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Volumn 16, Issue 6, 2012, Pages 793-803

Translational recoding in archaea

Author keywords

Gene expression; Hyperthermophiles; Programmed frameshifting; Pseudogenes; Stop codon readthrough

Indexed keywords

ARCHAEAL PROTEIN; DRUG DERIVATIVE; LYSINE; PYRROLYSINE; SELENOCYSTEINE;

EID: 84868363982     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-012-0482-8     Document Type: Review
Times cited : (27)

References (83)
  • 2
    • 72649106932 scopus 로고    scopus 로고
    • The selenium to selenoprotein pathway in eukaryotes: more molecular partners than anticipated
    • Allmang C, Wurth L, Krol A (2009) The selenium to selenoprotein pathway in eukaryotes: more molecular partners than anticipated. Biochim Biophys Acta 1790: 1415-1423.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1415-1423
    • Allmang, C.1    Wurth, L.2    Krol, A.3
  • 4
  • 5
    • 78651536777 scopus 로고    scopus 로고
    • An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea
    • Atkinson GC, Hauryliuk V, Tenson T (2011) An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea. BMC Evol Biol 11: 22-31.
    • (2011) BMC Evol Biol , vol.11 , pp. 22-31
    • Atkinson, G.C.1    Hauryliuk, V.2    Tenson, T.3
  • 6
    • 0025996978 scopus 로고
    • Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium
    • Axley MJ, Bock A, Stadtman TC (1991) Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium. Proc Natl Acad Sci USA 88: 8450-8454.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8450-8454
    • Axley, M.J.1    Bock, A.2    Stadtman, T.C.3
  • 7
    • 0346155809 scopus 로고    scopus 로고
    • Pseudogenes: are they "Junk" or functional DNA?
    • Balakirev ES, Ayala FJ (2003) Pseudogenes: are they "Junk" or functional DNA? Annu Rev Genet 37: 123-151.
    • (2003) Annu Rev Genet , vol.37 , pp. 123-151
    • Balakirev, E.S.1    Ayala, F.J.2
  • 8
    • 0037139583 scopus 로고    scopus 로고
    • Recoding: translational bifurcations in gene expression
    • Baranov PV, Gesteland RF, Atkins JF (2002) Recoding: translational bifurcations in gene expression. Gene 286: 187-201.
    • (2002) Gene , vol.286 , pp. 187-201
    • Baranov, P.V.1    Gesteland, R.F.2    Atkins, J.F.3
  • 12
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA
    • Chambers I, Frampton J, Goldfarb P, Affara N, McBain W, Harrison PR (1986) The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA. EMBO J 5: 1221-1227.
    • (1986) EMBO J , vol.5 , pp. 1221-1227
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    McBain, W.5    Harrison, P.R.6
  • 13
    • 20444480652 scopus 로고    scopus 로고
    • Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes
    • Chavatte L, Brown BA, Driscoll DM (2005) Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes. Nat Struct Mol Biol 12: 408-416.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 408-416
    • Chavatte, L.1    Brown, B.A.2    Driscoll, D.M.3
  • 14
    • 0038353117 scopus 로고    scopus 로고
    • Identification of an archaeal alpha-l-fucosidase encoded by an interrupted gene-production of a functional enzyme by mutations mimicking programmed-1 frameshifting
    • Cobucci-Ponzano B, Trincone A, Giordano A, Rossi M, Moracci M (2003a) Identification of an archaeal alpha-l-fucosidase encoded by an interrupted gene-production of a functional enzyme by mutations mimicking programmed-1 frameshifting. J Biol Chem 278: 14622-14631.
    • (2003) J Biol Chem , vol.278 , pp. 14622-14631
    • Cobucci-Ponzano, B.1    Trincone, A.2    Giordano, A.3    Rossi, M.4    Moracci, M.5
  • 15
    • 0042527531 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant
    • Cobucci-Ponzano B, Trincone A, Giordano A, Rossi M, Moracci M (2003b) Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant. Biochemistry 42: 9525-9531.
    • (2003) Biochemistry , vol.42 , pp. 9525-9531
    • Cobucci-Ponzano, B.1    Trincone, A.2    Giordano, A.3    Rossi, M.4    Moracci, M.5
  • 16
    • 17644427704 scopus 로고    scopus 로고
    • Probing the catalytically essential residues of the alpha-l-fucosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus
    • Cobucci-Ponzano B, Mazzone M, Rossi M, Moracci M (2005a) Probing the catalytically essential residues of the alpha-l-fucosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus. Biochemistry 44: 6331-6342.
    • (2005) Biochemistry , vol.44 , pp. 6331-6342
    • Cobucci-Ponzano, B.1    Mazzone, M.2    Rossi, M.3    Moracci, M.4
  • 21
    • 0001398071 scopus 로고
    • Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety
    • Cone JE, Del Rio RM, Davis JN, Stadtman TC (1976) Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety. Proc Natl Acad Sci USA 73: 2659-2663.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2659-2663
    • Cone, J.E.1    Del Rio, R.M.2    Davis, J.N.3    Stadtman, T.C.4
  • 22
    • 0034677213 scopus 로고    scopus 로고
    • A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs
    • Copeland PR, Fletcher JE, Carlson BA, Hatfield DL, Driscoll DM (2000) A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs. EMBO J 19: 306-314.
    • (2000) EMBO J , vol.19 , pp. 306-314
    • Copeland, P.R.1    Fletcher, J.E.2    Carlson, B.A.3    Hatfield, D.L.4    Driscoll, D.M.5
  • 23
    • 0031935826 scopus 로고    scopus 로고
    • The Mof2/Sui1 protein is a general monitor of translational accuracy
    • Cui Y, Dinman JD, Kinzy TG, Peltz SW (1998) The Mof2/Sui1 protein is a general monitor of translational accuracy. Mol Cell Biol 18: 1506-1516.
    • (1998) Mol Cell Biol , vol.18 , pp. 1506-1516
    • Cui, Y.1    Dinman, J.D.2    Kinzy, T.G.3    Peltz, S.W.4
  • 25
    • 84855906967 scopus 로고    scopus 로고
    • Control of gene expression by translational recoding
    • Dinman JD (2012) Control of gene expression by translational recoding. Adv Protein Chem Struct Biol 86: 129-149.
    • (2012) Adv Protein Chem Struct Biol , vol.86 , pp. 129-149
    • Dinman, J.D.1
  • 26
    • 0029870925 scopus 로고    scopus 로고
    • Programmed translational frameshifting
    • Farabaugh PJ (1996) Programmed translational frameshifting. Microbiol Rev 60: 103.
    • (1996) Microbiol Rev , vol.60 , pp. 103
    • Farabaugh, P.J.1
  • 27
    • 60749118139 scopus 로고    scopus 로고
    • A pyrrolysine analogue for protein click chemistry
    • Fekner T, Li X, Lee MM, Chan MK (2009) A pyrrolysine analogue for protein click chemistry. Angew Chem Int Ed 48: 1633-1635.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 1633-1635
    • Fekner, T.1    Li, X.2    Lee, M.M.3    Chan, M.K.4
  • 29
    • 79959314842 scopus 로고    scopus 로고
    • Functional context, biosynthesis, and genetic encoding of pyrrolysine
    • Gaston MA, Jiang RS, Krzycki JA (2011a) Functional context, biosynthesis, and genetic encoding of pyrrolysine. Curr Opin Microbiol 14: 342-349.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 342-349
    • Gaston, M.A.1    Jiang, R.S.2    Krzycki, J.A.3
  • 30
    • 79953249251 scopus 로고    scopus 로고
    • The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine
    • Gaston MA, Zhang LW, Green-Church KB, Krzycki JA (2011b) The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471: 647-650.
    • (2011) Nature , vol.471 , pp. 647-650
    • Gaston, M.A.1    Zhang, L.W.2    Green-Church, K.B.3    Krzycki, J.A.4
  • 31
    • 79951830445 scopus 로고    scopus 로고
    • Light-activated kinases enable temporal dissection of signaling networks in living cells
    • Gautier A, Deiters A, Chin JW (2011) Light-activated kinases enable temporal dissection of signaling networks in living cells. J Am Chem Soc 133: 2124-2127.
    • (2011) J Am Chem Soc , vol.133 , pp. 2124-2127
    • Gautier, A.1    Deiters, A.2    Chin, J.W.3
  • 32
    • 0029896020 scopus 로고    scopus 로고
    • Recoding: dynamic reprogramming of translation
    • Gesteland RF, Atkins JF (1996) Recoding: dynamic reprogramming of translation. Annu Rev Biochem 65: 741-768.
    • (1996) Annu Rev Biochem , vol.65 , pp. 741-768
    • Gesteland, R.F.1    Atkins, J.F.2
  • 35
    • 0026755739 scopus 로고
    • Methanococcus voltae harbors four gene clusters potentially encoding two [NiFe] and two [NiFeSe] hydrogenases, each of the cofactor F420-reducing or F420-non-reducing types
    • Halboth S, Klein A (1992) Methanococcus voltae harbors four gene clusters potentially encoding two [NiFe] and two [NiFeSe] hydrogenases, each of the cofactor F420-reducing or F420-non-reducing types. Mol Gen Genet 233: 217-224.
    • (1992) Mol Gen Genet , vol.233 , pp. 217-224
    • Halboth, S.1    Klein, A.2
  • 36
    • 77958464370 scopus 로고    scopus 로고
    • Expanding the genetic code of yeast for incorporation of diverse unnatural amino acids via a pyrrolysyl-tRNA synthetase/tRNA pair
    • Hancock SM, Uprety R, Deiters A, Chin JW (2010) Expanding the genetic code of yeast for incorporation of diverse unnatural amino acids via a pyrrolysyl-tRNA synthetase/tRNA pair. J Am Chem Soc 132: 14819-14824.
    • (2010) J Am Chem Soc , vol.132 , pp. 14819-14824
    • Hancock, S.M.1    Uprety, R.2    Deiters, A.3    Chin, J.W.4
  • 37
    • 0037165964 scopus 로고    scopus 로고
    • A new UAG-encoded residue in the structure of a methanogen methyltransferase
    • Hao B, Gong WM, Ferguson TK, James CM, Krzycki JA, Chan MK (2002) A new UAG-encoded residue in the structure of a methanogen methyltransferase. Science 296: 1462-1466.
    • (2002) Science , vol.296 , pp. 1462-1466
    • Hao, B.1    Gong, W.M.2    Ferguson, T.K.3    James, C.M.4    Krzycki, J.A.5    Chan, M.K.6
  • 39
    • 0036314772 scopus 로고    scopus 로고
    • Studying Genomes through the aeons: protein families, pseudogenes and proteome evolution
    • Harrison PM, Gerstein M (2002) Studying Genomes through the aeons: protein families, pseudogenes and proteome evolution. J Mol Biol 318: 1155-1174.
    • (2002) J Mol Biol , vol.318 , pp. 1155-1174
    • Harrison, P.M.1    Gerstein, M.2
  • 42
    • 0035823612 scopus 로고    scopus 로고
    • The amber codon in the gene encoding the monomethylamine methyltransferase isolated from Methanosarcina barkeri is translated as a sense codon
    • James CM, Ferguson TK, Leykam JF, Krzycki JA (2001) The amber codon in the gene encoding the monomethylamine methyltransferase isolated from Methanosarcina barkeri is translated as a sense codon. J Biol Chem 276: 34252-34258.
    • (2001) J Biol Chem , vol.276 , pp. 34252-34258
    • James, C.M.1    Ferguson, T.K.2    Leykam, J.F.3    Krzycki, J.A.4
  • 43
    • 0019497185 scopus 로고
    • Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form
    • Jones JB, Stadtman TC (1981) Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form. J Biol Chem 256: 656-663.
    • (1981) J Biol Chem , vol.256 , pp. 656-663
    • Jones, J.B.1    Stadtman, T.C.2
  • 44
    • 0018420256 scopus 로고
    • Occurrence of selenocysteine in the selenium-dependent formate dehydrogenase of Methanococcus vannielii
    • Jones JB, Dilworth GL, Stadtman TC (1979) Occurrence of selenocysteine in the selenium-dependent formate dehydrogenase of Methanococcus vannielii. Arch Biochem Biophys 195: 255-260.
    • (1979) Arch Biochem Biophys , vol.195 , pp. 255-260
    • Jones, J.B.1    Dilworth, G.L.2    Stadtman, T.C.3
  • 47
    • 2942546160 scopus 로고    scopus 로고
    • The prokaryotic selenoproteome
    • Kryukov GV, Gladyshev VN (2004) The prokaryotic selenoproteome. EMBO Rep 5: 538-543.
    • (2004) EMBO Rep , vol.5 , pp. 538-543
    • Kryukov, G.V.1    Gladyshev, V.N.2
  • 48
    • 4644255236 scopus 로고    scopus 로고
    • Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases
    • Krzycki JA (2004) Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr Opin Chem Biol 8: 484-491.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 484-491
    • Krzycki, J.A.1
  • 49
    • 27844438536 scopus 로고    scopus 로고
    • The direct genetic encoding of pyrrolysine
    • Krzycki JA (2005) The direct genetic encoding of pyrrolysine. Curr Opin Microbiol 8: 706-712.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 706-712
    • Krzycki, J.A.1
  • 50
    • 0031915895 scopus 로고    scopus 로고
    • Universally conserved translation initiation factors
    • Kyrpides NC, Woese CR (1998) Universally conserved translation initiation factors. Proc Natl Acad Sci USA 95: 224-228.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 224-228
    • Kyrpides, N.C.1    Woese, C.R.2
  • 51
    • 70449571896 scopus 로고    scopus 로고
    • A pyrrolysine analogue for site-specific protein ubiquitination
    • Li X, Fekner T, Ottesen JJ, Chan MK (2009) A pyrrolysine analogue for site-specific protein ubiquitination. Angew Chem Int Ed 48: 9184-9187.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 9184-9187
    • Li, X.1    Fekner, T.2    Ottesen, J.J.3    Chan, M.K.4
  • 54
    • 33751081532 scopus 로고    scopus 로고
    • The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes
    • Maeder DL, Anderson I, Brettin TS, Bruce DC, Gilna P, Han CS, Lapidus A, Metcalf WW, Saunders E, Tapia R, Sowers KR (2006) The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes. J Bacteriol 188: 7922-7931.
    • (2006) J Bacteriol , vol.188 , pp. 7922-7931
    • Maeder, D.L.1    Anderson, I.2    Brettin, T.S.3    Bruce, D.C.4    Gilna, P.5    Han, C.S.6    Lapidus, A.7    Metcalf, W.W.8    Saunders, E.9    Tapia, R.10    Sowers, K.R.11
  • 55
    • 0842267214 scopus 로고    scopus 로고
    • Reprogrammed genetic decoding in cellular gene expression
    • Namy O, Rousset JP, Napthine S, Brierley I (2004) Reprogrammed genetic decoding in cellular gene expression. Mol Cell 13: 157-168.
    • (2004) Mol Cell , vol.13 , pp. 157-168
    • Namy, O.1    Rousset, J.P.2    Napthine, S.3    Brierley, I.4
  • 56
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding N-epsilon-acetyllysine in recombinant proteins
    • Neumann H, Peak-Chew SY, Chin JW (2008) Genetically encoding N-epsilon-acetyllysine in recombinant proteins. Nat Chem Biol 4: 232-234.
    • (2008) Nat Chem Biol , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 59
    • 0002317079 scopus 로고
    • The need for selenite and molybdate in the formation of formic dehydrogenase by members of the coli-aerogenes group of bacteria
    • Pinsent J (1954) The need for selenite and molybdate in the formation of formic dehydrogenase by members of the coli-aerogenes group of bacteria. Biochem J 57: 10-16.
    • (1954) Biochem J , vol.57 , pp. 10-16
    • Pinsent, J.1
  • 62
    • 77956800914 scopus 로고    scopus 로고
    • Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea
    • Rother M, Krzycki JA (2010) Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea. Archaea Int Microbiol J.
    • (2010) Archaea Int Microbiol J
    • Rother, M.1    Krzycki, J.A.2
  • 63
    • 0034595505 scopus 로고    scopus 로고
    • Identification and characterisation of the selenocysteine-specific translation factor SelB from the archaeon Methanococcus jannaschii
    • Rother M, Wilting R, Commans S, Bock A (2000) Identification and characterisation of the selenocysteine-specific translation factor SelB from the archaeon Methanococcus jannaschii. J Mol Biol 299: 351-358.
    • (2000) J Mol Biol , vol.299 , pp. 351-358
    • Rother, M.1    Wilting, R.2    Commans, S.3    Bock, A.4
  • 65
    • 0028214048 scopus 로고
    • Translational control in production of transposase and in transposition of insertion sequence-Is3
    • Sekine Y, Eisaki N, Ohtsubo E (1994) Translational control in production of transposase and in transposition of insertion sequence-Is3. J Mol Biol 235: 1406-1420.
    • (1994) J Mol Biol , vol.235 , pp. 1406-1420
    • Sekine, Y.1    Eisaki, N.2    Ohtsubo, E.3
  • 66
    • 80155192426 scopus 로고    scopus 로고
    • A pilot study of bacterial genes with disrupted ORFs reveals a surprising profusion of protein sequence recoding mediated by ribosomal frameshifting and transcriptional realignment
    • Sharma V, Firth AE, Antonov I, Fayet O, Atkins JF, Borodovsky M, Baranov PV (2011) A pilot study of bacterial genes with disrupted ORFs reveals a surprising profusion of protein sequence recoding mediated by ribosomal frameshifting and transcriptional realignment. Mol Biol Evol 28: 3195-3211.
    • (2011) Mol Biol Evol , vol.28 , pp. 3195-3211
    • Sharma, V.1    Firth, A.E.2    Antonov, I.3    Fayet, O.4    Atkins, J.F.5    Borodovsky, M.6    Baranov, P.V.7
  • 68
    • 0027233609 scopus 로고
    • A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is post-translationally processed by cleavage at a defined position
    • Sorgenfrei O, Linder D, Karas M, Klein A (1993) A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is post-translationally processed by cleavage at a defined position. Eur J Biochem 213: 1355-1358.
    • (1993) Eur J Biochem , vol.213 , pp. 1355-1358
    • Sorgenfrei, O.1    Linder, D.2    Karas, M.3    Klein, A.4
  • 69
    • 45549108749 scopus 로고    scopus 로고
    • Eukaryotic selenoprotein synthesis: mechanistic insight incorporating new factors and new functions for old factors
    • Squires JE, Berry MJ (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
  • 70
    • 0037166006 scopus 로고    scopus 로고
    • Pyrrolysine encoded by UAG in archaea: charging of a UAG-decoding specialized tRNA
    • Srinivasan G, James CM, Krzycki JA (2002) Pyrrolysine encoded by UAG in archaea: charging of a UAG-decoding specialized tRNA. Science 296: 1459-1462.
    • (2002) Science , vol.296 , pp. 1459-1462
    • Srinivasan, G.1    James, C.M.2    Krzycki, J.A.3
  • 71
    • 72649093146 scopus 로고    scopus 로고
    • Selenoproteins in archaea and gram-positive bacteria
    • Stock T, Rother M (2009) Selenoproteins in archaea and gram-positive bacteria. Biochim Biophys Acta 1790: 1520-1532.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1520-1532
    • Stock, T.1    Rother, M.2
  • 72
    • 72949104139 scopus 로고    scopus 로고
    • In vivo requirement of selenophosphate for selenoprotein synthesis in archaea
    • Stock T, Selzer M, Rother M (2010) In vivo requirement of selenophosphate for selenoprotein synthesis in archaea. Mol Microbiol 75: 149-160.
    • (2010) Mol Microbiol , vol.75 , pp. 149-160
    • Stock, T.1    Selzer, M.2    Rother, M.3
  • 74
    • 0031017621 scopus 로고    scopus 로고
    • A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri
    • Vorholt JA, Vaupel M, Thauer RK (1997) A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri. Mol Microbiol 23: 1033-1042.
    • (1997) Mol Microbiol , vol.23 , pp. 1033-1042
    • Vorholt, J.A.1    Vaupel, M.2    Thauer, R.K.3
  • 75
    • 0031557397 scopus 로고    scopus 로고
    • Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion
    • Wilting R, Schorling S, Persson BC, Bock A (1997) Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion. J Mol Biol 266: 637-641.
    • (1997) J Mol Biol , vol.266 , pp. 637-641
    • Wilting, R.1    Schorling, S.2    Persson, B.C.3    Bock, A.4
  • 76
    • 4944237752 scopus 로고    scopus 로고
    • Conserved translational frameshift in dsDNA bacteriophage tail assembly genes
    • Xu J, Hendrix RW, Duda RL (2004) Conserved translational frameshift in dsDNA bacteriophage tail assembly genes. Mol Cell 16: 11-21.
    • (2004) Mol Cell , vol.16 , pp. 11-21
    • Xu, J.1    Hendrix, R.W.2    Duda, R.L.3
  • 77
    • 42249114824 scopus 로고    scopus 로고
    • Crystallographic studies on multiple conformational states of active-site loops in pyrrolysyl-tRNA synthetase
    • Yanagisawa T, Ishii R, Fukunaga R, Kobayashi T, Sakamoto K, Yokoyama S (2008a) Crystallographic studies on multiple conformational states of active-site loops in pyrrolysyl-tRNA synthetase. J Mol Biol 378: 634-652.
    • (2008) J Mol Biol , vol.378 , pp. 634-652
    • Yanagisawa, T.1    Ishii, R.2    Fukunaga, R.3    Kobayashi, T.4    Sakamoto, K.5    Yokoyama, S.6
  • 78
    • 56049106840 scopus 로고    scopus 로고
    • Multistep engineering of pyrrolysyl-tRNA synthetase to genetically encode N(epsilon)-(o-Azidobenzyloxycarbonyl) lysine for Site-specific protein modification
    • Yanagisawa T, Ishii R, Fukunaga R, Kobayashi T, Sakamoto K, Yokoyama S (2008b) Multistep engineering of pyrrolysyl-tRNA synthetase to genetically encode N(epsilon)-(o-Azidobenzyloxycarbonyl) lysine for Site-specific protein modification. Chem Biol 15: 1187-1197.
    • (2008) Chem Biol , vol.15 , pp. 1187-1197
    • Yanagisawa, T.1    Ishii, R.2    Fukunaga, R.3    Kobayashi, T.4    Sakamoto, K.5    Yokoyama, S.6
  • 80
    • 20144384309 scopus 로고    scopus 로고
    • Pyrrolysine and selenocysteine use dissimilar decoding strategies
    • Zhang Y, Baranov PV, Atkins JF, Gladyshev VN (2005) Pyrrolysine and selenocysteine use dissimilar decoding strategies. J Biol Chem 280: 20740-20751.
    • (2005) J Biol Chem , vol.280 , pp. 20740-20751
    • Zhang, Y.1    Baranov, P.V.2    Atkins, J.F.3    Gladyshev, V.N.4
  • 81
    • 33845406199 scopus 로고    scopus 로고
    • Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residues
    • Zhang Y, Romero H, Salinas G, Gladyshev VN (2006) Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residues. Genome Biol 7: R94.
    • (2006) Genome Biol , vol.7
    • Zhang, Y.1    Romero, H.2    Salinas, G.3    Gladyshev, V.N.4
  • 82
    • 0001256080 scopus 로고
    • Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli
    • Zinoni F, Birkmann A, Stadtman TC, Bock A (1986) Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. Proc Natl Acad Sci USA 83: 4650-4654.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4650-4654
    • Zinoni, F.1    Birkmann, A.2    Stadtman, T.C.3    Bock, A.4
  • 83
    • 0006385397 scopus 로고
    • Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon
    • Zinoni F, Birkmann A, Leinfelder W, Bock A (1987) Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon. Proc Natl Acad Sci USA 84: 3156-3160.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3156-3160
    • Zinoni, F.1    Birkmann, A.2    Leinfelder, W.3    Bock, A.4


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