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A universal trend of amino acid gain and loss in protein evolution

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TLDR
Comparison of sets of orthologous proteins encoded by triplets of closely related genomes from 15 taxa representing all three domains of life and phylogenies to polarize amino acid substitutions shows expansion of initially under-represented amino acids apparently continues to this day.
Abstract
A comparison of corresponding sets of proteins encoded by closely related genes from organisms representing all three domains of life (Bacteria, Archaea and Eukaryota) suggests that the order in which the genetic code was assembled over 3.5 billion years ago continues to influence the evolution of proteins today. Across these diverse genomes, evolving proteins have accumulated Cys, Met, His, Ser and Phe, and lost many of their Pro, Ala, Glu and Gly residues. The same nine amino acids are currently accrued or lost in human proteins as shown by analysis of nucleotide polymorphisms. The amino acids with declining frequencies were probably among the first incorporated into the genetic code, and most of those with increasing frequencies were probably recruited late. Amino acid composition of proteins varies substantially between taxa and, thus, can evolve. For example, proteins from organisms with (G + C)-rich (or (A + T)-rich) genomes contain more (or fewer) amino acids encoded by (G + C)-rich codons1,2,3,4. However, no universal trends in ongoing changes of amino acid frequencies have been reported. We compared sets of orthologous proteins encoded by triplets of closely related genomes from 15 taxa representing all three domains of life (Bacteria, Archaea and Eukaryota), and used phylogenies to polarize amino acid substitutions. Cys, Met, His, Ser and Phe accrue in at least 14 taxa, whereas Pro, Ala, Glu and Gly are consistently lost. The same nine amino acids are currently accrued or lost in human proteins, as shown by analysis of non-synonymous single-nucleotide polymorphisms. All amino acids with declining frequencies are thought to be among the first incorporated into the genetic code; conversely, all amino acids with increasing frequencies, except Ser, were probably recruited late5,6,7. Thus, expansion of initially under-represented amino acids, which began over 3,400 million years ago8,9, apparently continues to this day.

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The changing faces of glutathione, a cellular protagonist

TL;DR: The significance of GSH as a major factor in regulation of cell life, proliferation, and death, should be regarded as the integrated result of all these roles it can play.
Journal ArticleDOI

Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility

TL;DR: In this article, the pK values of the ionizable groups in proteins and their relationship with their environment are discussed. And the important contributions they make to protein stability and solubility.
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Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy

TL;DR: Sequence analyses based on the results imply that foldable sequences with more compact unfolded states are a more recent result of protein evolution.
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Synonymous Codon Usage in Escherichia coli: Selection for Translational Accuracy

TL;DR: It is concluded that selection on synonymous codon use in E. coli is largely due to selection for translational accuracy, to reduce the costs of both missense and nonsense errors.
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Potential role of glutathione in evolution of thiol-based redox signaling sites in proteins.

TL;DR: A redox-active disulfide may be introduced into a protein structure by stepwise mutation of two residues in the native sequence to Cys, which is likely to be the cysteine of the CSD which undergoes nucleophilic attack by thioredoxin.
References
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Journal ArticleDOI

Adaptive protein evolution at the Adh locus in Drosophila

TL;DR: A simple statistical test of the neutral protein evolution hypothesis is proposed based on a comparison of the number of amino-acid replacement substitutions to synonymous substitutions in the coding region of a locus, finding that there are more fixed replacement differences between species than expected.
Journal ArticleDOI

Genome sequence of the Brown Norway rat yields insights into mammalian evolution

Richard A. Gibbs, +242 more
- 01 Apr 2004 - 
TL;DR: This first comprehensive analysis of the genome sequence of the Brown Norway (BN) rat strain is reported, which is the third complete mammalian genome to be deciphered, and three-way comparisons with the human and mouse genomes resolve details of mammalian evolution.

Genome sequence of the Brown Norway rat yields insights into mammalian evolutionRat Genome Sequencing Project ConsortiumNature200442849352115057822

Richard A. Gibbs, +226 more
Abstract: The laboratory rat (Rattus norvegicus) is an indispensable tool in experimental medicine and drug development, having made inestimable contributions to human health. We report here the genome sequence of the Brown Norway (BN) rat strain. The sequence represents a high-quality ‘draft’ covering over 90% of the genome. The BN rat sequence is the third complete mammalian genome to be deciphered, and three-way comparisons with the human and mouse genomes resolve details of mammalian evolution. This first comprehensive analysis includes genes and proteins and their relation to human disease, repeated sequences, comparative genome-wide studies of mammalian orthologous chromosomal regions and rearrangement breakpoints, reconstruction of ancestral karyotypes and the events leading to existing species, rates of variation, and lineage-specific and lineage-independent evolutionary events such as expansion of gene families, orthology relations and protein evolution.
Journal ArticleDOI

Sequencing and comparison of yeast species to identify genes and regulatory elements

TL;DR: A comparative analysis of the yeast Saccharomyces cerevisiae based on high-quality draft sequences of three related species, which inferred a putative function for most of these motifs, and provided insights into their combinatorial interactions.
Journal ArticleDOI

New Agrobacterium helper plasmids for gene transfer to plants

TL;DR: The construction of new helper Ti plasmids for Agrobacterium-mediated plant transformation using T-DNA regions deleted using site-directed mutagenesis to yield replicons carrying thevir genes that will complement binary vectorsin trans.
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