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Volumn 55, Issue 7, 2016, Pages 1149-1158

Distributive O-GlcNAcylation on the Highly Repetitive C-Terminal Domain of RNA Polymerase II

Author keywords

[No Author keywords available]

Indexed keywords

RNA;

EID: 84959341434     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b01280     Document Type: Article
Times cited : (24)

References (35)
  • 1
    • 84889051321 scopus 로고    scopus 로고
    • RNA polymerase II C-terminal domain: tethering transcription to transcript and template
    • Corden, J. L. (2013) RNA polymerase II C-terminal domain: tethering transcription to transcript and template Chem. Rev. 113, 8423-8455 10.1021/cr400158h
    • (2013) Chem. Rev. , vol.113 , pp. 8423-8455
    • Corden, J.L.1
  • 2
    • 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. 113, 8456-8490 10.1021/cr400071f
    • (2013) Chem. Rev. , vol.113 , pp. 8456-8490
    • Eick, D.1    Geyer, M.2
  • 3
    • 84867160564 scopus 로고    scopus 로고
    • The RNA polymerase II CTD coordinates transcription and RNA processing
    • Hsin, J. P. and Manley, J. L. (2012) The RNA polymerase II CTD coordinates transcription and RNA processing Genes Dev. 26, 2119-2137 10.1101/gad.200303.112
    • (2012) Genes Dev. , vol.26 , pp. 2119-2137
    • Hsin, J.P.1    Manley, J.L.2
  • 4
    • 84892653664 scopus 로고    scopus 로고
    • RNA polymerase II CTD modifications: How many tales from a single tail
    • Napolitano, G., Lania, L., and Majello, B. (2014) RNA polymerase II CTD modifications: How many tales from a single tail J. Cell. Physiol. 229, 538-544 10.1002/jcp.24483
    • (2014) J. Cell. Physiol. , vol.229 , pp. 538-544
    • Napolitano, G.1    Lania, L.2    Majello, B.3
  • 5
    • 84872405841 scopus 로고    scopus 로고
    • Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription
    • Heidemann, M., Hintermair, C., Voß, K., and Eick, D. (2013) Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription Biochim. Biophys. Acta, Gene Regul. Mech. 1829, 55-62 10.1016/j.bbagrm.2012.08.013
    • (2013) Biochim. Biophys. Acta, Gene Regul. Mech. , vol.1829 , pp. 55-62
    • Heidemann, M.1    Hintermair, C.2    Voß, K.3    Eick, D.4
  • 6
    • 84894610074 scopus 로고    scopus 로고
    • Cross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA polymerase II
    • Yogesha, S. D., Mayfield, J. E., and Zhang, Y. (2014) Cross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA polymerase II Molecules 19, 1481-1511 10.3390/molecules19021481
    • (2014) Molecules , vol.19 , pp. 1481-1511
    • Yogesha, S.D.1    Mayfield, J.E.2    Zhang, Y.3
  • 7
    • 0034307008 scopus 로고    scopus 로고
    • Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription
    • Komarnitsky, P., Cho, E. J., and Buratowski, S. (2000) Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription Genes Dev. 14, 2452-2460 10.1101/gad.824700
    • (2000) Genes Dev. , vol.14 , pp. 2452-2460
    • Komarnitsky, P.1    Cho, E.J.2    Buratowski, S.3
  • 8
    • 84889028380 scopus 로고    scopus 로고
    • The writers, readers, and functions of the RNA polymerase II C-terminal domain code
    • Jeronimo, C., Bataille, A. R., and Robert, F. (2013) The writers, readers, and functions of the RNA polymerase II C-terminal domain code Chem. Rev. 113, 8491-8522 10.1021/cr4001397
    • (2013) Chem. Rev. , vol.113 , pp. 8491-8522
    • Jeronimo, C.1    Bataille, A.R.2    Robert, F.3
  • 9
    • 0027289130 scopus 로고
    • RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc
    • Kelly, W. G., Dahmus, M. E., and Hart, G. W. (1993) RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc J. Biol. Chem. 268, 10416-10424
    • (1993) J. Biol. Chem. , vol.268 , pp. 10416-10424
    • Kelly, W.G.1    Dahmus, M.E.2    Hart, G.W.3
  • 10
    • 84863610013 scopus 로고    scopus 로고
    • Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo
    • Ranuncolo, S. M., Ghosh, S., Hanover, J. A., Hart, G. W., and Lewis, B. A. (2012) Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo J. Biol. Chem. 287, 23549-23561 10.1074/jbc.M111.330910
    • (2012) J. Biol. Chem. , vol.287 , pp. 23549-23561
    • Ranuncolo, S.M.1    Ghosh, S.2    Hanover, J.A.3    Hart, G.W.4    Lewis, B.A.5
  • 11
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres, C. R. and Hart, G. W. (1984) Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc J. Biol. Chem. 259, 3308-3317
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 12
    • 84903767444 scopus 로고    scopus 로고
    • O-GlcNAc profiling: from proteins to proteomes
    • Ma, J. and Hart, G. W. (2014) O-GlcNAc profiling: from proteins to proteomes Clin. Proteomics 11, 8 10.1186/1559-0275-11-8
    • (2014) Clin. Proteomics , vol.11 , pp. 8
    • Ma, J.1    Hart, G.W.2
  • 13
    • 84928254126 scopus 로고    scopus 로고
    • A little sugar goes a long way: the cell biology of O-GlcNAc
    • Bond, M. R. and Hanover, J. A. (2015) A little sugar goes a long way: The cell biology of O-GlcNAc J. Cell Biol. 208, 869-880 10.1083/jcb.201501101
    • (2015) J. Cell Biol. , vol.208 , pp. 869-880
    • Bond, M.R.1    Hanover, J.A.2
  • 14
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • Kreppel, L. K., Blomberg, M. A., and Hart, G. W. (1997) Dynamic glycosylation of nuclear and cytosolic proteins cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats J. Biol. Chem. 272, 9308-9315 10.1074/jbc.272.14.9308
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 15
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain
    • Gao, Y., Wells, L., Comer, F. I., Parker, G. J., and Hart, G. W. (2001) Dynamic O-glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain J. Biol. Chem. 276, 9838-9845 10.1074/jbc.M010420200
    • (2001) J. Biol. Chem. , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 16
    • 84918501751 scopus 로고    scopus 로고
    • O-GlcNAc and the epigenetic regulation of gene expression
    • Lewis, B. A. and Hanover, J. A. (2014) O-GlcNAc and the epigenetic regulation of gene expression J. Biol. Chem. 289, 34440-34448 10.1074/jbc.R114.595439
    • (2014) J. Biol. Chem. , vol.289 , pp. 34440-34448
    • Lewis, B.A.1    Hanover, J.A.2
  • 17
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
    • Hart, G. W., Slawson, C., Ramirez-Correa, G., and Lagerlof, O. (2011) Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease Annu. Rev. Biochem. 80, 825 10.1146/annurev-biochem-060608-102511
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 18
    • 84885044676 scopus 로고    scopus 로고
    • O-GlcNAcylation at promoters, nutrient sensors, and transcriptional regulation
    • Lewis, B. A. (2013) O-GlcNAcylation at promoters, nutrient sensors, and transcriptional regulation Biochim. Biophys. Acta, Gene Regul. Mech. 1829, 1202-1206 10.1016/j.bbagrm.2013.09.003
    • (2013) Biochim. Biophys. Acta, Gene Regul. Mech. , vol.1829 , pp. 1202-1206
    • Lewis, B.A.1
  • 19
    • 0035800086 scopus 로고    scopus 로고
    • Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II
    • Comer, F. I. and Hart, G. W. (2001) Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II Biochemistry 40, 7845-7852 10.1021/bi0027480
    • (2001) Biochemistry , vol.40 , pp. 7845-7852
    • Comer, F.I.1    Hart, G.W.2
  • 20
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus, M. B., Nam, Y., Jiang, J., Sliz, P., and Walker, S. (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate Nature 469, 564-567 10.1038/nature09638
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5
  • 21
    • 1642528971 scopus 로고    scopus 로고
    • Analysis of the requirement for RNA polymerase II CTD heptapeptide repeats in pre-mRNA splicing and 3′-end cleavage
    • Rosonina, E. and Blencowe, B. J. (2004) Analysis of the requirement for RNA polymerase II CTD heptapeptide repeats in pre-mRNA splicing and 3′-end cleavage RNA 10, 581-589 10.1261/rna.5207204
    • (2004) RNA , vol.10 , pp. 581-589
    • Rosonina, E.1    Blencowe, B.J.2
  • 22
    • 79952747341 scopus 로고    scopus 로고
    • Metabolic cross-talk allows labeling of O-linked β-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway
    • Boyce, M., Carrico, I. S., Ganguli, A. S., Yu, S. H., Hangauer, M. J., Hubbard, S. C., Kohler, J. J., and Bertozzi, C. R. (2011) Metabolic cross-talk allows labeling of O-linked β-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway Proc. Natl. Acad. Sci. U. S. A. 108, 3141-3146 10.1073/pnas.1010045108
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 3141-3146
    • Boyce, M.1    Carrico, I.S.2    Ganguli, A.S.3    Yu, S.H.4    Hangauer, M.J.5    Hubbard, S.C.6    Kohler, J.J.7    Bertozzi, C.R.8
  • 23
    • 84897499290 scopus 로고    scopus 로고
    • Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated
    • Ortiz-Meoz, R. F., Merbl, Y., Kirschner, M. W., and Walker, S. (2014) Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated J. Am. Chem. Soc. 136, 4845-4848 10.1021/ja500451w
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 4845-4848
    • Ortiz-Meoz, R.F.1    Merbl, Y.2    Kirschner, M.W.3    Walker, S.4
  • 24
    • 84857193629 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification regulates CREB-mediated gene expression and memory formation
    • Rexach, J. E., Clark, P. M., Mason, D. E., Neve, R. L., Peters, E. C., and Hsieh-Wilson, L. C. (2012) Dynamic O-GlcNAc modification regulates CREB-mediated gene expression and memory formation Nat. Chem. Biol. 8, 253-261 10.1038/nchembio.770
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 253-261
    • Rexach, J.E.1    Clark, P.M.2    Mason, D.E.3    Neve, R.L.4    Peters, E.C.5    Hsieh-Wilson, L.C.6
  • 26
    • 4744341309 scopus 로고    scopus 로고
    • The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α
    • Jinek, M., Rehwinkel, J., Lazarus, B. D., Izaurralde, E., Hanover, J. A., and Conti, E. (2004) The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α Nat. Struct. Mol. Biol. 11, 1001-1007 10.1038/nsmb833
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1001-1007
    • Jinek, M.1    Rehwinkel, J.2    Lazarus, B.D.3    Izaurralde, E.4    Hanover, J.A.5    Conti, E.6
  • 27
    • 0030944105 scopus 로고    scopus 로고
    • O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • Lubas, W. A., Frank, D. W., Krause, M., and Hanover, J. A. (1997) O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats J. Biol. Chem. 272, 9316-9324 10.1074/jbc.272.14.9316
    • (1997) J. Biol. Chem. , vol.272 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.A.4
  • 28
    • 84860184939 scopus 로고    scopus 로고
    • Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation
    • Hanover, J. A., Krause, M. W., and Love, D. C. (2012) Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation Nat. Rev. Mol. Cell Biol. 13, 312-321 10.1038/nrm3334
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 312-321
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 29
    • 80051586712 scopus 로고    scopus 로고
    • Monitoring processivity and length control of a carbohydrate polymerase
    • Levengood, M. R., Splain, R. A., and Kiessling, L. L. (2011) Monitoring processivity and length control of a carbohydrate polymerase J. Am. Chem. Soc. 133, 12758-12766 10.1021/ja204448t
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 12758-12766
    • Levengood, M.R.1    Splain, R.A.2    Kiessling, L.L.3
  • 30
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 Ångstrom resolution
    • Cramer, P., Bushnell, D. A., and Kornberg, R. D. (2001) Structural basis of transcription: RNA polymerase II at 2.8 Ångstrom resolution Science 292, 1863-1876 10.1126/science.1059493
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 31
    • 14844290215 scopus 로고    scopus 로고
    • Structures of complete RNA polymerase II and its subcomplex, Rpb4/7
    • Armache, K. J., Mitterweger, S., Meinhart, A., and Cramer, P. (2005) Structures of complete RNA polymerase II and its subcomplex, Rpb4/7 J. Biol. Chem. 280, 7131-7134 10.1074/jbc.M413038200
    • (2005) J. Biol. Chem. , vol.280 , pp. 7131-7134
    • Armache, K.J.1    Mitterweger, S.2    Meinhart, A.3    Cramer, P.4
  • 32
  • 33
    • 84884589009 scopus 로고    scopus 로고
    • The C-terminal domain of Rpb1 functions on other RNA polymerase II subunits
    • Suh, H., Hazelbaker, D. Z., Soares, L. M., and Buratowski, S. (2013) The C-terminal domain of Rpb1 functions on other RNA polymerase II subunits Mol. Cell 51, 850-858 10.1016/j.molcel.2013.08.015
    • (2013) Mol. Cell , vol.51 , pp. 850-858
    • Suh, H.1    Hazelbaker, D.Z.2    Soares, L.M.3    Buratowski, S.4
  • 35
    • 84941595627 scopus 로고    scopus 로고
    • Enhanced transfer of a photocross-linking N-acetylglucosamine (GlcNAc) analog by an O-GlcNAc transferase mutant with converted substrate specificity
    • Rodriguez, A. C., Yu, S. H., Li, B., Zegzouti, H., and Kohler, J. J. (2015) Enhanced transfer of a photocross-linking N-acetylglucosamine (GlcNAc) analog by an O-GlcNAc transferase mutant with converted substrate specificity J. Biol. Chem. 290, 22638-22648 10.1074/jbc.M115.667006
    • (2015) J. Biol. Chem. , vol.290 , pp. 22638-22648
    • Rodriguez, A.C.1    Yu, S.H.2    Li, B.3    Zegzouti, H.4    Kohler, J.J.5


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