메뉴 건너뛰기




Volumn 299, Issue 2, 2004, Pages 294-302

Regulated compartmentalization of the putative DEAD-box helicase MDDX28 within the mitochondria in COS-1 cells

Author keywords

Cox; cytochrome c oxidase; EGFP; enhanced green fluorescence protein; mitochondrial DNA; Mitochondrial inner membrane; mitochondrial targeting signal; mtDNA; MTS; paraformaldehyde; PBS; PFA; phosphate buffered saline; Punctate structures; Transcription inhibition

Indexed keywords

ETHIDIUM BROMIDE; HELICASE; PEPTIDE DERIVATIVE; POLYPEPTIDE; RNA BINDING PROTEIN;

EID: 4444341362     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.05.019     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 0020039867 scopus 로고
    • Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: Comparison with endoplasmic reticulum and mitochondrial membranes
    • Fujiki Y., Fowler S., Shio H., Hubbard A.L., Lazarow P.B. Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membranes. J. Cell Biol. 93:1982;103-110
    • (1982) J. Cell Biol. , vol.93 , pp. 103-110
    • Fujiki, Y.1    Fowler, S.2    Shio, H.3    Hubbard, A.L.4    Lazarow, P.B.5
  • 3
    • 0026052097 scopus 로고
    • MRNA leader length and initiation codon context determine alternative AUG selection for the yeast gene MOD5
    • Slusher L.B., Gillman E.C., Martin N.C., Hopper A.K. mRNA leader length and initiation codon context determine alternative AUG selection for the yeast gene MOD5. Proc. Natl. Acad. Sci. U. S. A. 88:1991;9789-9793
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 9789-9793
    • Slusher, L.B.1    Gillman, E.C.2    Martin, N.C.3    Hopper, A.K.4
  • 4
    • 0032531934 scopus 로고    scopus 로고
    • Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localization signal and a strong classical mitochondrial signal, respectively
    • Otterlei M., Haug T., Nagelhus T.A., Slupphaug G., Lindmo T., Krokan H. Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localization signal and a strong classical mitochondrial signal, respectively. Nucleic Acids Res. 26:1998;4611-4617
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4611-4617
    • Otterlei, M.1    Haug, T.2    Nagelhus, T.A.3    Slupphaug, G.4    Lindmo, T.5    Krokan, H.6
  • 5
    • 0033533721 scopus 로고    scopus 로고
    • The yeast CDC9 gene encodes both a nuclear and a mitochondrial form of DNA ligase I
    • Willer M., Rainey M., Pullen T., Stirling C.J. The yeast CDC9 gene encodes both a nuclear and a mitochondrial form of DNA ligase I. Curr. Biol. 9:1999;1085-1094
    • (1999) Curr. Biol. , vol.9 , pp. 1085-1094
    • Willer, M.1    Rainey, M.2    Pullen, T.3    Stirling, C.J.4
  • 6
    • 0032960864 scopus 로고    scopus 로고
    • The human DNA ligase III gene encodes nuclear and mitochondrial proteins
    • Lakshimpathy U., Campbell C. The human DNA ligase III gene encodes nuclear and mitochondrial proteins. Mol. Cell. Biol. 19:1999;3869-3876
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3869-3876
    • Lakshimpathy, U.1    Campbell, C.2
  • 8
    • 0037126059 scopus 로고    scopus 로고
    • Dual localization of human topoisomerase IIIα to mitochondria and nucleus
    • Wang Y., Lyu Y.L., Wang J.C. Dual localization of human topoisomerase IIIα to mitochondria and nucleus. Proc. Natl. Acad. Sci. U. S. A. 99:2002;12114-12119
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12114-12119
    • Wang, Y.1    Lyu, Y.L.2    Wang, J.C.3
  • 9
    • 0035943626 scopus 로고    scopus 로고
    • Cloning and characterization of MDDX28, a putative dead-box helicase with mitochondrial and nuclear localization
    • Valgardsdottir R., Brede G., Eide L.G., Frengen E., Prydz H. Cloning and characterization of MDDX28, a putative dead-box helicase with mitochondrial and nuclear localization. J. Biol. Chem. 276:2001;32056-32063
    • (2001) J. Biol. Chem. , vol.276 , pp. 32056-32063
    • Valgardsdottir, R.1    Brede, G.2    Eide, L.G.3    Frengen, E.4    Prydz, H.5
  • 10
    • 0038079978 scopus 로고    scopus 로고
    • Transport signals and transcription inhibition dependent nuclear localization of the putative DEAD-box helicase MDDX28
    • Valgardsdottir R., Prydz H. Transport signals and transcription inhibition dependent nuclear localization of the putative DEAD-box helicase MDDX28. J. Biol. Chem. 278:2003;21146-21154
    • (2003) J. Biol. Chem. , vol.278 , pp. 21146-21154
    • Valgardsdottir, R.1    Prydz, H.2
  • 11
    • 0037154983 scopus 로고    scopus 로고
    • The contribution of nuclear compartmentalization to gene regulation
    • Carmo-Fonseca M. The contribution of nuclear compartmentalization to gene regulation. Cell. 108:2002;513-521
    • (2002) Cell , vol.108 , pp. 513-521
    • Carmo-Fonseca, M.1
  • 12
  • 13
    • 0018400885 scopus 로고
    • Visualization of yeast mitochondrial DNA with the fluorescent stain 'DAPI'
    • Williamson D.H., Fennel D.J. Visualization of yeast mitochondrial DNA with the fluorescent stain 'DAPI'. Methods Enzymol. 56:1979;728-733
    • (1979) Methods Enzymol. , vol.56 , pp. 728-733
    • Williamson, D.H.1    Fennel, D.J.2
  • 14
    • 0023442326 scopus 로고
    • Isolation of morphologically intact mitochondrial nucleoids from the yeast, Saccharomyces cerevisiae
    • Miyakawa I., Sando N., Kawano S., Nakamura S., Kuroiwa T. Isolation of morphologically intact mitochondrial nucleoids from the yeast, Saccharomyces cerevisiae. J. Cell Sci. 88:1987;431-439
    • (1987) J. Cell Sci. , vol.88 , pp. 431-439
    • Miyakawa, I.1    Sando, N.2    Kawano, S.3    Nakamura, S.4    Kuroiwa, T.5
  • 17
    • 0035931747 scopus 로고    scopus 로고
    • Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability
    • Hobbs A.E., Srinivasan M., McCaffery J.M., Jensen R.E. Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability. J. Cell Biol. 152:2001;401-410
    • (2001) J. Cell Biol. , vol.152 , pp. 401-410
    • Hobbs, A.E.1    Srinivasan, M.2    McCaffery, J.M.3    Jensen, R.E.4
  • 18
    • 0025738016 scopus 로고
    • Freeze-substitution and Lowicryl HM20 embedding of fixed rat brain: Suitability for immunogold ultrastructural localization of neural antigens
    • Van Lookeren Campagne M., Oestreicher A.B., van der Krift T.P., Gispen W.H., Verkleij A.J. Freeze-substitution and Lowicryl HM20 embedding of fixed rat brain: suitability for immunogold ultrastructural localization of neural antigens. J. Histochem. Cytochem. 39:1991;1267-1279
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 1267-1279
    • Van Lookeren Campagne, M.1    Oestreicher, A.B.2    Van Der Krift, T.P.3    Gispen, W.H.4    Verkleij, A.J.5
  • 19
    • 0342375000 scopus 로고    scopus 로고
    • Quantitative immunogold analysis suggests different modes of expression of AMPA and NMDA receptors in hippocampal synapses
    • Takumi Y., Ramirez-Leon V., Rinvik E., Ottersen O.P. Quantitative immunogold analysis suggests different modes of expression of AMPA and NMDA receptors in hippocampal synapses. Nat. Neurosci. 2:1999;618-624
    • (1999) Nat. Neurosci. , vol.2 , pp. 618-624
    • Takumi, Y.1    Ramirez-Leon, V.2    Rinvik, E.3    Ottersen, O.P.4
  • 20
    • 0016376551 scopus 로고
    • The isolation of outer and inner mitochondrial membranes
    • Greenawalt J.W. The isolation of outer and inner mitochondrial membranes. Methods Enzymol. 31:1974;310-323
    • (1974) Methods Enzymol. , vol.31 , pp. 310-323
    • Greenawalt, J.W.1
  • 21
    • 0034703062 scopus 로고    scopus 로고
    • Interaction of mammalian mitochondrial ribosomes with the inner membrane
    • Liu M., Spremulli L. Interaction of mammalian mitochondrial ribosomes with the inner membrane. J. Biol. Chem. 275:2000;29400-29406
    • (2000) J. Biol. Chem. , vol.275 , pp. 29400-29406
    • Liu, M.1    Spremulli, L.2
  • 22
    • 0032421354 scopus 로고    scopus 로고
    • Function of lipid rafts in biological membranes
    • Brown D.A., London E. Function of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14:1998;111-136
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 23
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:1982;97-102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 24
    • 0030740548 scopus 로고    scopus 로고
    • Small nucleolar RNAs and rRNA processing. Delocalization of some small nucleolar RNPs after actinomycin D treatment to deplete early pre-rRNAs
    • Rivera-Leon R., Gerbi S.A. Small nucleolar RNAs and rRNA processing. Delocalization of some small nucleolar RNPs after actinomycin D treatment to deplete early pre-rRNAs. Chromosoma. 105:1997;506-514
    • (1997) Chromosoma , vol.105 , pp. 506-514
    • Rivera-Leon, R.1    Gerbi, S.A.2
  • 26
    • 0032866533 scopus 로고    scopus 로고
    • 3-D organization of ribosomal transcription units after DRB inhibition of RNA polymerase II transcription
    • Le Panse S., Masson C., Heliot L., Chassery J.M., Junera H.R., Hernandez-Verdun D. 3-D organization of ribosomal transcription units after DRB inhibition of RNA polymerase II transcription. J. Cell Sci. 112:1999;2145-2154
    • (1999) J. Cell Sci. , vol.112 , pp. 2145-2154
    • Le Panse, S.1    Masson, C.2    Heliot, L.3    Chassery, J.M.4    Junera, H.R.5    Hernandez-Verdun, D.6
  • 28
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres J.F., Screaton G.R., Krainer A.R. A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev. 12:1998;55-66
    • (1998) Genes Dev. , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 29
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma S., Dreyfuss G. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature. 355:1992;730-732
    • (1992) Nature , vol.355 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 30
    • 0036920468 scopus 로고    scopus 로고
    • PSKH1, a novel splice factor compartment-associated serine kinase
    • Brede G., Solheim J., Prydz H. PSKH1, a novel splice factor compartment-associated serine kinase. Nucleic Acids Res. 30:2002;5301-5309
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5301-5309
    • Brede, G.1    Solheim, J.2    Prydz, H.3
  • 31
    • 0036351201 scopus 로고    scopus 로고
    • Release of snRNP and RNA from transcription sites in adenovirus-infected cells
    • Aspegren A., Bridge E. Release of snRNP and RNA from transcription sites in adenovirus-infected cells. Exp. Cell Res. 276:2002;273-283
    • (2002) Exp. Cell Res. , vol.276 , pp. 273-283
    • Aspegren, A.1    Bridge, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.