메뉴 건너뛰기




Volumn 26, Issue 9, 2009, Pages 2031-2040

Low exchangeability of selenocysteine, the 21st amino acid, in vertebrate proteins

Author keywords

Cysteine; Exchangeability; Selenium; Selenocysteine; Selenoproteins; Vertebrates

Indexed keywords

AMINO ACID; CYSTEINE; ENZYME; PROTEIN; PROTEOME; SELENIUM; SELENOCYSTEINE; SELENOPROTEIN; THIOREDOXIN REDUCTASE;

EID: 68949206430     PISSN: 07374038     EISSN: 15371719     Source Type: Journal    
DOI: 10.1093/molbev/msp109     Document Type: Article
Times cited : (34)

References (64)
  • 1
    • 0037133671 scopus 로고    scopus 로고
    • Metabolic efficiency and amino acid composition in the proteomes of Escherichia coli and Bacillus subtilis
    • Akashi H, Gojobori T. 2002. Metabolic efficiency and amino acid composition in the proteomes of Escherichia coli and Bacillus subtilis. Proc Natl Acad Sci USA. 99:3695-3700.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3695-3700
    • Akashi, H.1    Gojobori, T.2
  • 2
    • 0037307413 scopus 로고    scopus 로고
    • Signatures of natural selection in the human genome
    • Bamshad M, Wooding SP. 2003. Signatures of natural selection in the human genome. Nat Rev Genet. 4:99-111.
    • (2003) Nat Rev Genet , vol.4 , pp. 99-111
    • Bamshad, M.1    Wooding, S.P.2
  • 3
    • 0032555240 scopus 로고    scopus 로고
    • Antarctic fish hemoglobins: Evidence for adaptive evolution at subzero temperature
    • Bargelloni L, Marcato S, Patarnello T. 1998. Antarctic fish hemoglobins: evidence for adaptive evolution at subzero temperature. Proc Natl Acad Sci USA. 95:8670-8675.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8670-8675
    • Bargelloni, L.1    Marcato, S.2    Patarnello, T.3
  • 6
    • 0026722791 scopus 로고
    • Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation
    • Berry MJ, Mai AL, Kieffer J, Harney JW, Larsen P. 1992. Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation. Endocrinology. 131:1448-1852.
    • (1992) Endocrinology , vol.131 , pp. 1448-1852
    • Berry, M.J.1    Mai, A.L.2    Kieffer, J.3    Harney, J.W.4    Larsen, P.5
  • 7
    • 33846696837 scopus 로고    scopus 로고
    • Late-Neoproterozoic deep-ocean oxygenation and the rise of animal life
    • Canfield DE, Poulton SW, Narbonne GM. 2007. Late-Neoproterozoic deep-ocean oxygenation and the rise of animal life. Science. 315:92-95.
    • (2007) Science , vol.315 , pp. 92-95
    • Canfield, D.E.1    Poulton, S.W.2    Narbonne, G.M.3
  • 9
    • 73049092961 scopus 로고    scopus 로고
    • On the unique function of selenocysteine - insights from the evolution of selenoproteins
    • Advanced online publication. doi:10.1016/j.bbagen.2009.03.027
    • Castellano S. 2009. On the unique function of selenocysteine - insights from the evolution of selenoproteins. Biochim Biophys Acta. Advanced online publication. doi:10.1016/j.bbagen.2009.03.027.
    • (2009) Biochim Biophys Acta
    • Castellano, S.1
  • 10
    • 38549134928 scopus 로고    scopus 로고
    • SelenoDB 1.0: A database of selenoprotein genes, proteins and SECIS elements
    • Castellano S, Gladyshev VN, Guigó R, Berry MJ. 2008. SelenoDB 1.0: a database of selenoprotein genes, proteins and SECIS elements. Nucl Acids Res. 36:D339-D343.
    • (2008) Nucl Acids Res , vol.36
    • Castellano, S.1    Gladyshev, V.N.2    Guigó, R.3    Berry, M.J.4
  • 11
    • 28044461261 scopus 로고    scopus 로고
    • Castellano S, Lobanov AV, Chapple C, et al. (11 co-authors). 2005. Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family. Proc Natl Acad Sci USA. 102:16188-16193.
    • Castellano S, Lobanov AV, Chapple C, et al. (11 co-authors). 2005. Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family. Proc Natl Acad Sci USA. 102:16188-16193.
  • 13
    • 31144465926 scopus 로고    scopus 로고
    • Hearing silence: Non-neutral evolution at synonymous sites in mammals
    • Chamary JV, Guigó R, Parmley JL, Hurst LD. 2006. Hearing silence: non-neutral evolution at synonymous sites in mammals. Nat Rev Genet. 7:98-108.
    • (2006) Nat Rev Genet , vol.7 , pp. 98-108
    • Chamary, J.V.1    Guigó, R.2    Parmley, J.L.3    Hurst, L.D.4
  • 14
    • 51849120724 scopus 로고    scopus 로고
    • Relaxation of selective constraints causes independent selenoprotein extinction in insect genomes
    • Chapple CE, Guigó R. 2008. Relaxation of selective constraints causes independent selenoprotein extinction in insect genomes. PLoS ONE. 3:e2968.
    • (2008) PLoS ONE , vol.3
    • Chapple, C.E.1    Guigó, R.2
  • 15
    • 0041317009 scopus 로고    scopus 로고
    • Mechanism and regulation of selenoprotein synthesis
    • Driscoll DM, Copeland DR. 2003. Mechanism and regulation of selenoprotein synthesis. Annu Rev Nutr. 23:17-40.
    • (2003) Annu Rev Nutr , vol.23 , pp. 17-40
    • Driscoll, D.M.1    Copeland, D.R.2
  • 16
    • 47149117454 scopus 로고    scopus 로고
    • Drosophila 12 Genomes Consortium. 2007. Evolution of genes and genomes on the Drosophila phylogeny. Nature. 450:203-218.
    • Drosophila 12 Genomes Consortium. 2007. Evolution of genes and genomes on the Drosophila phylogeny. Nature. 450:203-218.
  • 18
    • 34447546660 scopus 로고    scopus 로고
    • The distribution of fitness effects of new mutations
    • Eyre-Walker A, Keightley PD. 2007. The distribution of fitness effects of new mutations. Nat Rev Genet. 8:610-618.
    • (2007) Nat Rev Genet , vol.8 , pp. 610-618
    • Eyre-Walker, A.1    Keightley, P.D.2
  • 19
    • 84959795073 scopus 로고
    • Phylogenetic analysis under Dollo's law
    • Farris JS. 1977. Phylogenetic analysis under Dollo's law. Syst Zool. 26:77-88.
    • (1977) Syst Zool , vol.26 , pp. 77-88
    • Farris, J.S.1
  • 20
    • 84959747425 scopus 로고
    • Toward defining the course of evolution: Minimum change for a specific tree topology
    • Fitch WM. 1971. Toward defining the course of evolution: minimum change for a specific tree topology. Syst Zool. 20:406-416.
    • (1971) Syst Zool , vol.20 , pp. 406-416
    • Fitch, W.M.1
  • 21
    • 33846481119 scopus 로고    scopus 로고
    • Polymorphism analysis of six selenoprotein genes: Support for a selective sweep at the glutathione peroxidase 1 locus (3p21) in Asian populations
    • Foster CB, Aswath A, Chanock SJ, McKay HF, Peters U. 2006. Polymorphism analysis of six selenoprotein genes: support for a selective sweep at the glutathione peroxidase 1 locus (3p21) in Asian populations. BMC Genet. 7:56.
    • (2006) BMC Genet , vol.7 , pp. 56
    • Foster, C.B.1    Aswath, A.2    Chanock, S.J.3    McKay, H.F.4    Peters, U.5
  • 22
    • 0027399530 scopus 로고    scopus 로고
    • Gish W, States DJ. 1993. Identification of protein coding regions by database similarity search. Nat Genet. 3:266-272.
    • Gish W, States DJ. 1993. Identification of protein coding regions by database similarity search. Nat Genet. 3:266-272.
  • 23
    • 0018692402 scopus 로고
    • The spandrels of San Marco and the Panglossian paradigm
    • Gould SJ, Lewontin RC. 1979. The spandrels of San Marco and the Panglossian paradigm. Proc R Soc Lond. 205:581-598.
    • (1979) Proc R Soc Lond , vol.205 , pp. 581-598
    • Gould, S.J.1    Lewontin, R.C.2
  • 24
    • 0016197604 scopus 로고
    • Amino acid difference formula to help explain protein evolution
    • Grantham R. 1974. Amino acid difference formula to help explain protein evolution. Science. 185:862-864.
    • (1974) Science , vol.185 , pp. 862-864
    • Grantham, R.1
  • 26
    • 0022376704 scopus 로고
    • Dating of the human-ape splitting by a molecular clock of mitochondrial DNA
    • Hasegawa M, Kishino H, Yano T. 1985. Dating of the human-ape splitting by a molecular clock of mitochondrial DNA. J Mol Evol. 22:160-174.
    • (1985) J Mol Evol , vol.22 , pp. 160-174
    • Hasegawa, M.1    Kishino, H.2    Yano, T.3
  • 27
    • 34548346860 scopus 로고    scopus 로고
    • Promoter regions of many neural- and nutrition-related genes have experienced positive selection during human evolution
    • Haygood R, Fedrigo O, Hanson B, Yokoyama KD, Wray GA. 2007. Promoter regions of many neural- and nutrition-related genes have experienced positive selection during human evolution. Nat Genet. 39:1140-1144.
    • (2007) Nat Genet , vol.39 , pp. 1140-1144
    • Haygood, R.1    Fedrigo, O.2    Hanson, B.3    Yokoyama, K.D.4    Wray, G.A.5
  • 28
    • 0036846746 scopus 로고    scopus 로고
    • The origin and evolution of model organisms
    • Hedges SB. 2002. The origin and evolution of model organisms. Nat Rev Genet. 3:838-849.
    • (2002) Nat Rev Genet , vol.3 , pp. 838-849
    • Hedges, S.B.1
  • 30
    • 0036184745 scopus 로고    scopus 로고
    • Generating samples under a Wright-Fisher neutral model of genetic variation
    • Hudson RR. 2002. Generating samples under a Wright-Fisher neutral model of genetic variation. Bioinformatics. 18:337-338.
    • (2002) Bioinformatics , vol.18 , pp. 337-338
    • Hudson, R.R.1
  • 31
    • 0042314356 scopus 로고    scopus 로고
    • Sulfur and selenium: The role of oxidation state in protein structure and function
    • Jacob G, Giles GI, Giles NM, Sies NH. 2003. Sulfur and selenium: the role of oxidation state in protein structure and function. Angew Chem Int Ed. 42:4742-4758.
    • (2003) Angew Chem Int Ed , vol.42 , pp. 4742-4758
    • Jacob, G.1    Giles, G.I.2    Giles, N.M.3    Sies, N.H.4
  • 32
    • 27144469008 scopus 로고    scopus 로고
    • Selenocysteine in proteins - properties and biotechnological use
    • Johansson L, Gafvelin G, Arnér ES. 2005. Selenocysteine in proteins - properties and biotechnological use. Biochim Biophys Acta. 1726:1-13.
    • (2005) Biochim Biophys Acta , vol.1726 , pp. 1-13
    • Johansson, L.1    Gafvelin, G.2    Arnér, E.S.3
  • 33
    • 0025610787 scopus 로고
    • Genetic code 1990
    • Jukes TH. 1990. Genetic code 1990. Experientia. 46:1149-1157.
    • (1990) Experientia , vol.46 , pp. 1149-1157
    • Jukes, T.H.1
  • 36
    • 29144494461 scopus 로고    scopus 로고
    • Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases
    • Kim HY, Gladyshev VN. 2005. Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases. PLoS Biol. 3:e375.
    • (2005) PLoS Biol , vol.3
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 38
    • 0023907071 scopus 로고
    • Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine
    • Leinfelder W, Zehelein E, Mandrand-Berthelot M, Böck A. 1988. Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature. 331:723-725.
    • (1988) Nature , vol.331 , pp. 723-725
    • Leinfelder, W.1    Zehelein, E.2    Mandrand-Berthelot, M.3    Böck, A.4
  • 39
    • 0023087564 scopus 로고
    • A global view of human selenium nutrition
    • Levander OA. 1987. A global view of human selenium nutrition. Ann Rev Nutr. 7:227-250.
    • (1987) Ann Rev Nutr , vol.7 , pp. 227-250
    • Levander, O.A.1
  • 40
    • 37549062738 scopus 로고    scopus 로고
    • Evolutionary dynamics of eukaryotic selenoproteomes: Large selenoproteomes may associate with aquatic life and small with terrestrial life
    • Lobanov AV, Fomenko DE, Zhang Y, Sengupta A, Hatfield DL, Gladyshev VN. 2007. Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic life and small with terrestrial life. Genome Biol. 8:R198.
    • (2007) Genome Biol , vol.8
    • Lobanov, A.V.1    Fomenko, D.E.2    Zhang, Y.3    Sengupta, A.4    Hatfield, D.L.5    Gladyshev, V.N.6
  • 41
    • 45549107469 scopus 로고    scopus 로고
    • Reduced reliance on the trace element selenium during evolution of mammals
    • Lobanov AV, Hatfield DL, Gladyshev VN. 2008a. Reduced reliance on the trace element selenium during evolution of mammals. Genome Biol. 9:R62.
    • (2008) Genome Biol , vol.9
    • Lobanov, A.V.1    Hatfield, D.L.2    Gladyshev, V.N.3
  • 42
    • 37549018459 scopus 로고    scopus 로고
    • Selenoproteinless animals: Selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesis
    • Lobanov AV, Hatfield DL, Gladyshev VN. 2008b. Selenoproteinless animals: selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesis. Protein Sci. 17:176-182.
    • (2008) Protein Sci , vol.17 , pp. 176-182
    • Lobanov, A.V.1    Hatfield, D.L.2    Gladyshev, V.N.3
  • 43
    • 34547396004 scopus 로고    scopus 로고
    • The frailty of adaptive hypotheses for the origins of organismal complexity
    • Lynch M. 2007. The frailty of adaptive hypotheses for the origins of organismal complexity. Proc Natl Acad Sci USA. 104:8597-8604.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8597-8604
    • Lynch, M.1
  • 45
    • 20144388947 scopus 로고    scopus 로고
    • Margulies EH, Vinson JP. NISC Comparative Sequencing Program, et al. (11 co-authors). 2005. An initial strategy for the systematic identification of functional elements in the human genome by low-redundancy comparative sequencing. Proc Natl Acad Sci USA. 102:3354-3359.
    • Margulies EH, Vinson JP. NISC Comparative Sequencing Program, et al. (11 co-authors). 2005. An initial strategy for the systematic identification of functional elements in the human genome by low-redundancy comparative sequencing. Proc Natl Acad Sci USA. 102:3354-3359.
  • 46
    • 1642282195 scopus 로고    scopus 로고
    • The allele frequency spectrum in genome-wide human variation data reveals signals of differential demographic history in three large world populations
    • Marth GT, Czabarka E, Murvai J, Sherry ST. 2004. The allele frequency spectrum in genome-wide human variation data reveals signals of differential demographic history in three large world populations. Genetics. 166:351-372.
    • (2004) Genetics , vol.166 , pp. 351-372
    • Marth, G.T.1    Czabarka, E.2    Murvai, J.3    Sherry, S.T.4
  • 48
    • 35349001696 scopus 로고    scopus 로고
    • Which evolutionary processes influence natural genetic variation for phenotypic traits?
    • Mitchell-Olds T, Willis JH, Goldstein DB. 2007. Which evolutionary processes influence natural genetic variation for phenotypic traits? Nat Rev Genet. 8:845-856.
    • (2007) Nat Rev Genet , vol.8 , pp. 845-856
    • Mitchell-Olds, T.1    Willis, J.H.2    Goldstein, D.B.3
  • 49
    • 0018415510 scopus 로고
    • Two types of amino acid substitutions in protein evolution
    • Miyata T, Miyazawa S, Yasunaga T. 1979. Two types of amino acid substitutions in protein evolution. J Mol Evol. 12:219-236.
    • (1979) J Mol Evol , vol.12 , pp. 219-236
    • Miyata, T.1    Miyazawa, S.2    Yasunaga, T.3
  • 51
    • 33846552919 scopus 로고    scopus 로고
    • Nikolaev S, Montoya-Burgos JI, Margulies EH, ISC Comparative Sequencing Program. Rougemont J, Nyffeler B, Antonarakis SE. 2007. Early history of mammals is elucidated with the ENCODE multiple species sequencing data. PLoS Genet. 3:e2.
    • Nikolaev S, Montoya-Burgos JI, Margulies EH, ISC Comparative Sequencing Program. Rougemont J, Nyffeler B, Antonarakis SE. 2007. Early history of mammals is elucidated with the ENCODE multiple species sequencing data. PLoS Genet. 3:e2.
  • 52
    • 0030928378 scopus 로고    scopus 로고
    • Seq-Gen: An application for the Monte Carlo simulation of DNA sequence evolution along phylogenetic trees
    • Rambaut A, Grassly NC. 1997. Seq-Gen: an application for the Monte Carlo simulation of DNA sequence evolution along phylogenetic trees. Comput Appl Biosci. 13:235-238.
    • (1997) Comput Appl Biosci , vol.13 , pp. 235-238
    • Rambaut, A.1    Grassly, N.C.2
  • 53
    • 0026587399 scopus 로고
    • Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase
    • Rocher C, Lalanne JL, Chaudière J. 1992. Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase. Eur J Biochem. 205:955-960.
    • (1992) Eur J Biochem , vol.205 , pp. 955-960
    • Rocher, C.1    Lalanne, J.L.2    Chaudière, J.3
  • 54
    • 0037910313 scopus 로고    scopus 로고
    • Patterns of transitional mutation biases. within and among mammalian genomes
    • Rosenberg MS, Subramanian S, Kumar S. 2003. Patterns of transitional mutation biases. within and among mammalian genomes. Mol Biol Evol. 20:988-993.
    • (2003) Mol Biol Evol , vol.20 , pp. 988-993
    • Rosenberg, M.S.1    Subramanian, S.2    Kumar, S.3
  • 55
    • 0019381641 scopus 로고
    • Selenium in the environment
    • Shamberger RJ. 1981. Selenium in the environment. Sci Total Environ. 17:59-74.
    • (1981) Sci Total Environ , vol.17 , pp. 59-74
    • Shamberger, R.J.1
  • 56
    • 35348855020 scopus 로고    scopus 로고
    • Identification and characterization of a selenoprotein family containing a diselenide bond in a redox motif
    • Shchedrina VA, Novoselov SV, Malinouski MY, Gladyshev VN. 2007. Identification and characterization of a selenoprotein family containing a diselenide bond in a redox motif. Proc Natl Acad Sci USA. 104:13919-13924.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13919-13924
    • Shchedrina, V.A.1    Novoselov, S.V.2    Malinouski, M.Y.3    Gladyshev, V.N.4
  • 57
  • 58
    • 0031230362 scopus 로고    scopus 로고
    • Environmental occurrence of selenium in waters and related health significance
    • Valentine JL. 1997. Environmental occurrence of selenium in waters and related health significance. Biomed Environ Sci. 10:292-299.
    • (1997) Biomed Environ Sci , vol.10 , pp. 292-299
    • Valentine, J.L.1
  • 59
    • 0035895505 scopus 로고    scopus 로고
    • Venter JC, Adams MD, Myers EW, et al. (275 co-authors). 2001. The sequence of the human genome. Science. 291:1304-1351.
    • Venter JC, Adams MD, Myers EW, et al. (275 co-authors). 2001. The sequence of the human genome. Science. 291:1304-1351.
  • 62
    • 25444482352 scopus 로고    scopus 로고
    • The exchangeability of amino acids in proteins
    • Yampolsky LY, Stoltzfus A. 2005. The exchangeability of amino acids in proteins. Genetics. 170:1459-1472.
    • (2005) Genetics , vol.170 , pp. 1459-1472
    • Yampolsky, L.Y.1    Stoltzfus, A.2
  • 63
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • Zhong L, Holmgren A. 2000. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J Biol Chem. 275:18121-18128.
    • (2000) J Biol Chem , vol.275 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2
  • 64
    • 0034791426 scopus 로고    scopus 로고
    • A simple algorithm to infer gene duplication and speciation events on a gene tree
    • Zmasek CM, Eddy SR. 2001. A simple algorithm to infer gene duplication and speciation events on a gene tree. Bioinformatics. 17:821-828.
    • (2001) Bioinformatics , vol.17 , pp. 821-828
    • Zmasek, C.M.1    Eddy, S.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.