메뉴 건너뛰기




Volumn 10, Issue 10, 2015, Pages 2405-2414

Chemical Tools to Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN; NUCLEOPHILE; PEPTIDOMIMETIC AGENT; PHOSPHATASE; PROLINE; RNA POLYMERASE II; PHOSPHOPROTEIN PHOSPHATASE;

EID: 84944745055     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b00296     Document Type: Article
Times cited : (23)

References (42)
  • 1
    • 84888991588 scopus 로고    scopus 로고
    • The RNA polymerase II carboxy-terminal domain (CTD) code
    • Eick, D. and Geyer, M. (2013) The RNA polymerase II carboxy-terminal domain (CTD) code Chem. Rev. (Washington, DC, U. S.) 113, 8456-8490 10.1021/cr400071f
    • (2013) Chem. Rev. (Washington, DC, U. S.) , vol.113 , pp. 8456-8490
    • Eick, D.1    Geyer, M.2
  • 2
    • 84856273602 scopus 로고    scopus 로고
    • A universal RNA polymerase II CTD cycle is orchestrated by complex interplays between kinase, phosphatase, and isomerase enzymes along genes
    • Bataille, A. R., Jeronimo, C., Jacques, P. E., Laramee, L., Fortin, M. E., Forest, A., Bergeron, M., Hanes, S. D., and Robert, F. (2012) A universal RNA polymerase II CTD cycle is orchestrated by complex interplays between kinase, phosphatase, and isomerase enzymes along genes Mol. Cell 45, 158-170 10.1016/j.molcel.2011.11.024
    • (2012) Mol. Cell , vol.45 , pp. 158-170
    • Bataille, A.R.1    Jeronimo, C.2    Jacques, P.E.3    Laramee, L.4    Fortin, M.E.5    Forest, A.6    Bergeron, M.7    Hanes, S.D.8    Robert, F.9
  • 3
    • 70449641057 scopus 로고    scopus 로고
    • Progression through the RNA polymerase II CTD cycle
    • Buratowski, S. (2009) Progression through the RNA polymerase II CTD cycle Mol. Cell 36, 541-546 10.1016/j.molcel.2009.10.019
    • (2009) Mol. Cell , vol.36 , pp. 541-546
    • Buratowski, S.1
  • 6
    • 84896933783 scopus 로고    scopus 로고
    • The Ess1 prolyl isomerase: Traffic cop of the RNA polymerase II transcription cycle
    • Hanes, S. D. (2014) The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle Biochim. Biophys. Acta, Gene Regul. Mech. 1839, 316-333 10.1016/j.bbagrm.2014.02.001
    • (2014) Biochim. Biophys. Acta, Gene Regul. Mech. , vol.1839 , pp. 316-333
    • Hanes, S.D.1
  • 7
    • 34548660854 scopus 로고    scopus 로고
    • Prolyl cis-trans isomerization as a molecular timer
    • Lu, K. P., Finn, G., Lee, T. H., and Nicholson, L. K. (2007) Prolyl cis-trans isomerization as a molecular timer Nat. Chem. Biol. 3, 619-629 10.1038/nchembio.2007.35
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 619-629
    • Lu, K.P.1    Finn, G.2    Lee, T.H.3    Nicholson, L.K.4
  • 9
    • 0347361694 scopus 로고    scopus 로고
    • The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae
    • Wu, X., Rossettini, A., and Hanes, S. D. (2003) The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae Genetics 165, 1687-1702
    • (2003) Genetics , vol.165 , pp. 1687-1702
    • Wu, X.1    Rossettini, A.2    Hanes, S.D.3
  • 10
    • 0034679626 scopus 로고    scopus 로고
    • The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery
    • Wu, X., Wilcox, C. B., Devasahayam, G., Hackett, R. L., Arevalo-Rodriguez, M., Cardenas, M. E., Heitman, J., and Hanes, S. D. (2000) The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery EMBO J. 19, 3727-3738 10.1093/emboj/19.14.3727
    • (2000) EMBO J. , vol.19 , pp. 3727-3738
    • Wu, X.1    Wilcox, C.B.2    Devasahayam, G.3    Hackett, R.L.4    Arevalo-Rodriguez, M.5    Cardenas, M.E.6    Heitman, J.7    Hanes, S.D.8
  • 11
    • 0344011538 scopus 로고    scopus 로고
    • Pin1 modulates the structure and function of human RNA polymerase II
    • Xu, Y. X., Hirose, Y., Zhou, X. Z., Lu, K. P., and Manley, J. L. (2003) Pin1 modulates the structure and function of human RNA polymerase II Genes Dev. 17, 2765-2776 10.1101/gad.1135503
    • (2003) Genes Dev. , vol.17 , pp. 2765-2776
    • Xu, Y.X.1    Hirose, Y.2    Zhou, X.Z.3    Lu, K.P.4    Manley, J.L.5
  • 12
    • 55949110622 scopus 로고    scopus 로고
    • The structure of Fcp1, an essential RNA polymerase II CTD phosphatase
    • Ghosh, A., Shuman, S., and Lima, C. D. (2008) The structure of Fcp1, an essential RNA polymerase II CTD phosphatase Mol. Cell 32, 478-490 10.1016/j.molcel.2008.09.021
    • (2008) Mol. Cell , vol.32 , pp. 478-490
    • Ghosh, A.1    Shuman, S.2    Lima, C.D.3
  • 13
  • 14
    • 12844250536 scopus 로고    scopus 로고
    • Small CTD phosphatases function in silencing neuronal gene expression
    • Yeo, M., Lee, S. K., Lee, B., Ruiz, E. C., Pfaff, S. L., and Gill, G. N. (2005) Small CTD phosphatases function in silencing neuronal gene expression Science 307, 596-600 10.1126/science.1100801
    • (2005) Science , vol.307 , pp. 596-600
    • Yeo, M.1    Lee, S.K.2    Lee, B.3    Ruiz, E.C.4    Pfaff, S.L.5    Gill, G.N.6
  • 15
    • 33751538328 scopus 로고    scopus 로고
    • Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1
    • Zhang, Y., Kim, Y., Genoud, N., Gao, J., Kelly, J. W., Pfaff, S. L., Gill, G. N., Dixon, J. E., and Noel, J. P. (2006) Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1 Mol. Cell 24, 759-770 10.1016/j.molcel.2006.10.027
    • (2006) Mol. Cell , vol.24 , pp. 759-770
    • Zhang, Y.1    Kim, Y.2    Genoud, N.3    Gao, J.4    Kelly, J.W.5    Pfaff, S.L.6    Gill, G.N.7    Dixon, J.E.8    Noel, J.P.9
  • 16
    • 0036863611 scopus 로고    scopus 로고
    • A role for SSU72 in balancing RNA polymerase II transcription elongation and termination
    • Dichtl, B., Blank, D., Ohnacker, M., Friedlein, A., Roeder, D., Langen, H., and Keller, W. (2002) A role for SSU72 in balancing RNA polymerase II transcription elongation and termination Mol. Cell 10, 1139-1150 10.1016/S1097-2765(02)00707-4
    • (2002) Mol. Cell , vol.10 , pp. 1139-1150
    • Dichtl, B.1    Blank, D.2    Ohnacker, M.3    Friedlein, A.4    Roeder, D.5    Langen, H.6    Keller, W.7
  • 17
    • 0345269802 scopus 로고    scopus 로고
    • Ssu72 is a phosphatase essential for transcription termination of snoRNAs and specific mRNAs in yeast
    • Ganem, C., Devaux, F., Torchet, C., Jacq, C., Quevillon-Cheruel, S., Labesse, G., Facca, C., and Faye, G. (2003) Ssu72 is a phosphatase essential for transcription termination of snoRNAs and specific mRNAs in yeast EMBO J. 22, 1588-1598 10.1093/emboj/cdg141
    • (2003) EMBO J. , vol.22 , pp. 1588-1598
    • Ganem, C.1    Devaux, F.2    Torchet, C.3    Jacq, C.4    Quevillon-Cheruel, S.5    Labesse, G.6    Facca, C.7    Faye, G.8
  • 18
    • 0035893314 scopus 로고    scopus 로고
    • Opposing effects of Ctk1 kinase and Fcp1 phosphatase at ser 2 of the RNA polymerase II C-terminal domain
    • Cho, E. J., Kobor, M. S., Kim, M., Greenblatt, J., and Buratowski, S. (2001) Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain Genes Dev. 15, 3319-3329 10.1101/gad.935901
    • (2001) Genes Dev. , vol.15 , pp. 3319-3329
    • Cho, E.J.1    Kobor, M.S.2    Kim, M.3    Greenblatt, J.4    Buratowski, S.5
  • 19
    • 0033564705 scopus 로고    scopus 로고
    • A protein phosphatase functions to recycle RNA polymerase II
    • Cho, H., Kim, T. K., Mancebo, H., Lane, W. S., Flores, O., and Reinberg, D. (1999) A protein phosphatase functions to recycle RNA polymerase II Genes Dev. 13, 1540-1552 10.1101/gad.13.12.1540
    • (1999) Genes Dev. , vol.13 , pp. 1540-1552
    • Cho, H.1    Kim, T.K.2    Mancebo, H.3    Lane, W.S.4    Flores, O.5    Reinberg, D.6
  • 20
    • 0016711868 scopus 로고
    • Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts, J. F., Halvorson, H. R., and Brennan, M. (1975) Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues Biochemistry 14, 4953-4963 10.1021/bi00693a026
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 21
    • 0000882208 scopus 로고
    • Hypothesis about the function of membrane-buried proline residues in transport proteins
    • Brandl, C. J. and Deber, C. M. (1986) Hypothesis about the function of membrane-buried proline residues in transport proteins Proc. Natl. Acad. Sci. U. S. A. 83, 917-921 10.1073/pnas.83.4.917
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 917-921
    • Brandl, C.J.1    Deber, C.M.2
  • 22
    • 0037126686 scopus 로고    scopus 로고
    • Proline cis-trans isomerization and protein folding
    • Wedemeyer, W. J., Welker, E., and Scheraga, H. A. (2002) Proline cis-trans isomerization and protein folding Biochemistry 41, 14637-14644 10.1021/bi020574b
    • (2002) Biochemistry , vol.41 , pp. 14637-14644
    • Wedemeyer, W.J.1    Welker, E.2    Scheraga, H.A.3
  • 23
    • 84928101953 scopus 로고    scopus 로고
    • Stereospecific phosphorylation by the central mitotic kinase Cdk1-cyclin B
    • Etzkorn, F. A. and Zhao, S. (2015) Stereospecific phosphorylation by the central mitotic kinase Cdk1-cyclin B ACS Chem. Biol. 10, 952-956 10.1021/cb500815b
    • (2015) ACS Chem. Biol. , vol.10 , pp. 952-956
    • Etzkorn, F.A.1    Zhao, S.2
  • 25
    • 0344951058 scopus 로고    scopus 로고
    • Serine-cis-proline and serine-trans-proline isosteres: Stereoselective synthesis of (Z)- and (E)-alkene mimics by Still-Wittig and Ireland-Claisen rearrangements
    • Wang, X. J., Hart, S. A., Xu, B., Mason, M. D., Goodell, J. R., and Etzkorn, F. A. (2003) Serine-cis-proline and serine-trans-proline isosteres: stereoselective synthesis of (Z)- and (E)-alkene mimics by Still-Wittig and Ireland-Claisen rearrangements J. Org. Chem. 68, 2343-2349 10.1021/jo026663b
    • (2003) J. Org. Chem. , vol.68 , pp. 2343-2349
    • Wang, X.J.1    Hart, S.A.2    Xu, B.3    Mason, M.D.4    Goodell, J.R.5    Etzkorn, F.A.6
  • 26
    • 9644302270 scopus 로고    scopus 로고
    • Conformationally locked isostere of phosphoSer-cis-Pro inhibits Pin1 23-fold better than phosphoSer-trans-Pro isostere
    • Wang, X. J., Xu, B., Mullins, A. B., Neiler, F. K., and Etzkorn, F. A. (2004) Conformationally locked isostere of phosphoSer-cis-Pro inhibits Pin1 23-fold better than phosphoSer-trans-Pro isostere J. Am. Chem. Soc. 126, 15533-15542 10.1021/ja046396m
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15533-15542
    • Wang, X.J.1    Xu, B.2    Mullins, A.B.3    Neiler, F.K.4    Etzkorn, F.A.5
  • 28
    • 33751090746 scopus 로고    scopus 로고
    • Phosphorylation and functions of the RNA polymerase II CTD
    • Phatnani, H. P. and Greenleaf, A. L. (2006) Phosphorylation and functions of the RNA polymerase II CTD Genes Dev. 20, 2922-2936 10.1101/gad.1477006
    • (2006) Genes Dev. , vol.20 , pp. 2922-2936
    • Phatnani, H.P.1    Greenleaf, A.L.2
  • 29
    • 84865845346 scopus 로고    scopus 로고
    • Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1
    • Kubicek, K., Cerna, H., Holub, P., Pasulka, J., Hrossova, D., Loehr, F., Hofr, C., Vanacova, S., and Stefl, R. (2012) Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1 Genes Dev. 26, 1891-1896 10.1101/gad.192781.112
    • (2012) Genes Dev. , vol.26 , pp. 1891-1896
    • Kubicek, K.1    Cerna, H.2    Holub, P.3    Pasulka, J.4    Hrossova, D.5    Loehr, F.6    Hofr, C.7    Vanacova, S.8    Stefl, R.9
  • 30
    • 79953127123 scopus 로고    scopus 로고
    • Cis-Proline-mediated Ser(P)5 dephosphorylation by the RNA polymerase II C-terminal domain phosphatase Ssu72
    • Werner-Allen, J. W., Lee, C. J., Liu, P., Nicely, N. I., Wang, S., Greenleaf, A. L., and Zhou, P. (2011) cis-Proline-mediated Ser(P)5 dephosphorylation by the RNA polymerase II C-terminal domain phosphatase Ssu72 J. Biol. Chem. 286, 5717-5726 10.1074/jbc.M110.197129
    • (2011) J. Biol. Chem. , vol.286 , pp. 5717-5726
    • Werner-Allen, J.W.1    Lee, C.J.2    Liu, P.3    Nicely, N.I.4    Wang, S.5    Greenleaf, A.L.6    Zhou, P.7
  • 31
    • 77958018260 scopus 로고    scopus 로고
    • Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex
    • Xiang, K., Nagaike, T., Xiang, S., Kilic, T., Beh, M. M., Manley, J. L., and Tong, L. (2010) Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex Nature 467, 729-733 10.1038/nature09391
    • (2010) Nature , vol.467 , pp. 729-733
    • Xiang, K.1    Nagaike, T.2    Xiang, S.3    Kilic, T.4    Beh, M.M.5    Manley, J.L.6    Tong, L.7
  • 32
    • 79952180042 scopus 로고    scopus 로고
    • Crystal structure of Ssu72, an essential eukaryotic phosphatase specific for the C-terminal domain of RNA polymerase II, in complex with a transition state analogue
    • Zhang, Y., Zhang, M., and Zhang, Y. (2011) Crystal structure of Ssu72, an essential eukaryotic phosphatase specific for the C-terminal domain of RNA polymerase II, in complex with a transition state analogue Biochem. J. 434, 435-444 10.1042/BJ20101471
    • (2011) Biochem. J. , vol.434 , pp. 435-444
    • Zhang, Y.1    Zhang, M.2    Zhang, Y.3
  • 33
    • 84884621009 scopus 로고    scopus 로고
    • Novel modifications on C-terminal domain of RNA polymerase II can fine-tune the phosphatase activity of Ssu72
    • Luo, Y., Yogesha, S. D., Cannon, J. R., Yan, W., Ellington, A. D., Brodbelt, J. S., and Zhang, Y. (2013) novel modifications on C-terminal domain of RNA polymerase II can fine-tune the phosphatase activity of Ssu72 ACS Chem. Biol. 8, 2042-2052 10.1021/cb400229c
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2042-2052
    • Luo, Y.1    Yogesha, S.D.2    Cannon, J.R.3    Yan, W.4    Ellington, A.D.5    Brodbelt, J.S.6    Zhang, Y.7
  • 34
    • 0345373987 scopus 로고    scopus 로고
    • Functional interactions between the transcription and mRNA 3′ end processing machineries mediated by Ssu72 and Sub1
    • He, X., Khan, A. U., Cheng, H., Pappas, D. L., Jr., Hampsey, M., and Moore, C. L. (2003) Functional interactions between the transcription and mRNA 3′ end processing machineries mediated by Ssu72 and Sub1 Genes Dev. 17, 1030-1042 10.1101/gad.1075203
    • (2003) Genes Dev. , vol.17 , pp. 1030-1042
    • He, X.1    Khan, A.U.2    Cheng, H.3    Pappas, D.L.4    Hampsey, M.5    Moore, C.L.6
  • 35
    • 33846611494 scopus 로고    scopus 로고
    • Role for the Ssu72 C-terminal domain phosphatase in RNA polymerase II transcription elongation
    • Reyes-Reyes, M. and Hampsey, M. (2007) Role for the Ssu72 C-terminal domain phosphatase in RNA polymerase II transcription elongation Mol. Cell. Biol. 27, 926-936 10.1128/MCB.01361-06
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 926-936
    • Reyes-Reyes, M.1    Hampsey, M.2
  • 37
    • 0037181170 scopus 로고    scopus 로고
    • Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1
    • Kops, O., Zhou, X. Z., and Lu, K. P. (2002) Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1 FEBS Lett. 513, 305-311 10.1016/S0014-5793(02)02288-3
    • (2002) FEBS Lett. , vol.513 , pp. 305-311
    • Kops, O.1    Zhou, X.Z.2    Lu, K.P.3
  • 38
    • 0032951711 scopus 로고    scopus 로고
    • Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3′-end formation of a pre-mRNA in Saccharomyces cerevisiae
    • Hani, J., Schelbert, B., Bernhardt, A., Domdey, H., Fischer, G., Wiebauer, K., and Rahfeld, J. U. (1999) Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in 3′-end formation of a pre-mRNA in Saccharomyces cerevisiae J. Biol. Chem. 274, 108-116 10.1074/jbc.274.1.108
    • (1999) J. Biol. Chem. , vol.274 , pp. 108-116
    • Hani, J.1    Schelbert, B.2    Bernhardt, A.3    Domdey, H.4    Fischer, G.5    Wiebauer, K.6    Rahfeld, J.U.7
  • 39
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • Verdecia, M. A., Bowman, M. E., Lu, K. P., Hunter, T., and Noel, J. P. (2000) Structural basis for phosphoserine-proline recognition by group IV WW domains Nat. Struct. Biol. 7, 639-643 10.1038/77929
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 40
    • 0345735669 scopus 로고    scopus 로고
    • Dephosphorylation of RNA polymerase II by CTD-phosphatase FCP1 is inhibited by phospho-CTD associating proteins
    • Palancade, B., Marshall, N. F., Tremeau-Bravard, A., Bensaude, O., Dahmus, M. E., and Dubois, M. F. (2004) Dephosphorylation of RNA polymerase II by CTD-phosphatase FCP1 is inhibited by phospho-CTD associating proteins J. Mol. Biol. 335, 415-424 10.1016/j.jmb.2003.10.036
    • (2004) J. Mol. Biol. , vol.335 , pp. 415-424
    • Palancade, B.1    Marshall, N.F.2    Tremeau-Bravard, A.3    Bensaude, O.4    Dahmus, M.E.5    Dubois, M.F.6
  • 42
    • 0036535975 scopus 로고    scopus 로고
    • Pinning down proline-directed phosphorylation signaling
    • Lu, K. P., Liou, Y. C., and Zhou, X. Z. (2002) Pinning down proline-directed phosphorylation signaling Trends Cell Biol. 12, 164-172 10.1016/S0962-8924(02)02253-5
    • (2002) Trends Cell Biol. , vol.12 , pp. 164-172
    • Lu, K.P.1    Liou, Y.C.2    Zhou, X.Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.