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Amino Acid metabolism conflicts with protein diversity.
Krick, Teresa; Verstraete, Nina; Alonso, Leonardo G; Shub, David A; Ferreiro, Diego U; Shub, Michael; Sánchez, Ignacio E.
Afiliação
  • Krick T; Departamento de Matemática, Facultad de Ciencias Exactas y Naturales and IMAS-CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Verstraete N; Protein Physiology Laboratory, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales and IQUIBICEN-CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Alonso LG; Fundación Instituto Leloir-IIBBA CONICET, Buenos Aires, Argentina.
  • Shub DA; Department of Biological Sciences, University at Albany, State University of New York.
  • Ferreiro DU; Protein Physiology Laboratory, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales and IQUIBICEN-CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Shub M; IMAS-CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina.
  • Sánchez IE; Protein Physiology Laboratory, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales and IQUIBICEN-CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina isanchez@qb.fcen.uba.ar.
Mol Biol Evol ; 31(11): 2905-12, 2014 Nov.
Article em En | MEDLINE | ID: mdl-25086000
The 20 protein-coding amino acids are found in proteomes with different relative abundances. The most abundant amino acid, leucine, is nearly an order of magnitude more prevalent than the least abundant amino acid, cysteine. Amino acid metabolic costs differ similarly, constraining their incorporation into proteins. On the other hand, a diverse set of protein sequences is necessary to build functional proteomes. Here, we present a simple model for a cost-diversity trade-off postulating that natural proteomes minimize amino acid metabolic flux while maximizing sequence entropy. The model explains the relative abundances of amino acids across a diverse set of proteomes. We found that the data are remarkably well explained when the cost function accounts for amino acid chemical decay. More than 100 organisms reach comparable solutions to the trade-off by different combinations of proteome cost and sequence diversity. Quantifying the interplay between proteome size and entropy shows that proteomes can get optimally large and diverse.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Biossíntese de Proteínas / Genoma / Proteoma / Aminoácidos / Modelos Biológicos Idioma: En Revista: Mol Biol Evol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Argentina País de publicação: Estados Unidos
Texto completo
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XML
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Biossíntese de Proteínas / Genoma / Proteoma / Aminoácidos / Modelos Biológicos Idioma: En Revista: Mol Biol Evol Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Argentina País de publicação: Estados Unidos