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Volumn 51, Issue 3, 2013, Pages 151-161

Iron availability modulates aberrant splicing of ferrochelatase through the iron- and 2-oxoglutarate dependent dioxygenase Jmjd6 and U2AF65

Author keywords

Aberrant splicing; Ferrochelatase; Iron; Jmjd6; U2AF65

Indexed keywords

2 OXOGLUTARIC ACID; DIOXYGENASE; FERROCHELATASE; IRON; JUMONJI DOMAIN CONTAINING PROTEIN 6; LYSINE; MESSENGER RNA; MESSENGER RNA PRECURSOR; PROTEIN; SMALL INTERFERING RNA; U2 SNRNP AUXILIARY FACTOR 65; UNCLASSIFIED DRUG;

EID: 84881025042     PISSN: 10799796     EISSN: 10960961     Source Type: Journal    
DOI: 10.1016/j.bcmd.2013.05.008     Document Type: Article
Times cited : (31)

References (45)
  • 2
    • 0000718795 scopus 로고    scopus 로고
    • Disorders of heme biosynthesis: X-linked sideroblastic anemia and the porphyrias
    • McGraw-Hill, New York, C.R. Scriver, M. Beaugrand, W.S. Sly, D. Valle (Eds.)
    • Anderson K., Sassa S., Bishop D.F., Desnick R.J. Disorders of heme biosynthesis: X-linked sideroblastic anemia and the porphyrias. The Metabolic and Molecular Basis of Inherited Disease 2001, 2991-3062. McGraw-Hill, New York. C.R. Scriver, M. Beaugrand, W.S. Sly, D. Valle (Eds.).
    • (2001) The Metabolic and Molecular Basis of Inherited Disease , pp. 2991-3062
    • Anderson, K.1    Sassa, S.2    Bishop, D.F.3    Desnick, R.J.4
  • 4
    • 69749102217 scopus 로고    scopus 로고
    • Iron intake does not significantly correlate with iron deficiency among young Japanese women: a cross-sectional study
    • Asakura K., Sasaki S., Murakami K., et al. Iron intake does not significantly correlate with iron deficiency among young Japanese women: a cross-sectional study. Public Health Nutr. 2009, 12:1373-1383.
    • (2009) Public Health Nutr. , vol.12 , pp. 1373-1383
    • Asakura, K.1    Sasaki, S.2    Murakami, K.3
  • 5
    • 79952768708 scopus 로고    scopus 로고
    • Jumonji domain-containing protein 6 (Jmjd6) is required for angiogenic sprouting and regulates splicing of VEGF-receptor 1
    • Boeckel J.N., Guarani V., Koyanagi M., et al. Jumonji domain-containing protein 6 (Jmjd6) is required for angiogenic sprouting and regulates splicing of VEGF-receptor 1. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:3276-3281.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 3276-3281
    • Boeckel, J.N.1    Guarani, V.2    Koyanagi, M.3
  • 6
    • 0032725555 scopus 로고    scopus 로고
    • Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer
    • Burden A.E., Wu C., Dailey T.A., et al. Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer. Biochim. Biophys. Acta 1999, 1435:191-197.
    • (1999) Biochim. Biophys. Acta , vol.1435 , pp. 191-197
    • Burden, A.E.1    Wu, C.2    Dailey, T.A.3
  • 7
    • 77949328686 scopus 로고    scopus 로고
    • Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery
    • Crooks D.R., Ghosh M.C., Haller R.G., et al. Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery. Blood 2010, 115:860-869.
    • (2010) Blood , vol.115 , pp. 860-869
    • Crooks, D.R.1    Ghosh, M.C.2    Haller, R.G.3
  • 8
    • 42449112043 scopus 로고    scopus 로고
    • Distinct ex vivo susceptibility of B-cell subsets to epstein-barr virus infection according to differentiation status and tissue origin
    • Dorner M., Zucol F., Berger C., et al. Distinct ex vivo susceptibility of B-cell subsets to epstein-barr virus infection according to differentiation status and tissue origin. J. Virol. 2008, 82:4400-4412.
    • (2008) J. Virol. , vol.82 , pp. 4400-4412
    • Dorner, M.1    Zucol, F.2    Berger, C.3
  • 9
    • 0001037808 scopus 로고
    • Cycloheximide: aspects of inhibition of protein synthesis in mammalian cells
    • Ennis H.L., Lubin M. Cycloheximide: aspects of inhibition of protein synthesis in mammalian cells. Science 1964, 146:1474-1476.
    • (1964) Science , vol.146 , pp. 1474-1476
    • Ennis, H.L.1    Lubin, M.2
  • 10
    • 0028234733 scopus 로고
    • Mammalian ferrochelatase, a new addition to the metalloenzyme family
    • Ferreira G.C., Franco R., Lloyd S.G., et al. Mammalian ferrochelatase, a new addition to the metalloenzyme family. J. Biol. Chem. 1994, 269:7062-7065.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7062-7065
    • Ferreira, G.C.1    Franco, R.2    Lloyd, S.G.3
  • 11
    • 78651320424 scopus 로고    scopus 로고
    • The UCSC Genome Browser database: update 2011
    • Fujita P.A., Rhead B., Zweig A.S., et al. The UCSC Genome Browser database: update 2011. Nucleic Acids Res. 2011, 39:D876-D882.
    • (2011) Nucleic Acids Res. , vol.39
    • Fujita, P.A.1    Rhead, B.2    Zweig, A.S.3
  • 12
    • 29244454253 scopus 로고    scopus 로고
    • Contribution of a common single-nucleotide polymorphism to the genetic predisposition for erythropoietic protoporphyria
    • Gouya L., Martin-Schmitt C., Robreau A.M., et al. Contribution of a common single-nucleotide polymorphism to the genetic predisposition for erythropoietic protoporphyria. Am. J. Hum. Genet. 2006, 78:2-14.
    • (2006) Am. J. Hum. Genet. , vol.78 , pp. 2-14
    • Gouya, L.1    Martin-Schmitt, C.2    Robreau, A.M.3
  • 13
    • 0036337671 scopus 로고    scopus 로고
    • The penetrance of dominant erythropoietic protoporphyria is modulated by expression of wildtype FECH
    • Gouya L., Puy H., Robreau A.M., et al. The penetrance of dominant erythropoietic protoporphyria is modulated by expression of wildtype FECH. Nat. Genet. 2002, 30:27-28.
    • (2002) Nat. Genet. , vol.30 , pp. 27-28
    • Gouya, L.1    Puy, H.2    Robreau, A.M.3
  • 14
    • 0343517444 scopus 로고    scopus 로고
    • Evidence for substrate-specific requirement of the splicing factor U2AF(35) and for its function after polypyrimidine tract recognition by U2AF(65)
    • Guth S., Martinez C., Gaur R.K., Valcarcel J. Evidence for substrate-specific requirement of the splicing factor U2AF(35) and for its function after polypyrimidine tract recognition by U2AF(65). Mol. Cell. Biol. 1999, 19:8263-8271.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8263-8271
    • Guth, S.1    Martinez, C.2    Gaur, R.K.3    Valcarcel, J.4
  • 15
    • 85008740092 scopus 로고    scopus 로고
    • Up-frameshift protein 1 (UPF1): multitalented entertainer in RNA decay
    • Imamachi N., Tani H., Akimitsu N. Up-frameshift protein 1 (UPF1): multitalented entertainer in RNA decay. Drug Discov. Ther. 2012, 6:55-61.
    • (2012) Drug Discov. Ther. , vol.6 , pp. 55-61
    • Imamachi, N.1    Tani, H.2    Akimitsu, N.3
  • 16
    • 0018610784 scopus 로고
    • New micro-turbidimetric method for determination of protein in cerebrospinal fluid and urine
    • Iwata J., Nishikaze O. New micro-turbidimetric method for determination of protein in cerebrospinal fluid and urine. Clin. Chem. 1979, 25:1317-1319.
    • (1979) Clin. Chem. , vol.25 , pp. 1317-1319
    • Iwata, J.1    Nishikaze, O.2
  • 17
    • 84863523889 scopus 로고    scopus 로고
    • A broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65)
    • Jenkins J.L., Laird K.M., Kielkopf C.L. A broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65). Biochemistry 2012, 51:5223-5225.
    • (2012) Biochemistry , vol.51 , pp. 5223-5225
    • Jenkins, J.L.1    Laird, K.M.2    Kielkopf, C.L.3
  • 18
    • 0042671357 scopus 로고    scopus 로고
    • Pre-mRNA splicing: awash in a sea of proteins
    • Jurica M.S., Moore M.J. Pre-mRNA splicing: awash in a sea of proteins. Mol. Cell 2003, 12:5-14.
    • (2003) Mol. Cell , vol.12 , pp. 5-14
    • Jurica, M.S.1    Moore, M.J.2
  • 20
    • 0036226603 scopus 로고    scopus 로고
    • BLAT-the BLAST-like alignment tool
    • Kent W.J. BLAT-the BLAST-like alignment tool. Genome Res. 2002, 12:656-664.
    • (2002) Genome Res. , vol.12 , pp. 656-664
    • Kent, W.J.1
  • 21
    • 0036079158 scopus 로고    scopus 로고
    • The human genome browser at UCSC
    • Kent W.J., Sugnet C.W., Furey T.S., et al. The human genome browser at UCSC. Genome Res. 2002, 12:996-1006.
    • (2002) Genome Res. , vol.12 , pp. 996-1006
    • Kent, W.J.1    Sugnet, C.W.2    Furey, T.S.3
  • 22
    • 17444385938 scopus 로고    scopus 로고
    • Induction of a SSAT isoform in response to hypoxia or iron deficiency and its protective effects on cell death
    • Kim K., Ryu J.H., Park J.W., et al. Induction of a SSAT isoform in response to hypoxia or iron deficiency and its protective effects on cell death. Biochem. Biophys. Res. Commun. 2005, 331:78-85.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 78-85
    • Kim, K.1    Ryu, J.H.2    Park, J.W.3
  • 23
    • 0019142091 scopus 로고
    • Human myeloid leukemia cell lines: a review
    • Koeffler H.P., Golde D.W. Human myeloid leukemia cell lines: a review. Blood 1980, 56:344-350.
    • (1980) Blood , vol.56 , pp. 344-350
    • Koeffler, H.P.1    Golde, D.W.2
  • 24
    • 56749085451 scopus 로고    scopus 로고
    • Body iron metabolism and pathophysiology of iron overload
    • Kohgo Y., Ikuta K., Ohtake T., et al. Body iron metabolism and pathophysiology of iron overload. Int. J. Hematol. 2008, 88:7-15.
    • (2008) Int. J. Hematol. , vol.88 , pp. 7-15
    • Kohgo, Y.1    Ikuta, K.2    Ohtake, T.3
  • 25
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in human
    • Kumar S., Bandyopadhyay U. Free heme toxicity and its detoxification systems in human. Toxicol. Lett. 2005, 157:175-188.
    • (2005) Toxicol. Lett. , vol.157 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 27
    • 0037422575 scopus 로고    scopus 로고
    • Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans
    • Lewis B.P., Green R.E., Brenner S.E. Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:189-192.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 189-192
    • Lewis, B.P.1    Green, R.E.2    Brenner, S.E.3
  • 28
    • 0016640079 scopus 로고
    • Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome
    • Lozzio C.B., Lozzio B.B. Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome. Blood 1975, 45:321-334.
    • (1975) Blood , vol.45 , pp. 321-334
    • Lozzio, C.B.1    Lozzio, B.B.2
  • 29
    • 0024316258 scopus 로고
    • A micro-method for measuring total protein in cerebrospinal fluid by using benzethonium chloride in microtiter plate wells
    • Luxton R.W., Patel P., Keir G., Thompson E.J. A micro-method for measuring total protein in cerebrospinal fluid by using benzethonium chloride in microtiter plate wells. Clin. Chem. 1989, 35:1731-1734.
    • (1989) Clin. Chem. , vol.35 , pp. 1731-1734
    • Luxton, R.W.1    Patel, P.2    Keir, G.3    Thompson, E.J.4
  • 30
    • 79960646885 scopus 로고    scopus 로고
    • Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF
    • Mackereth C.D., Madl T., Bonnal S., et al. Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF. Nature 2011, 475:408-411.
    • (2011) Nature , vol.475 , pp. 408-411
    • Mackereth, C.D.1    Madl, T.2    Bonnal, S.3
  • 31
    • 0032126635 scopus 로고    scopus 로고
    • Analysis of the human ferrochelatase promoter in transgenic mice
    • Magness S.T., Tugores A., Diala E.S., Brenner D.A. Analysis of the human ferrochelatase promoter in transgenic mice. Blood 1998, 92:320-328.
    • (1998) Blood , vol.92 , pp. 320-328
    • Magness, S.T.1    Tugores, A.2    Diala, E.S.3    Brenner, D.A.4
  • 32
    • 33750053338 scopus 로고    scopus 로고
    • In vivo requirement of the small subunit of U2AF for recognition of a weak 3' splice site
    • Pacheco T.R., Coelho M.B., Desterro J.M., et al. In vivo requirement of the small subunit of U2AF for recognition of a weak 3' splice site. Mol. Cell. Biol. 2006, 26:8183-8190.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8183-8190
    • Pacheco, T.R.1    Coelho, M.B.2    Desterro, J.M.3
  • 33
    • 28644444870 scopus 로고    scopus 로고
    • A GFP-based reporter system to monitor nonsense-mediated mRNA decay
    • Paillusson A., Hirschi N., Vallan C., et al. A GFP-based reporter system to monitor nonsense-mediated mRNA decay. Nucleic Acids Res. 2005, 33:e54.
    • (2005) Nucleic Acids Res. , vol.33
    • Paillusson, A.1    Hirschi, N.2    Vallan, C.3
  • 34
    • 0032964289 scopus 로고    scopus 로고
    • Cellular iron metabolism
    • Ponka P. Cellular iron metabolism. Kidney Int. Suppl. 1999, 69:S2-S11.
    • (1999) Kidney Int. Suppl. , vol.69
    • Ponka, P.1
  • 35
    • 79956220088 scopus 로고    scopus 로고
    • Inhibition of 2-oxoglutarate dependent oxygenases
    • Rose N.R., McDonough M.A., King O.N., et al. Inhibition of 2-oxoglutarate dependent oxygenases. Chem. Soc. Rev. 2011, 40:4364-4397.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 4364-4397
    • Rose, N.R.1    McDonough, M.A.2    King, O.N.3
  • 37
    • 0031779289 scopus 로고    scopus 로고
    • Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria
    • Rufenacht U.B., Gouya L., Schneider-Yin X., et al. Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria. Am. J. Hum. Genet. 1998, 62:1341-1352.
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 1341-1352
    • Rufenacht, U.B.1    Gouya, L.2    Schneider-Yin, X.3
  • 38
    • 0034663191 scopus 로고    scopus 로고
    • Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria
    • Schneider-Yin X., Gouya L., Dorsey M., et al. Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria. Blood 2000, 96:1545-1549.
    • (2000) Blood , vol.96 , pp. 1545-1549
    • Schneider-Yin, X.1    Gouya, L.2    Dorsey, M.3
  • 40
    • 0033862936 scopus 로고    scopus 로고
    • Regulation of the expression of human ferrochelatase by intracellular iron levels
    • Taketani S., Adachi Y., Nakahashi Y. Regulation of the expression of human ferrochelatase by intracellular iron levels. Eur. J. Biochem. 2000, 267:4685-4692.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4685-4692
    • Taketani, S.1    Adachi, Y.2    Nakahashi, Y.3
  • 41
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 0035488612 scopus 로고    scopus 로고
    • Dietary habits among the JPHC study participants at baseline survey. Japan Public Health Center-based Prospective Study on Cancer and Cardiovascular Diseases
    • Tsugane S., Sasaki S., Kobayashi M., et al. Dietary habits among the JPHC study participants at baseline survey. Japan Public Health Center-based Prospective Study on Cancer and Cardiovascular Diseases. J. Epidemiol. 2001, 11:S30-S43.
    • (2001) J. Epidemiol. , vol.11
    • Tsugane, S.1    Sasaki, S.2    Kobayashi, M.3
  • 43
    • 0028034531 scopus 로고
    • A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene
    • Tugores A., Magness S.T., Brenner D.A. A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene. J. Biol. Chem. 1994, 269:30789-30797.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30789-30797
    • Tugores, A.1    Magness, S.T.2    Brenner, D.A.3
  • 44
    • 67650072604 scopus 로고    scopus 로고
    • Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing
    • Webby C.J., Wolf A., Gromak N., et al. Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science 2009, 325:90-93.
    • (2009) Science , vol.325 , pp. 90-93
    • Webby, C.J.1    Wolf, A.2    Gromak, N.3
  • 45
    • 0024408832 scopus 로고
    • Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor
    • Zamore P.D., Green M.R. Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. Proc. Natl. Acad. Sci. U. S. A. 1989, 86:9243-9247.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 9243-9247
    • Zamore, P.D.1    Green, M.R.2


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