메뉴 건너뛰기




Volumn 21, Issue 21, 2007, Pages 2818-2831

Phosphorylation of histone H3 at Ser10 facilitates RNA polymerase II release from promoter-proximal pausing in Drosophila

Author keywords

Chromatin; Histone; Kinase; Transcription

Indexed keywords

HEAT SHOCK PROTEIN 70; HISTONE H3; PROTEIN KINASE; PROTEIN KINASE JIL 1; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 35948954744     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.1604007     Document Type: Article
Times cited : (93)

References (51)
  • 2
    • 0142123203 scopus 로고    scopus 로고
    • Transcription factor and polymerase recruitment, modification, and movement on dhsp70 in vivo in the minutes following heat shock
    • Boehm, A.K., Saunders, A., Werner, J., and Lis, J.T. 2003. Transcription factor and polymerase recruitment, modification, and movement on dhsp70 in vivo in the minutes following heat shock. Mol. Cell. Biol. 23: 7628-7637.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7628-7637
    • Boehm, A.K.1    Saunders, A.2    Werner, J.3    Lis, J.T.4
  • 3
    • 0033695926 scopus 로고    scopus 로고
    • Light induces chromatin modification in cells of the mammalian circadian clock
    • Crosio, C., Cermakian, N., Allis, C.D., and Sassone-Corsi, P. 2000. Light induces chromatin modification in cells of the mammalian circadian clock. Nat. Neurosci. 3: 1241-1247.
    • (2000) Nat. Neurosci , vol.3 , pp. 1241-1247
    • Crosio, C.1    Cermakian, N.2    Allis, C.D.3    Sassone-Corsi, P.4
  • 4
    • 0348143169 scopus 로고    scopus 로고
    • Chromatin remodeling and neuronal response: Multiple signaling pathways induce specific histone H3 modifications and early gene expression in hippocampal neurons
    • Crosio, C., Heitz, E., Allis, C.D., Borrelli, E., and Sassone-Corsi, P. 2003. Chromatin remodeling and neuronal response: Multiple signaling pathways induce specific histone H3 modifications and early gene expression in hippocampal neurons. J. Cell Sci. 116: 4905-4914.
    • (2003) J. Cell Sci , vol.116 , pp. 4905-4914
    • Crosio, C.1    Heitz, E.2    Allis, C.D.3    Borrelli, E.4    Sassone-Corsi, P.5
  • 5
    • 0041975981 scopus 로고    scopus 로고
    • MSK1 and MSK2 mediate mitogen- and stress-induced phosphorylation of histone H3: A controversy resolved
    • doi: 10.1126/stke.2003. 195.pe33
    • Davie, J.R. 2003. MSK1 and MSK2 mediate mitogen- and stress-induced phosphorylation of histone H3: A controversy resolved. Sci. STKE 2003: PE33. doi: 10.1126/stke.2003. 195.pe33.
    • (2003) Sci. STKE , vol.2003
    • Davie, J.R.1
  • 7
    • 0026348276 scopus 로고
    • CTD kinase associated with yeast RNA polymerase II initiation factor b
    • Feaver, W.J., Gileadi, O., Li, Y., and Kornberg, R.D. 1991. CTD kinase associated with yeast RNA polymerase II initiation factor b. Cell 67: 1223-1230.
    • (1991) Cell , vol.67 , pp. 1223-1230
    • Feaver, W.J.1    Gileadi, O.2    Li, Y.3    Kornberg, R.D.4
  • 9
    • 10844264219 scopus 로고    scopus 로고
    • Genomic deletions of the Drosophila melanogaster Hsp70 genes
    • Gong, W.J. and Golic, K.G. 2004. Genomic deletions of the Drosophila melanogaster Hsp70 genes. Genetics 168: 1467-1476.
    • (2004) Genetics , vol.168 , pp. 1467-1476
    • Gong, W.J.1    Golic, K.G.2
  • 10
    • 34447098370 scopus 로고    scopus 로고
    • A chromatin landmark and transcription initiation at most promoters in human cells
    • Guenther, M.G., Levine, S.S., Boyer, L.A., Jaenisch, R., and Young, R.A. 2007. A chromatin landmark and transcription initiation at most promoters in human cells. Cell 130: 77-88.
    • (2007) Cell , vol.130 , pp. 77-88
    • Guenther, M.G.1    Levine, S.S.2    Boyer, L.A.3    Jaenisch, R.4    Young, R.A.5
  • 12
    • 28844475262 scopus 로고    scopus 로고
    • Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
    • Hirota, T., Lipp, J.J., Toh, B.H., and Peters, J.M. 2005. Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature 438: 1176-1180.
    • (2005) Nature , vol.438 , pp. 1176-1180
    • Hirota, T.1    Lipp, J.J.2    Toh, B.H.3    Peters, J.M.4
  • 13
    • 23744514308 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription
    • Jang, M.K., Mochizuki, K., Zhou, M., Jeong, H.S., Brady, J.N., and Ozato, K. 2005. The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription. Mol. Cell 19: 523-534.
    • (2005) Mol. Cell , vol.19 , pp. 523-534
    • Jang, M.K.1    Mochizuki, K.2    Zhou, M.3    Jeong, H.S.4    Brady, J.N.5    Ozato, K.6
  • 14
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. and Allis, C.D. 2001. Translating the histone code. Science 293: 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 15
    • 0033166349 scopus 로고    scopus 로고
    • JIL-1: A novel chromosomal tandem kinase implicated in transcriptional regulation in Drosophila
    • Jin, Y., Wang, Y., Walker, D.L., Dong, H., Conley, C., Johansen, J., and Johansen, K.M. 1999. JIL-1: A novel chromosomal tandem kinase implicated in transcriptional regulation in Drosophila. Mol. Cell 4: 129-135.
    • (1999) Mol. Cell , vol.4 , pp. 129-135
    • Jin, Y.1    Wang, Y.2    Walker, D.L.3    Dong, H.4    Conley, C.5    Johansen, J.6    Johansen, K.M.7
  • 16
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides, T. 2002. Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12: 198-209.
    • (2002) Curr. Opin. Genet. Dev , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 18
    • 0037229898 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 during transcriptional activation depends on promoter structure
    • Labrador, M. and Corces, V.G. 2003. Phosphorylation of histone H3 during transcriptional activation depends on promoter structure. Genes & Dev. 17: 43-48.
    • (2003) Genes & Dev , vol.17 , pp. 43-48
    • Labrador, M.1    Corces, V.G.2
  • 19
    • 0034175631 scopus 로고    scopus 로고
    • P-TEFb kinase recruitment and function at heat shock loci
    • Lis, J.T., Mason, P., Peng, J., Price, D.H., and Werner, J. 2000. P-TEFb kinase recruitment and function at heat shock loci. Genes & Dev. 14: 792-803.
    • (2000) Genes & Dev , vol.14 , pp. 792-803
    • Lis, J.T.1    Mason, P.2    Peng, J.3    Price, D.H.4    Werner, J.5
  • 20
    • 0035839135 scopus 로고    scopus 로고
    • Snf1-A histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription
    • Lo, W.S., Duggan, L., Emre, N.C., Belotserkovskya, R., Lane, W.S., Shiekhattar, R., and Berger, S.L. 2001. Snf1-A histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science 293: 1142-1146.
    • (2001) Science , vol.293 , pp. 1142-1146
    • Lo, W.S.1    Duggan, L.2    Emre, N.C.3    Belotserkovskya, R.4    Lane, W.S.5    Shiekhattar, R.6    Berger, S.L.7
  • 21
    • 16344395502 scopus 로고    scopus 로고
    • Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms
    • Lo, W.S., Gamache, E.R., Henry, K.W., Yang, D., Pillus, L., and Berger, S.L. 2005. Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms. EMBO J. 24: 997-1008.
    • (2005) EMBO J , vol.24 , pp. 997-1008
    • Lo, W.S.1    Gamache, E.R.2    Henry, K.W.3    Yang, D.4    Pillus, L.5    Berger, S.L.6
  • 22
    • 0026731557 scopus 로고
    • Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II
    • Lu, H., Zawel, L., Fisher, L., Egly, J.M., and Reinberg, D. 1992. Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II. Nature 358: 641-645.
    • (1992) Nature , vol.358 , pp. 641-645
    • Lu, H.1    Zawel, L.2    Fisher, L.3    Egly, J.M.4    Reinberg, D.5
  • 24
    • 0025872683 scopus 로고
    • Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors
    • Mahadevan, L.C., Willis, A.C., and Barratt, M.J. 1991. Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors. Cell 65: 775-783.
    • (1991) Cell , vol.65 , pp. 775-783
    • Mahadevan, L.C.1    Willis, A.C.2    Barratt, M.J.3
  • 25
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxylterminal domain kinase
    • Marshall, N.F., Peng, J., Xie, Z., and Price, D.H. 1996. Control of RNA polymerase II elongation potential by a novel carboxylterminal domain kinase. J. Biol. Chem. 271: 27176-27183.
    • (1996) J. Biol. Chem , vol.271 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, Z.3    Price, D.H.4
  • 26
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • Ng, H.H., Robert, F., Young, R.A., and Struhl, K. 2003. Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol. Cell 11: 709-719.
    • (2003) Mol. Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 27
    • 0033639243 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 correlates with transcriptionally active loci
    • Nowak, S.J. and Corces, V.G. 2000. Phosphorylation of histone H3 correlates with transcriptionally active loci. Genes & Dev. 14: 3003-3013.
    • (2000) Genes & Dev , vol.14 , pp. 3003-3013
    • Nowak, S.J.1    Corces, V.G.2
  • 28
    • 1642326716 scopus 로고    scopus 로고
    • Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation
    • Nowak, S.J. and Corces, V.G. 2004. Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation. Trends Genet. 20: 214-220.
    • (2004) Trends Genet , vol.20 , pp. 214-220
    • Nowak, S.J.1    Corces, V.G.2
  • 29
    • 0042470618 scopus 로고    scopus 로고
    • Protein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster
    • Nowak, S.J., Pai, C.Y., and Corces, V.G. 2003. Protein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster. Mol. Cell. Biol. 23: 6129-6138.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 6129-6138
    • Nowak, S.J.1    Pai, C.Y.2    Corces, V.G.3
  • 30
    • 0037154982 scopus 로고    scopus 로고
    • A unified theory of gene expression
    • Orphanides, G. and Reinberg, D. 2002. A unified theory of gene expression. Cell 108: 439-451.
    • (2002) Cell , vol.108 , pp. 439-451
    • Orphanides, G.1    Reinberg, D.2
  • 31
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • doi: 10.1016/j.cub.2004.07.007
    • Peterson, C.L. and Laniel, M.A. 2004. Histones and histone modifications. Curr. Biol. 14: R546-R551. doi: 10.1016/j.cub.2004.07.007.
    • (2004) Curr. Biol , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 32
    • 0019413560 scopus 로고
    • Monoclonal antibodies against a nuclear membrane protein of Drosophila. Localization by indirect immunofluorescence and detection of antigen using a new protein blotting procedure
    • Risau, W., Saumweber, H., and Symmons, P. 1981. Monoclonal antibodies against a nuclear membrane protein of Drosophila. Localization by indirect immunofluorescence and detection of antigen using a new protein blotting procedure. Exp. Cell Res. 133: 47-54.
    • (1981) Exp. Cell Res , vol.133 , pp. 47-54
    • Risau, W.1    Saumweber, H.2    Symmons, P.3
  • 34
  • 35
    • 0026666047 scopus 로고
    • A carboxyl-terminal-domain kinase associated with RNA polymerase II transcription factor δ from rat liver
    • Serizawa, H., Conaway, R.C., and Conaway, J.W. 1992. A carboxyl-terminal-domain kinase associated with RNA polymerase II transcription factor δ from rat liver. Proc. Natl. Acad. Sci. 89: 7476-7480.
    • (1992) Proc. Natl. Acad. Sci , vol.89 , pp. 7476-7480
    • Serizawa, H.1    Conaway, R.C.2    Conaway, J.W.3
  • 36
    • 33645667110 scopus 로고    scopus 로고
    • SWI/SNF: The crossroads where extracellular signaling pathways meet chromatin
    • Simone, C. 2006. SWI/SNF: The crossroads where extracellular signaling pathways meet chromatin. J. Cell. Physiol. 207: 309-314.
    • (2006) J. Cell. Physiol , vol.207 , pp. 309-314
    • Simone, C.1
  • 38
    • 17744371151 scopus 로고    scopus 로고
    • The Drosophila trithorax group protein Kismet facilitates an early step in transcriptional elongation by RNA Polymerase II
    • Srinivasan, S., Armstrong, J.A., Deuring, R., Dahlsveen, I.K., McNeill, H., and Tamkun, J.W. 2005. The Drosophila trithorax group protein Kismet facilitates an early step in transcriptional elongation by RNA Polymerase II. Development 132: 1623-1635.
    • (2005) Development , vol.132 , pp. 1623-1635
    • Srinivasan, S.1    Armstrong, J.A.2    Deuring, R.3    Dahlsveen, I.K.4    McNeill, H.5    Tamkun, J.W.6
  • 39
    • 4344592639 scopus 로고    scopus 로고
    • Distinct stimulus-specific histone modifications at hsp70 chromatin targeted by the transcription factor heat shock factor-1
    • Thomson, S., Hollis, A., Hazzalin, C.A., and Mahadevan, L.C. 2004. Distinct stimulus-specific histone modifications at hsp70 chromatin targeted by the transcription factor heat shock factor-1. Mol. Cell 15: 585-594.
    • (2004) Mol. Cell , vol.15 , pp. 585-594
    • Thomson, S.1    Hollis, A.2    Hazzalin, C.A.3    Mahadevan, L.C.4
  • 40
    • 0030201467 scopus 로고    scopus 로고
    • Flies on steroids-Drosophila metamorphosis and the mechanisms of steroid hormone action
    • Thummel, C.S. 1996. Flies on steroids-Drosophila metamorphosis and the mechanisms of steroid hormone action. Trends Genet. 12: 306-310.
    • (1996) Trends Genet , vol.12 , pp. 306-310
    • Thummel, C.S.1
  • 41
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner, B.M. 2000. Histone acetylation and an epigenetic code. Bioessays 22: 836-845.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 42
    • 0035473486 scopus 로고    scopus 로고
    • 14-3-3 proteins: Bringing new definitions to scaffolding
    • Tzivion, G., Shen, Y.H., and Zhu, J. 2001. 14-3-3 proteins: Bringing new definitions to scaffolding. Oncogene 20: 6331-6338.
    • (2001) Oncogene , vol.20 , pp. 6331-6338
    • Tzivion, G.1    Shen, Y.H.2    Zhu, J.3
  • 43
    • 33750448996 scopus 로고    scopus 로고
    • Induction of progesterone target genes requires activation of erk and msk kinases and phosphorylation of histone h3
    • Vicent, G.P., Ballare, C., Nacht, A.S., Clausell, J., Subtil-Rodriguez, A., Quiles, I., Jordan, A., and Beato, M. 2006. Induction of progesterone target genes requires activation of erk and msk kinases and phosphorylation of histone h3. Mol. Cell 24: 367-381.
    • (2006) Mol. Cell , vol.24 , pp. 367-381
    • Vicent, G.P.1    Ballare, C.2    Nacht, A.S.3    Clausell, J.4    Subtil-Rodriguez, A.5    Quiles, I.6    Jordan, A.7    Beato, M.8
  • 44
    • 0035906859 scopus 로고    scopus 로고
    • The JIL-1 tandem kinase mediates histone H3 phosphorylation and is required for maintenance of chromatin structure in Drosophila
    • Wang, Y., Zhang, W., Jin, Y., Johansen, J., and Johansen, K.M. 2001. The JIL-1 tandem kinase mediates histone H3 phosphorylation and is required for maintenance of chromatin structure in Drosophila. Cell 105: 433-443.
    • (2001) Cell , vol.105 , pp. 433-443
    • Wang, Y.1    Zhang, W.2    Jin, Y.3    Johansen, J.4    Johansen, K.M.5
  • 45
    • 0027135208 scopus 로고
    • Locus-specific variation in phosphorylation state of RNA polymerase II in vivo: Correlations with gene activity and transcript processing
    • Weeks, J.R., Hardin, S.E., Shen, J., Lee, J.M., and Greenleaf, A.L. 1993. Locus-specific variation in phosphorylation state of RNA polymerase II in vivo: Correlations with gene activity and transcript processing. Genes & Dev. 7: 2329-2344.
    • (1993) Genes & Dev , vol.7 , pp. 2329-2344
    • Weeks, J.R.1    Hardin, S.E.2    Shen, J.3    Lee, J.M.4    Greenleaf, A.L.5
  • 46
    • 0025955517 scopus 로고
    • Stress-induced oligomerization and chromosomal relocalization of heat-shock factor
    • Westwood, J.T., Clos, J., and Wu, C. 1991. Stress-induced oligomerization and chromosomal relocalization of heat-shock factor. Nature 353: 822-827.
    • (1991) Nature , vol.353 , pp. 822-827
    • Westwood, J.T.1    Clos, J.2    Wu, C.3
  • 48
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression
    • Yamamoto, Y., Verma, U.N., Prajapati, S., Kwak, Y.T., and Gaynor, R.B. 2003. Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression. Nature 423: 655-659.
    • (2003) Nature , vol.423 , pp. 655-659
    • Yamamoto, Y.1    Verma, U.N.2    Prajapati, S.3    Kwak, Y.T.4    Gaynor, R.B.5
  • 49
    • 23744467035 scopus 로고    scopus 로고
    • Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4
    • Yang, Z., Yik, J.H., Chen, R., He, N., Jang, M.K., Ozato, K., and Zhou, Q. 2005. Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4. Mol. Cell 19: 535-545.
    • (2005) Mol. Cell , vol.19 , pp. 535-545
    • Yang, Z.1    Yik, J.H.2    Chen, R.3    He, N.4    Jang, M.K.5    Ozato, K.6    Zhou, Q.7
  • 50
    • 0347622767 scopus 로고    scopus 로고
    • Genetic and phenotypic analysis of alleles of the Drosophila chromosomal JIL-1 kinase reveals a functional requirement at multiple developmental stages
    • Zhang, W., Jin, Y., Ji, Y., Girton, J., Johansen, J., and Johansen, K.M. 2003. Genetic and phenotypic analysis of alleles of the Drosophila chromosomal JIL-1 kinase reveals a functional requirement at multiple developmental stages. Genetics 165: 1341-1354.
    • (2003) Genetics , vol.165 , pp. 1341-1354
    • Zhang, W.1    Jin, Y.2    Ji, Y.3    Girton, J.4    Johansen, J.5    Johansen, K.M.6
  • 51
    • 32244431871 scopus 로고    scopus 로고
    • The JIL-1 histone H3S10 kinase regulates dimethyl H3K9 modifications and heterochromatic spreading in Drosophila
    • Zhang, W., Deng, H., Bao, X., Lerach, S., Girton, J., Johansen, J., and Johansen, K.M. 2006. The JIL-1 histone H3S10 kinase regulates dimethyl H3K9 modifications and heterochromatic spreading in Drosophila. Development 133: 229-235.
    • (2006) Development , vol.133 , pp. 229-235
    • Zhang, W.1    Deng, H.2    Bao, X.3    Lerach, S.4    Girton, J.5    Johansen, J.6    Johansen, K.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.