2dt7 › Citations

Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP.

Kuwasako K, He F, Inoue M, Tanaka A, Sugano S, Güntert P, Muto Y, Yokoyama S
Structure 14 1677-89 (2006)
Cited: 19 times
EuropePMC logo PMID: 17098193

Abstract

The SF3a complex, consisting of SF3a60, SF3a66, and SF3a120, in 17S U2 snRNP is crucial to spliceosomal assembly. SF3a120 contains two tandem SURP domains (SURP1 and SURP2), and SURP2 is responsible for binding to SF3a60. We found that the SURP2 fragment forms a stable complex with an SF3a60 fragment (residues 71-107) and solved its structure by NMR spectroscopy. SURP2 exhibits a fold of the alpha1-alpha2-3(10)-alpha3 topology, and the SF3a60 fragment forms an amphipathic alpha helix intimately contacting alpha1 of SURP2. We also solved the SURP1 structure, which has the same fold as SURP2. The protein-binding interface of SURP2 is quite similar to the corresponding surface of SURP1, except for two amino acid residues. One of them, Leu169, is characteristic of SF3a120 SURP2 among SURP domains. Mutagenesis showed that this single Leu residue is the critical determinant for complex formation, which reveals the protein recognition mechanism in the subunit assembly.

Reviews - 2dt7 mentioned but not cited (1)

  1. Detailed close-ups and the big picture of spliceosomes. Jurica MS. Curr Opin Struct Biol 18 315-320 (2008)

Articles - 2dt7 mentioned but not cited (4)

  1. Intrinsic disorder in the human spliceosomal proteome. Korneta I, Bujnicki JM. PLoS Comput Biol 8 e1002641 (2012)
  2. Structural bioinformatics of the human spliceosomal proteome. Korneta I, Magnus M, Bujnicki JM. Nucleic Acids Res 40 7046-7065 (2012)
  3. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)
  4. Structural basis for the interaction between the first SURP domain of the SF3A1 subunit in U2 snRNP and the human splicing factor SF1. Nameki N, Takizawa M, Suzuki T, Tani S, Kobayashi N, Sakamoto T, Muto Y, Kuwasako K. Protein Sci 31 e4437 (2022)


Articles citing this publication (14)

  1. Re-evaluation of the role of calcium homeostasis endoplasmic reticulum protein (CHERP) in cellular calcium signaling. Lin-Moshier Y, Sebastian PJ, Higgins L, Sampson ND, Hewitt JE, Marchant JS. J Biol Chem 288 355-367 (2013)
  2. Transcriptome and long noncoding RNA sequencing of three extracellular vesicle subtypes released from the human colon cancer LIM1863 cell line. Chen M, Xu R, Ji H, Greening DW, Rai A, Izumikawa K, Ishikawa H, Takahashi N, Simpson RJ. Sci Rep 6 38397 (2016)
  3. Structure and assembly of the SF3a splicing factor complex of U2 snRNP. Lin PC, Xu RM. EMBO J 31 1579-1590 (2012)
  4. Disease-Causing Mutations in SF3B1 Alter Splicing by Disrupting Interaction with SUGP1. Zhang J, Ali AM, Lieu YK, Liu Z, Gao J, Rabadan R, Raza A, Mukherjee S, Manley JL. Mol Cell 76 82-95.e7 (2019)
  5. Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins. Crisci A, Raleff F, Bagdiul I, Raabe M, Urlaub H, Rain JC, Krämer A. Nucleic Acids Res 43 10456-10473 (2015)
  6. Solution structure of the yeast URN1 splicing factor FF domain: comparative analysis of charge distributions in FF domain structures-FFs and SURPs, two domains with a similar fold. Bonet R, Ramirez-Espain X, Macias MJ. Proteins 73 1001-1009 (2008)
  7. RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing. Kuwasako K, Takahashi M, Unzai S, Tsuda K, Yoshikawa S, He F, Kobayashi N, Güntert P, Shirouzu M, Ito T, Tanaka A, Yokoyama S, Hagiwara M, Kuroyanagi H, Muto Y. Nat Struct Mol Biol 21 778-786 (2014)
  8. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses. Kuwasako K, Dohmae N, Inoue M, Shirouzu M, Taguchi S, Güntert P, Séraphin B, Muto Y, Yokoyama S. Proteins 71 1617-1636 (2008)
  9. Interaction domains and nuclear targeting signals in subunits of the U2 small nuclear ribonucleoprotein particle-associated splicing factor SF3a. Huang CJ, Ferfoglia F, Raleff F, Krämer A. J Biol Chem 286 13106-13114 (2011)
  10. Cellular stress response 1 down-regulates the expression of epidermal growth factor receptor and platelet-derived growth factor receptor through inactivation of splicing factor 3A3. Zuo ZH, Yu YP, Martin A, Luo JH. Mol Carcinog 56 315-324 (2017)
  11. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment. Kuwasako K, Nameki N, Tsuda K, Takahashi M, Sato A, Tochio N, Inoue M, Terada T, Kigawa T, Kobayashi N, Shirouzu M, Ito T, Sakamoto T, Wakamatsu K, Güntert P, Takahashi S, Yokoyama S, Muto Y. Protein Sci 26 280-291 (2017)
  12. Proteins associated with SF3a60 in T. brucei. Nyambega B, Helbig C, Masiga DK, Clayton C, Levin MJ. PLoS One 9 e91956 (2014)
  13. Chromatin-Associated Protein Sugp2 Involved in mRNA Alternative Splicing During Mouse Spermatogenesis. Zhan J, Li J, Wu Y, Wu P, Yu Z, Cui P, Zhou M, Xu Y, Jin T, Du Z, Luo M, Liu C. Front Vet Sci 8 754021 (2021)
  14. In silico identification, characterization, and expression analysis of RNA recognition motif (RRM) containing RNA-binding proteins in Aedes aegypti. Sumitha MK, Kalimuthu M, Aarthy M, Paramasivan R, Kumar A, Gupta B. Parasitol Res 122 2847-2857 (2023)


Quick links