yamashita S, Takagi Y, Nagaike T, Tomita K. Nat Commun 8 15788 (2017)
  4. RNA Editing TUTase 1: structural foundation of substrate recognition, complex interactions and drug targeting. Rajappa-Titu L, Suematsu T, Munoz-Tello P, Long M, Demir Ö, Cheng KJ, Stagno JR, Luecke H, Amaro RE, Aphasizheva I, Aphasizhev R, Thore S. Nucleic Acids Res. 44 10862-10878 (2016)
  5. Structural basis for the activation of the C. elegans noncanonical cytoplasmic poly(A)-polymerase GLD-2 by GLD-3. Nakel K, Bonneau F, Eckmann CR, Conti E. Proc. Natl. Acad. Sci. U.S.A. 112 8614-8619 (2015)
  6. Biochemical and structural bioinformatics studies of fungal CutA nucleotidyltransferases explain their unusual specificity toward CTP and increased tendency for cytidine incorporation at the 3'-terminal positions of synthesized tails. Kobyłecki K, Kuchta K, Dziembowski A, Ginalski K, Tomecki R. RNA 23 1902-1926 (2017)
  7. Structural basis for acceptor RNA substrate selectivity of the 3' terminal uridylyl transferase Tailor. Kroupova A, Ivascu A, Reimão-Pinto MM, Ameres SL, Jinek M. Nucleic Acids Res. 47 1030-1042 (2019)
  8. RNA surveillance by uridylation-dependent RNA decay in Schizosaccharomyces pombe. Chung CZ, Jaramillo JE, Ellis MJ, Bour DYN, Seidl LE, Jo DHS, Turk MA, Mann MR, Bi Y, Haniford DB, Duennwald ML, Heinemann IU. Nucleic Acids Res. 47 3045-3057 (2019)
  9. Structure and mechanism of CutA, RNA nucleotidyl transferase with an unusual preference for cytosine. Malik D, Kobyłecki K, Krawczyk P, Poznański J, Jakielaszek A, Napiórkowska A, Dziembowski A, Tomecki R, Nowotny M. Nucleic Acids Res 48 9387-9405 (2020)
  10. aBravo Is a Novel Aedes aegypti Antiviral Protein that Interacts with, but Acts Independently of, the Exogenous siRNA Pathway Effector Dicer 2. Varjak M, Gestuveo RJ, Burchmore R, Schnettler E, Kohl A. Viruses 12 (2020)