Published in

Oxford University Press (OUP), Molecular Biology and Evolution, 11(31), p. 2905-2912

DOI: 10.1093/molbev/msu228

Links

Tools

Export citation

Search in Google Scholar

Amino Acid Metabolism Conflicts with Protein Diversity

Journal article published in 2014 by Teresa Krick, Nina Verstraete, Leonardo G. Alonso, David A. Shub, Diego U. Ferreiro ORCID, Michael Shub, Ignacio E. Sanchez, Ignacio E. Sánchez
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Orange circle
Postprint: archiving restricted
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

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.