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Xiang, K., Nagaike, T., Xiang, S., Kilic, T., Beh, M. M., Manley, J. L., & Tong, L. (2010). Crystal structure of the human symplekin–Ssu72–CTD phosphopeptide complex. Nature, 467(7316), 729–733.

Authors 7
  1. Kehui Xiang (first)
  2. Takashi Nagaike (additional)
  3. Song Xiang (additional)
  4. Turgay Kilic (additional)
  5. Maia M. Beh (additional)
  6. James L. Manley (additional)
  7. Liang Tong (additional)
References 42 Referenced 152
  1. Takagaki, Y. & Manley, J. L. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol. Cell. Biol. 20, 1515–1525 (2000) (10.1128/MCB.20.5.1515-1525.2000) / Mol. Cell. Biol. by Y Takagaki (2000)
  2. Zhao, J., Kessler, M. M., Helmling, S., O’Connor, J. P. & Moore, C. L. Pta1, a component of yeast CFII, is required for both cleavage and poly(A) addition of mRNA precursor. Mol. Cell. Biol. 19, 7733–7740 (1999) (10.1128/MCB.19.11.7733) / Mol. Cell. Biol. by J Zhao (1999)
  3. Zhao, J., Hyman, L. & Moore, C. L. Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis. Microbiol. Mol. Biol. Rev. 63, 405–445 (1999) (10.1128/MMBR.63.2.405-445.1999) / Microbiol. Mol. Biol. Rev. by J Zhao (1999)
  4. Mandel, C. R., Bai, Y. & Tong, L. Protein factors in pre-mRNA 3′-end processing. Cell. Mol. Life Sci. 65, 1099–1122 (2008) (10.1007/s00018-007-7474-3) / Cell. Mol. Life Sci. by CR Mandel (2008)
  5. Calvo, O. & Manley, J. L. Strange bedfellows: polyadenylation factors at the promoter. Genes Dev. 17, 1321–1327 (2003) (10.1101/gad.1093603) / Genes Dev. by O Calvo (2003)
  6. Moore, M. J. & Proudfoot, N. J. Pre-mRNA processing reaches back to transcription and ahead to translation. Cell 136, 688–700 (2009) (10.1016/j.cell.2009.02.001) / Cell by MJ Moore (2009)
  7. He, X. et al. Functional interactions between the transcription and mRNA 3′ end processing machineries mediated by Ssu72 and Sub1. Genes Dev. 17, 1030–1042 (2003) (10.1101/gad.1075203) / Genes Dev. by X He (2003)
  8. Nedea, E. et al. Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3′-ends. J. Biol. Chem. 278, 33000–33010 (2003) (10.1074/jbc.M304454200) / J. Biol. Chem. by E Nedea (2003)
  9. Ghazy, M. A., He, X., Singh, B. N., Hampsey, M. & Moore, C. The essential N terminus of the Pta1 scaffold protein is required for snoRNA transcription termination and Ssu72 function but is dispensible for pre-mRNA 3′-end processing. Mol. Cell. Biol. 29, 2296–2307 (2009) (10.1128/MCB.01514-08) / Mol. Cell. Biol. by MA Ghazy (2009)
  10. Dichtl, B. et al. A role for SSU72 in balancing RNA polymerase II transcription elongation and termination. Mol. Cell 10, 1139–1150 (2002) (10.1016/S1097-2765(02)00707-4) / Mol. Cell by B Dichtl (2002)
  11. Meinhart, A., Silberzahn, T. & Cramer, P. The mRNA transcription/processing factor Ssu72 is a potential tyrosine phosphatase. J. Biol. Chem. 278, 15917–15921 (2003) (10.1074/jbc.M301643200) / J. Biol. Chem. by A Meinhart (2003)
  12. Ganem, C. et al. Ssu72 is a phosphatase essential for transcription termination of snoRNAs and specific mRNAs in yeast. EMBO J. 22, 1588–1598 (2003) (10.1093/emboj/cdg141) / EMBO J. by C Ganem (2003)
  13. Krishnamurthy, S., He, X., Reyes-Reyes, M., Moore, C. L. & Hampsey, M. Ssu72 is an RNA polymerase II CTD phosphatase. Mol. Cell 14, 387–394 (2004) (10.1016/S1097-2765(04)00235-7) / Mol. Cell by S Krishnamurthy (2004)
  14. Hausmann, S., Koiwa, H., Krishnamurthy, S., Hampsey, M. & Shuman, S. Different strategies for carboxyl-terminal domain (CTD) recognition by serine 5-specific CTD phosphatases. J. Biol. Chem. 280, 37681–37688 (2005) (10.1074/jbc.M505292200) / J. Biol. Chem. by S Hausmann (2005)
  15. St-Pierre, B. et al. Conserved and specific functions of mammalian ssu72. Nucleic Acids Res. 33, 464–477 (2005) (10.1093/nar/gki171) / Nucleic Acids Res. by B St-Pierre (2005)
  16. Reyes-Reyes, M. & Hampsey, M. Role for the Ssu72 C-terminal domain phosphatase in RNA polymerase II transcription elongation. Mol. Cell. Biol. 27, 926–936 (2007) (10.1128/MCB.01361-06) / Mol. Cell. Biol. by M Reyes-Reyes (2007)
  17. Ansari, A. & Hampsey, M. A role for the CPF 3′-end processing machinery in RNAP II-dependent gene looping. Genes Dev. 19, 2969–2978 (2005) (10.1101/gad.1362305) / Genes Dev. by A Ansari (2005)
  18. Su, X.-D., Taddei, N., Stefani, M., Ramponi, G. & Nordlund, P. The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature 370, 575–578 (1994) (10.1038/370575a0) / Nature by X-D Su (1994)
  19. Zhang, M., Van Etten, R. L. & Stauffacher, C. V. Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-Å resolution. Biochemistry 33, 11097–11105 (1994) (10.1021/bi00203a006) / Biochemistry by M Zhang (1994)
  20. Meinhart, A., Kamenski, T., Hoeppner, S., Baumli, S. & Cramer, P. A structural perspective of CTD function. Genes Dev. 19, 1401–1415 (2005) (10.1101/gad.1318105) / Genes Dev. by A Meinhart (2005)
  21. Zhang, Y. et al. Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1. Mol. Cell 24, 759–770 (2006) (10.1016/j.molcel.2006.10.027) / Mol. Cell by Y Zhang (2006)
  22. Kennedy, S. A. et al. Crystal structure of the HEAT domain from the pre-mRNA processing factor symplekin. J. Mol. Biol. 392, 115–128 (2009) (10.1016/j.jmb.2009.06.062) / J. Mol. Biol. by SA Kennedy (2009)
  23. Xu, Y.-X., Hirose, Y., Zhou, X. Z., Lu, K. P. & Manley, J. L. Pin1 modulates the structure and function of human RNA polymerase II. Genes Dev. 17, 2765–2776 (2003) (10.1101/gad.1135503) / Genes Dev. by Y-X Xu (2003)
  24. Krishnamurthy, S., Ghazy, M. A., Moore, C. & Hampsey, M. Functional interaction of the Ess1 prolyl isomerase with components of the RNA polymerase II initiation and termination machineries. Mol. Cell. Biol. 29, 2925–2934 (2009) (10.1128/MCB.01655-08) / Mol. Cell. Biol. by S Krishnamurthy (2009)
  25. Singh, N. et al. The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathway. Mol. Cell 36, 255–266 (2009) (10.1016/j.molcel.2009.08.018) / Mol. Cell by N Singh (2009)
  26. Hirose, Y. & Manley, J. L. RNA polymerase II is an essential mRNA polyadenylation factor. Nature 395, 93–96 (1998) (10.1038/25786) / Nature by Y Hirose (1998)
  27. Rozenblatt-Rosen, O. et al. The tumor suppressor Cdc73 functionally associates with CPSF and CstF 3′ mRNA processing factors. Proc. Natl Acad. Sci. USA 106, 755–760 (2009) (10.1073/pnas.0812023106) / Proc. Natl Acad. Sci. USA by O Rozenblatt-Rosen (2009)
  28. Shi, Y. et al. Molecular architecture of the human pre-mRNA 3′ processing complex. Mol. Cell 33, 365–376 (2009) (10.1016/j.molcel.2008.12.028) / Mol. Cell by Y Shi (2009)
  29. Takagaki, Y., Ryner, L. C. & Manley, J. L. Separation and characterization of a poly(A) polymerase and a cleavage/specificity factor required for pre-mRNA polyadenylation. Cell 52, 731–742 (1988) (10.1016/0092-8674(88)90411-4) / Cell by Y Takagaki (1988)
  30. McCracken, S. et al. The C-terminal domain of RNA polymerase II couples mRNA processing to transcription. Nature 385, 357–361 (1997) (10.1038/385357a0) / Nature by S McCracken (1997)
  31. Hendrickson, W. A., Horton, J. R. & LeMaster, D. M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9, 1665–1672 (1990) (10.1002/j.1460-2075.1990.tb08287.x) / EMBO J. by WA Hendrickson (1990)
  32. Hendrickson, W. A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51–58 (1991) (10.1126/science.1925561) / Science by WA Hendrickson (1991)
  33. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 (1997) (10.1016/S0076-6879(97)76066-X) / Methods Enzymol. by Z Otwinowski (1997)
  34. Weeks, C. M. & Miller, R. The design and implementation of SnB v2.0. J. Appl. Cryst. 32, 120–124 (1999) (10.1107/S0021889898010504) / J. Appl. Cryst. by CM Weeks (1999)
  35. Terwilliger, T. C. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374, 22–37 (2003) (10.1016/S0076-6879(03)74002-6) / Methods Enzymol. by TC Terwilliger (2003)
  36. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 (1991) (10.1107/S0108767390010224) / Acta Crystallogr. A by TA Jones (1991)
  37. Emsley, P. & Cowtan, K. D. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126–2132 (2004) (10.1107/S0907444904019158) / Acta Crystallogr. D Biol. Crystallogr. by P Emsley (2004)
  38. Brunger, A. T. et al. Crystallography & NMR System: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905–921 (1998) (10.1107/S0907444998003254) / Acta Crystallogr. D Biol. Crystallogr. by AT Brunger (1998)
  39. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53, 240–255 (1997) (10.1107/S0907444996012255) / Acta Crystallogr. D Biol. Crystallogr. by GN Murshudov (1997)
  40. Jogl, G., Tao, X., Xu, Y. & Tong, L. COMO: A program for combined molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 57, 1127–1134 (2001) (10.1107/S0907444901006783) / Acta Crystallogr. D Biol. Crystallogr. by G Jogl (2001)
  41. Hirose, Y. & Manley, J. L. RNA polymerase II is an essential mRNA polyadenylation factor. Nature 395, 93–96 (1998) (10.1038/25786) / Nature by Y Hirose (1998)
  42. Chapman, R. D. et al. Transcribing RNA polymerase II is phosphorylated at CTD residue serine-7. Science 318, 1780–1782 (2007) (10.1126/science.1145977) / Science by RD Chapman (2007)
Dates
Type When
Created 14 years, 11 months ago (Sept. 22, 2010, 12:58 p.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 1:46 p.m.)
Indexed 1 month ago (Aug. 2, 2025, 1:22 a.m.)
Issued 14 years, 11 months ago (Sept. 22, 2010)
Published 14 years, 11 months ago (Sept. 22, 2010)
Published Online 14 years, 11 months ago (Sept. 22, 2010)
Published Print 14 years, 11 months ago (Oct. 1, 2010)
Funders 0

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@article{Xiang_2010, title={Crystal structure of the human symplekin–Ssu72–CTD phosphopeptide complex}, volume={467}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature09391}, DOI={10.1038/nature09391}, number={7316}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Xiang, Kehui and Nagaike, Takashi and Xiang, Song and Kilic, Turgay and Beh, Maia M. and Manley, James L. and Tong, Liang}, year={2010}, month=sep, pages={729–733} }