메뉴 건너뛰기




Volumn 129, Issue 2-3, 2000, Pages 258-268

RNA polymerase II in Cajal bodies of amphibian oocytes

Author keywords

B snurposome; Cajal body; Coiled body; Germinal vesicle; Lampbrush chromosome; Oocyte; RNA polymerase II; Transcription

Indexed keywords

RNA POLYMERASE II;

EID: 0033925931     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2000.4231     Document Type: Article
Times cited : (46)

References (55)
  • 1
    • 0027370246 scopus 로고
    • Structure of the gene encoding the 14.5 kDa subunit of human RNA polymerase II
    • Acker J., Wintzerith M., Vigneron M., Kedinger C. Structure of the gene encoding the 14.5 kDa subunit of human RNA polymerase II. Nucleic Acids Res. 21:1993;5345-5350.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5345-5350
    • Acker, J.1    Wintzerith, M.2    Vigneron, M.3    Kedinger, C.4
  • 2
    • 0027975533 scopus 로고
    • A 14.4 kDa acidic subunit of human RNA polymerase II with a putative leucine-zipper
    • Acker J., Wintzerith M., Vigneron M., Kedinger C. A 14.4 kDa acidic subunit of human RNA polymerase II with a putative leucine-zipper. DNA Seq. 4:1994;329-331.
    • (1994) DNA Seq. , vol.4 , pp. 329-331
    • Acker, J.1    Wintzerith, M.2    Vigneron, M.3    Kedinger, C.4
  • 3
    • 0022132080 scopus 로고
    • Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases
    • Allison L. A., Moyle M., Shales M., Ingles C. J. Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases. Cell. 42:1985;599-610.
    • (1985) Cell , vol.42 , pp. 599-610
    • Allison, L.A.1    Moyle, M.2    Shales, M.3    Ingles, C.J.4
  • 4
    • 0031029143 scopus 로고    scopus 로고
    • Phosphorylation of the RNA polymerase II largest subunit during Xenopus laevis oocyte maturation
    • Bellier S., Dubois M.-F., Nishida E., Almouzni G., Bensaude O. Phosphorylation of the RNA polymerase II largest subunit during Xenopus laevis oocyte maturation. Mol. Cell. Biol. 17:1997;1434-1440.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1434-1440
    • Bellier, S.1    Dubois, M.-F.2    Nishida, E.3    Almouzni, G.4    Bensaude, O.5
  • 5
    • 0027397091 scopus 로고
    • A putative zinc-binding protein on lampbrush chromosome loops
    • Bellini M., Lacroix J.-C., Gall J. G. A putative zinc-binding protein on lampbrush chromosome loops. EMBO J. 12:1993;107-114.
    • (1993) EMBO J. , vol.12 , pp. 107-114
    • Bellini, M.1    Lacroix, J.-C.2    Gall, J.G.3
  • 6
    • 0028883688 scopus 로고
    • A zinc-binding domain is required for targeting the maternal nuclear protein PwA33 to lampbrush chromosome loops
    • Bellini M., Lacroix J.-C., Gall J. G. A zinc-binding domain is required for targeting the maternal nuclear protein PwA33 to lampbrush chromosome loops. J. Cell Biol. 131:1995;563-570.
    • (1995) J. Cell Biol. , vol.131 , pp. 563-570
    • Bellini, M.1    Lacroix, J.-C.2    Gall, J.G.3
  • 7
    • 0012882369 scopus 로고
    • Transcriptional units in eukaryotic chromosomes
    • Beyer A. L., McKnight S. L., Miller O. L. Transcriptional units in eukaryotic chromosomes. Mol. Genet. 3:1979;117-175.
    • (1979) Mol. Genet. , vol.3 , pp. 117-175
    • Beyer, A.L.1    McKnight, S.L.2    Miller, O.L.3
  • 9
    • 0028900584 scopus 로고
    • Transcription-dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains
    • Bregman D. B., Du L., van der Zee S., Warren S. L. Transcription-dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains. J. Cell Biol. 129:1995;287-298.
    • (1995) J. Cell Biol. , vol.129 , pp. 287-298
    • Bregman, D.B.1    Du, L.2    Van Der Zee, S.3    Warren, S.L.4
  • 10
    • 0015195938 scopus 로고
    • Incorporation of tritiated uridine in nuclei of Triturus oocytes treated with α-amanitin
    • Bucci S., Nardi I., Mancino G., Fiume L. Incorporation of tritiated uridine in nuclei of Triturus oocytes treated with α-amanitin. Exp. Cell Res. 69:1971;462-465.
    • (1971) Exp. Cell Res. , vol.69 , pp. 462-465
    • Bucci, S.1    Nardi, I.2    Mancino, G.3    Fiume, L.4
  • 12
    • 0026040680 scopus 로고
    • Association of RNA with the B and C snurposomes of Xenopus oocyte nuclei
    • Callan H. G., Gall J. G. Association of RNA with the B and C snurposomes of Xenopus oocyte nuclei. Chromosoma. 101:1991;69-82.
    • (1991) Chromosoma , vol.101 , pp. 69-82
    • Callan, H.G.1    Gall, J.G.2
  • 14
    • 0009370184 scopus 로고
    • A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II
    • Corden J. L., Cadena D. L., Ahearn J. M., Dahmus M. E. A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II. Proc. Natl. Acad. Sci. USA. 82:1985;7934-7938.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7934-7938
    • Corden, J.L.1    Cadena, D.L.2    Ahearn, J.M.3    Dahmus, M.E.4
  • 15
    • 0029760928 scopus 로고    scopus 로고
    • Reversible phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus M. E. Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J. Biol. Chem. 271:1996;19009-19012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19009-19012
    • Dahmus, M.E.1
  • 16
    • 0031032049 scopus 로고    scopus 로고
    • A functional interaction between the carboxy-terminal domain of RNA polymerase II and pre-mRNA splicing
    • Du L., Warren S. L. A functional interaction between the carboxy-terminal domain of RNA polymerase II and pre-mRNA splicing. J. Cell Biol. 136:1997;5-18.
    • (1997) J. Cell Biol. , vol.136 , pp. 5-18
    • Du, L.1    Warren, S.L.2
  • 17
    • 0028242341 scopus 로고
    • Inhibitors of transcription such as 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole and isoquinoline sulfonamide derivatives (H-8 and H-7) promote dephosphorylation of the carboxyl-terminal domain of RNA polymerase II largest subunit
    • Dubois M.-F., Nguyen V. T., Bellier S., Bensaude O. Inhibitors of transcription such as 5,6-dichloro-1-β-d-ribofuranosylbenzimidazole and isoquinoline sulfonamide derivatives (H-8 and H-7) promote dephosphorylation of the carboxyl-terminal domain of RNA polymerase II largest subunit. J. Biol. Chem. 269:1994;13331-13336.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13331-13336
    • Dubois, M.-F.1    Nguyen, V.T.2    Bellier, S.3    Bensaude, O.4
  • 18
    • 0343343965 scopus 로고
    • Differential inhibitory effect of a substituted benzimidazole on RNA labeling in polytene chromosomes
    • Egyházi E., Daneholt B., Edström J.-E., Lambert B., Ringborg U. Differential inhibitory effect of a substituted benzimidazole on RNA labeling in polytene chromosomes. J. Cell Biol. 47:1970;516-520.
    • (1970) J. Cell Biol. , vol.47 , pp. 516-520
    • Egyházi, E.1    Daneholt, B.2    Edström, J.-E.3    Lambert, B.4    Ringborg, U.5
  • 19
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan G. I., Lewis G. K., Ramsay G., Bishop J. M. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:1985;3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 20
    • 0032740248 scopus 로고    scopus 로고
    • Assembly of the nuclear transcription and processing machinery: Cajal bodies (coiled bodies) and transcriptosomes
    • Gall J. G., Bellini M., Wu Z., Murphy C. Assembly of the nuclear transcription and processing machinery: Cajal bodies (coiled bodies) and transcriptosomes. Mol. Biol. Cell. 10:1999;4385-4402.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4385-4402
    • Gall, J.G.1    Bellini, M.2    Wu, Z.3    Murphy, C.4
  • 22
    • 0031897697 scopus 로고    scopus 로고
    • Assembly of lampbrush chromosomes from sperm chromatin
    • Gall J. G., Murphy C. Assembly of lampbrush chromosomes from sperm chromatin. Mol. Biol. Cell. 9:1998;733-747.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 733-747
    • Gall, J.G.1    Murphy, C.2
  • 23
    • 0028928307 scopus 로고
    • Is the sphere organelle/coiled body a universal nuclear component
    • Gall J. G., Tsvetkov A., Wu Z., Murphy C. Is the sphere organelle/coiled body a universal nuclear component. Dev. Genet. 16:1995;25-35.
    • (1995) Dev. Genet. , vol.16 , pp. 25-35
    • Gall, J.G.1    Tsvetkov, A.2    Wu, Z.3    Murphy, C.4
  • 24
    • 0343683416 scopus 로고    scopus 로고
    • Nuclear distribution of transcription factors in relation to sites of transcription and RNA polymerase II
    • Grande M. A., van der Kraan I., de Jong L., van Driel R. Nuclear distribution of transcription factors in relation to sites of transcription and RNA polymerase II. J. Cell Sci. 110:1997;1781-1791.
    • (1997) J. Cell Sci. , vol.110 , pp. 1781-1791
    • Grande, M.A.1    Van Der Kraan, I.2    De Jong, L.3    Van Driel, R.4
  • 25
    • 0000502912 scopus 로고
    • The relationship between RNA synthesis and loop structure in lampbrush chromosomes
    • Izawa M., Allfrey V. G., Mirsky A. L. The relationship between RNA synthesis and loop structure in lampbrush chromosomes. Proc. Natl. Acad. Sci. USA. 49:1963;544-551.
    • (1963) Proc. Natl. Acad. Sci. USA , vol.49 , pp. 544-551
    • Izawa, M.1    Allfrey, V.G.2    Mirsky, A.L.3
  • 26
    • 0030793104 scopus 로고    scopus 로고
    • The cdk-cyclin H-MAT1 complex associated with TFIIH is localized in coiled bodies
    • Jordan P., Cunha C., Carmo-Fonseca M. The cdk-cyclin H-MAT1 complex associated with TFIIH is localized in coiled bodies. Mol. Biol. Cell. 8:1997;1207-1217.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1207-1217
    • Jordan, P.1    Cunha, C.2    Carmo-Fonseca, M.3
  • 27
    • 0031022189 scopus 로고    scopus 로고
    • Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-mRNA
    • Kim E., Du L., Bregman D. B., Warren S. L. Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-mRNA. J. Cell Biol. 136:1997;19-28.
    • (1997) J. Cell Biol. , vol.136 , pp. 19-28
    • Kim, E.1    Du, L.2    Bregman, D.B.3    Warren, S.L.4
  • 28
    • 0032562608 scopus 로고    scopus 로고
    • Structure and function in the nucleus
    • Lamond A. I., Earnshaw W. C. Structure and function in the nucleus. Science. 280:1998;547-553.
    • (1998) Science , vol.280 , pp. 547-553
    • Lamond, A.I.1    Earnshaw, W.C.2
  • 29
    • 0030005755 scopus 로고    scopus 로고
    • The I.M.A.G.E. Consortium: An integrated molecular analysis of genomes and their expression
    • Lennon G. G., Auffray C., Polymeropoulos M., Soares M. B. The I.M.A.G.E. Consortium: An integrated molecular analysis of genomes and their expression. Genomics. 33:1996;151-152.
    • (1996) Genomics , vol.33 , pp. 151-152
    • Lennon, G.G.1    Auffray, C.2    Polymeropoulos, M.3    Soares, M.B.4
  • 31
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall N., Peng J., Xie Z., Price D. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271:1996;27176-27183.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27176-27183
    • Marshall, N.1    Peng, J.2    Xie, Z.3    Price, D.4
  • 32
    • 0026725368 scopus 로고
    • Control of formation of two distinct classes of RNA polymerase II elongation complexes
    • Marshall N. F., Price D. H. Control of formation of two distinct classes of RNA polymerase II elongation complexes. Mol. Cell. Biol. 12:1992;2078-2090.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2078-2090
    • Marshall, N.F.1    Price, D.H.2
  • 33
    • 0029011873 scopus 로고
    • Purification of P-TEFb, a transcription factor required for the transition into productive elongation
    • Marshall N. F., Price D. H. Purification of P-TEFb, a transcription factor required for the transition into productive elongation. J. Biol. Chem. 270:1995;12335-12338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 34
    • 0031804377 scopus 로고    scopus 로고
    • Of coiled bodies, gems, and salmon
    • Matera A. G. Of coiled bodies, gems, and salmon. J. Cell. Biochem. 70:1998;181-192.
    • (1998) J. Cell. Biochem. , vol.70 , pp. 181-192
    • Matera, A.G.1
  • 35
    • 0033179146 scopus 로고    scopus 로고
    • Nuclear bodies: Multifaceted subdomains of the interchromatin space
    • Matera A. G. Nuclear bodies: Multifaceted subdomains of the interchromatin space. Trends Cell Biol. 9:1999;302-309.
    • (1999) Trends Cell Biol. , vol.9 , pp. 302-309
    • Matera, A.G.1
  • 37
    • 0028227208 scopus 로고
    • Functional substitution of an essential yeast RNA polymerase subunit by a highly conserved mammalian counterpart
    • McKune K., Woychik N. A. Functional substitution of an essential yeast RNA polymerase subunit by a highly conserved mammalian counterpart. Mol. Cell. Biol. 14:1994;4155-4159.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4155-4159
    • McKune, K.1    Woychik, N.A.2
  • 39
    • 0015490858 scopus 로고
    • Visualization of RNA synthesis on chromosomes
    • Miller O. L., Hamkalo B. A. Visualization of RNA synthesis on chromosomes. Int. Rev. Cytol. 33:1972;1-25.
    • (1972) Int. Rev. Cytol. , vol.33 , pp. 1-25
    • Miller, O.L.1    Hamkalo, B.A.2
  • 40
    • 0031834613 scopus 로고    scopus 로고
    • The cellular organization of gene expression
    • Misteli T., Spector D. L. The cellular organization of gene expression. Curr. Opin. Cell Biol. 10:1998;323-331.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 323-331
    • Misteli, T.1    Spector, D.L.2
  • 43
    • 0015947427 scopus 로고
    • Multiple forms of deoxyribonucleic acid-dependent ribonucleic acid polymerase in Xenopus laevis. Levels of activity during oocyte and embryonic development
    • Roeder R. G. Multiple forms of deoxyribonucleic acid-dependent ribonucleic acid polymerase in Xenopus laevis. Levels of activity during oocyte and embryonic development. J. Biol. Chem. 249:1974;249-256.
    • (1974) J. Biol. Chem. , vol.249 , pp. 249-256
    • Roeder, R.G.1
  • 44
    • 0006155776 scopus 로고
    • Structure of lampbrush chromosome loops during different states of transcriptional activity as visualized in the presence of physiological salt concentrations
    • Scheer U. Structure of lampbrush chromosome loops during different states of transcriptional activity as visualized in the presence of physiological salt concentrations. Biol. Cell. 59:1987;33-42.
    • (1987) Biol. Cell , vol.59 , pp. 33-42
    • Scheer, U.1
  • 45
    • 0032695210 scopus 로고    scopus 로고
    • Nuclear domains enriched in RNA 3′ processing factors associate with coiled bodies and histone genes in a cell cycle-dependent fashion
    • Schul W., van der Kraan I., Matera A. G., van Driel R., de Jong L. Nuclear domains enriched in RNA 3′ processing factors associate with coiled bodies and histone genes in a cell cycle-dependent fashion. Mol. Biol. Cell. 10:1999;3815-3824.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3815-3824
    • Schul, W.1    Van Der Kraan, I.2    Matera, A.G.3    Van Driel, R.4    De Jong, L.5
  • 46
    • 0031667334 scopus 로고    scopus 로고
    • Coiled bodies and U2 snRNA genes adjacent to coiled bodies are enriched in factors required for snRNA transcription
    • Schul W., van Driel R., de Jong L. Coiled bodies and U2 snRNA genes adjacent to coiled bodies are enriched in factors required for snRNA transcription. Mol. Biol. Cell. 9:1998;1025-1036.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1025-1036
    • Schul, W.1    Van Driel, R.2    De Jong, L.3
  • 47
    • 0019473616 scopus 로고
    • In vitro RNA synthesis in oocyte nuclei of the newt Notophthalmus
    • Schultz L. D., Kay B. K., Gall J. G. In vitro RNA synthesis in oocyte nuclei of the newt Notophthalmus. Chromosoma. 82:1981;171-187.
    • (1981) Chromosoma , vol.82 , pp. 171-187
    • Schultz, L.D.1    Kay, B.K.2    Gall, J.G.3
  • 48
    • 0017091157 scopus 로고
    • The inhibition by DRB (5,6-dichloro-1-β-d-ribofuranosylbenzimidazole) of hnRNA and mRNA production in HeLa cells
    • Sehgal P. B., Darnell J. E., Tamm I. The inhibition by DRB (5,6-dichloro-1-β-d-ribofuranosylbenzimidazole) of hnRNA and mRNA production in HeLa cells. Cell. 9:1976;473-480.
    • (1976) Cell , vol.9 , pp. 473-480
    • Sehgal, P.B.1    Darnell, J.E.2    Tamm, I.3
  • 49
    • 0014536593 scopus 로고
    • Evidence for a polarized movement of the lateral loops of newt lampbrush chromosomes during oogenesis
    • Snow M. H. L., Callan H. G. Evidence for a polarized movement of the lateral loops of newt lampbrush chromosomes during oogenesis. J. Cell Sci. 5:1969;1-25.
    • (1969) J. Cell Sci. , vol.5 , pp. 1-25
    • Snow, M.H.L.1    Callan, H.G.2
  • 50
    • 0024328155 scopus 로고
    • Inhibition of in vivo and in vitro transcription by monoclonal antibodies prepared against wheat germ RNA polymerase II that react with the heptapeptide repeat of eukaryotic RNA polymerase II
    • Thompson N. E., Steinberg T. H., Aronson D. B., Burgess R. R. Inhibition of in vivo and in vitro transcription by monoclonal antibodies prepared against wheat germ RNA polymerase II that react with the heptapeptide repeat of eukaryotic RNA polymerase II. J. Biol. Chem. 264:1989;11511-11520.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11511-11520
    • Thompson, N.E.1    Steinberg, T.H.2    Aronson, D.B.3    Burgess, R.R.4
  • 51
    • 0027324153 scopus 로고
    • Identification and characterization of a sphere organelle protein
    • Tuma R., Stolk J. A., Roth M. B. Identification and characterization of a sphere organelle protein. J. Cell Biol. 122:1993;767-773.
    • (1993) J. Cell Biol. , vol.122 , pp. 767-773
    • Tuma, R.1    Stolk, J.A.2    Roth, M.B.3
  • 52
    • 0015828732 scopus 로고
    • Protein incorporation by isolated amphibian oocytes. III. Optimum incubation conditions
    • Wallace R. A., Jared D. W., Dumont J. N., Sega M. W. Protein incorporation by isolated amphibian oocytes. III. Optimum incubation conditions. J. Exp. Zool. 184:1973;321-333.
    • (1973) J. Exp. Zool. , vol.184 , pp. 321-333
    • Wallace, R.A.1    Jared, D.W.2    Dumont, J.N.3    Sega, M.W.4
  • 53
    • 0025818887 scopus 로고
    • Small nuclear ribonucleoproteins and heterogeneous nuclear ribonucleoproteins in the amphibian germinal vesicle: Loops, spheres, and snurposomes
    • Wu Z., Murphy C., Callan H. G., Gall J. G. Small nuclear ribonucleoproteins and heterogeneous nuclear ribonucleoproteins in the amphibian germinal vesicle: Loops, spheres, and snurposomes. J. Cell Biol. 113:1991;465-483.
    • (1991) J. Cell Biol. , vol.113 , pp. 465-483
    • Wu, Z.1    Murphy, C.2    Callan, H.G.3    Gall, J.G.4
  • 54
    • 0028787404 scopus 로고
    • The transcriptional elongation inhibitor 5,6-dichloro-1-β-d-ribofuranosyl benzimidazole inhibits transcription factor IIH-associated protein kinase
    • Yankulov K., Yamashita K., Roy R., Egly J.-M., Bentley D. L. The transcriptional elongation inhibitor 5,6-dichloro-1-β-d-ribofuranosyl benzimidazole inhibits transcription factor IIH-associated protein kinase. J. Biol. Chem. 270:1995;23922-23925.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23922-23925
    • Yankulov, K.1    Yamashita, K.2    Roy, R.3    Egly, J.-M.4    Bentley, D.L.5
  • 55
    • 0029942906 scopus 로고    scopus 로고
    • TFIIH functions in regulating transcriptional elongation by RNA polymerase II in Xenopus oocytes
    • Yankulov K. Y., Pandes M., McCracken S., Bouchard D., Bentley D. L. TFIIH functions in regulating transcriptional elongation by RNA polymerase II in Xenopus oocytes. Mol. Cell. Biol. 16:1996;3291-3299.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3291-3299
    • Yankulov, K.Y.1    Pandes, M.2    McCracken, S.3    Bouchard, D.4    Bentley, D.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.