메뉴 건너뛰기




Volumn 41, Issue 14, 2013, Pages 6952-6959

UGA codon position-dependent incorporation of selenocysteine into mammalian selenoproteins

Author keywords

[No Author keywords available]

Indexed keywords

SELENOCYSTEINE; SELENOPROTEIN;

EID: 84881506440     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt409     Document Type: Article
Times cited : (29)

References (29)
  • 3
    • 77952563903 scopus 로고    scopus 로고
    • Selenoproteins-What unique properties can arise with selenocysteine in place of cysteiné
    • Arner E.S. (2010) Selenoproteins-What unique properties can arise with selenocysteine in place of cysteiné Exp. Cell Res., 316, 1296-1303
    • (2010) Exp. Cell Res , vol.316 , pp. 1296-1303
    • Arner, E.S.1
  • 4
    • 77649258954 scopus 로고    scopus 로고
    • Threading the needle: Getting selenocysteine into proteins
    • Donovan J. and Copeland P. (2010) Threading the needle: Getting selenocysteine into proteins. Antioxid. Redox Signal., 12, 881-892
    • (2010) Antioxid. Redox Signal , vol.12 , pp. 881-892
    • Donovan, J.1    Copeland, P.2
  • 5
    • 45549108749 scopus 로고    scopus 로고
    • Eukaryotic selenoprotein syn thesis: Mechanistic insight incorporating new factors and new functions for old factors
    • Squires J.E. and Berry M.J. (2008) Eukaryotic selenoprotein synthesis: Mechanistic insight incorporating new factors and new functions for old factors. IUBMB Life, 60, 232-235
    • (2008) IUBMB Life , vol.60 , pp. 232-235
    • Squires, J.E.1    Berry, M.J.2
  • 6
    • 0029832601 scopus 로고    scopus 로고
    • Selenocysteine incorporation in eukaryotes: Insights into mechanism and efficiency from sequence, structure, and spacing proximity studies of the type 1 deiodinase SECIS element
    • Martin G.W. 3rd, Harney J.W. and Berry M.J. (1996) Selenocysteine incorporation in eukaryotes: Insights into mechanism and efficiency from sequence, structure, and spacing proximity studies of the type 1 deiodinase SECIS element. RNA, 2, 171-182
    • (1996) RNA , vol.2 , pp. 171-182
    • Martin III, G.W.1    Harney, J.W.2    Berry, M.J.3
  • 8
    • 0027282772 scopus 로고
    • Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons
    • Berry M.J., Banu L., Harney J.W. and Larsen P.R. (1993) Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons. EMBO J., 12, 3315-3322
    • (1993) EMBO J. , vol.12 , pp. 3315-3322
    • Berry, M.J.1    Banu, L.2    Harney, J.W.3    Larsen, P.R.4
  • 9
    • 0032943632 scopus 로고    scopus 로고
    • Two distinct SECIS structures capable of directing selenocysteine incorporation in eukaryotes
    • Grundner-Culemann E., Martin G.W. 3rd, Harney J.W. and Berry M.J. (1999) Two distinct SECIS structures capable of directing selenocysteine incorporation in eukaryotes. RNA, 5, 625-635
    • (1999) RNA , vol.5 , pp. 625-635
    • Grundner-Culemann, E.1    Martin III, G.W.2    Harney, J.W.3    Berry, M.J.4
  • 10
    • 73049117878 scopus 로고    scopus 로고
    • Novel structural determinants in human SECIS elements modulate the translational recoding of UGA as selenocysteine
    • Latreche L., Jean-Jean O., Driscoll D.M. and Chavatte L. (2009) Novel structural determinants in human SECIS elements modulate the translational recoding of UGA as selenocysteine. Nucleic Acids Res., 37, 5868-5880
    • (2009) Nucleic Acids Res , vol.37 , pp. 5868-5880
    • Latreche, L.1    Jean-Jean, O.2    Driscoll, D.M.3    Chavatte, L.4
  • 11
    • 72649087329 scopus 로고    scopus 로고
    • Selenoprotein P-expression functions, and roles in mammals
    • Burk R.F. and Hill K.E. (2009) Selenoprotein P-expression, functions, and roles in mammals. Biochim. Biophys. Acta., 1790, 1441-1447
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1441-1447
    • Burk, R.F.1    Hill, K.E.2
  • 13
    • 0032561359 scopus 로고    scopus 로고
    • UGA codon position affects the efficiency of selenocysteine incorporation into glutathione peroxidase-1
    • Wen W., Weiss S. and Sunde R. (1998) UGA codon position affects the efficiency of selenocysteine incorporation into glutathione peroxidase-1. J. Biol. Chem., 273, 28533-28541
    • (1998) J. Biol. Chem , vol.273 , pp. 28533-28541
    • Wen, W.1    Weiss, S.2    Sunde, R.3
  • 14
    • 84866335791 scopus 로고    scopus 로고
    • A luciferase reporter assay to investigate the differential selenium-dependent stability of selenoprotein mRNAs
    • Banerjee S., Yang S. and Foster C.B. (2011) A luciferase reporter assay to investigate the differential selenium-dependent stability of selenoprotein mRNAs. J. Nutr. Biochem., 23, 1294-1301
    • (2011) J. Nutr. Biochem , vol.23 , pp. 1294-1301
    • Banerjee, S.1    Yang, S.2    Foster, C.B.3
  • 15
    • 84862235760 scopus 로고    scopus 로고
    • The differential expression of glutathione peroxidase 1 and 4 depends on the nature of the SECIS element
    • Latreche L., Duhieu S., Touat-Hamici Z., Jean-Jean O. and Chavatte L. (2012) The differential expression of glutathione peroxidase 1 and 4 depends on the nature of the SECIS element. RNA Biol., 9, 681-690
    • (2012) RNA Biol , vol.9 , pp. 681-690
    • Latreche, L.1    Duhieu, S.2    Touat-Hamici, Z.3    Jean-Jean, O.4    Chavatte, L.5
  • 16
    • 68949200868 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation
    • Budiman M., Bubenik J., Miniard A., Middleton L., Gerber C., Cash A. and Driscoll D. (2009) Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation. Mol. Cell, 35, 479-489
    • (2009) Mol. Cell , vol.35 , pp. 479-489
    • Budiman, M.1    Bubenik, J.2    Miniard, A.3    Middleton, L.4    Gerber, C.5    Cash, A.6    Driscoll, D.7
  • 17
    • 0036120731 scopus 로고    scopus 로고
    • Mammalian selenoprotein gene signature: Identification and functional analysis of selenoprotein genes using bioinformatics methods
    • Kryukov G.V. and Gladyshev V.N. (2002) Mammalian selenoprotein gene signature: Identification and functional analysis of selenoprotein genes using bioinformatics methods. Methods Enzymol., 347, 84-100
    • (2002) Methods Enzymol , vol.347 , pp. 84-100
    • Kryukov, G.V.1    Gladyshev, V.N.2
  • 18
    • 33747369873 scopus 로고    scopus 로고
    • Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase
    • Turanov A.A., Su D. and Gladyshev V.N. (2006) Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase. J. Biol. Chem., 281, 22953-22963
    • (2006) J. Biol. Chem , vol.281 , pp. 22953-22963
    • Turanov, A.A.1    Su, D.2    Gladyshev, V.N.3
  • 19
    • 77956655098 scopus 로고    scopus 로고
    • Mammalian thioredoxin reductase 1: Roles in redox homoeostasis and characterization of cellular targets
    • Turanov A.A., Kehr S., Marino S.M., Yoo M.H., Carlson B.A., Hatfield D.L. and Gladyshev V.N. (2010) Mammalian thioredoxin reductase 1: Roles in redox homoeostasis and characterization of cellular targets. Biochem. J., 430, 285-293
    • (2010) Biochem. J. , vol.430 , pp. 285-293
    • Turanov, A.A.1    Kehr, S.2    Marino, S.M.3    Yoo, M.H.4    Carlson, B.A.5    Hatfield, D.L.6    Gladyshev, V.N.7
  • 20
    • 22544451578 scopus 로고    scopus 로고
    • Mammalian selenoprotein thioredoxin-glutathione reductase Roles in disulfide bond formation and sperm maturation
    • Su D., Novoselov S.V., Sun Q.A., Moustafa M.E., Zhou Y., Oko R., Hatfield D.L. and Gladyshev V.N. (2005) Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation. J. Biol. Chem., 280, 26491-26498
    • (2005) J. Biol. Chem , vol.280 , pp. 26491-26498
    • Su, D.1    Novoselov, S.V.2    Sun, Q.A.3    Moustafa, M.E.4    Zhou, Y.5    Oko, R.6    Hatfield, D.L.7    Gladyshev, V.N.8
  • 21
    • 0023665902 scopus 로고
    • An analysis of 50-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M. (1987) An analysis of 50-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res., 15, 8125-8148
    • (1987) Nucleic Acids Res , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 23
    • 65549142249 scopus 로고    scopus 로고
    • Secis rnas and k-Turn binding proteins a survey of evolutionary conserved rna and protein motifs
    • Hatfield D., Berry M. and Gladyshev V. (eds, 2nd edn. Springer Science+Business Media, New York, NY, USA
    • Allmang C. and Krol A. (2006) SECIS RNAs and K-Turn binding proteins. A survey of evolutionary conserved RNA and protein motifs. In: Hatfield D., Berry M. and Gladyshev V. (eds), Selenium: Its Molecular Biology and Role in Human Health, 2nd edn. Springer Science+Business Media, New York, NY, USA, pp. 51-61
    • (2006) Selenium: Its Molecular Biology and Role in Human Health , pp. 51-61
    • Allmang, C.1    Krol, A.2
  • 25
    • 0034671770 scopus 로고    scopus 로고
    • SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy
    • Low S.C., Grundner-Culemann E., Harney J.W. and Berry M.J. (2000) SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy. EMBO J., 19, 6882-6890
    • (2000) EMBO J. , vol.19 , pp. 6882-6890
    • Low, S.C.1    Grundner-Culemann, E.2    Harney, J.W.3    Berry, M.J.4
  • 26
    • 68949200868 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation
    • Budiman M.E., Bubenik J.L., Miniard A.C., Middleton L.M., Gerber C.A., Cash A. and Driscoll D.M. (2009) Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation. Mol. Cell, 35, 479-489
    • (2009) Mol. Cell , vol.35 , pp. 479-489
    • Budiman, M.E.1    Bubenik, J.L.2    Miniard, A.C.3    Middleton, L.M.4    Gerber, C.A.5    Cash, A.6    Driscoll, D.M.7
  • 28
    • 80053204231 scopus 로고    scopus 로고
    • Identification of a signature motif for the eIF4a3-SECIS interaction
    • Budiman M.E., Bubenik J.L. and Driscoll D.M. (2011) Identification of a signature motif for the eIF4a3-SECIS interaction. Nucleic Acids Res., 39, 7730-7739
    • (2011) Nucleic Acids Res , vol.39 , pp. 7730-7739
    • Budiman, M.E.1    Bubenik, J.L.2    Driscoll, D.M.3
  • 29
    • 33845432312 scopus 로고    scopus 로고
    • Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck
    • Stoytcheva Z., Tujebajeva R., Harney J. and Berry M. (2006) Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck. Mol. Cell. Biol., 26, 9177-9184
    • (2006) Mol. Cell. Biol , vol.26 , pp. 9177-9184
    • Stoytcheva, Z.1    Tujebajeva, R.2    Harney, J.3    Berry, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.