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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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A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank.

TL;DR: An evolutionary model with sites evolving independently under a global constraint on the conservation of structural stability is introduced and the effective selection process reproduces well amino acid distributions as observed in the protein sequences in the PDB.
Journal ArticleDOI

Protein evolution: causes of trends in amino-acid gain and loss.

TL;DR: Evidence is provided that the patterns observed conform with standard, nearly neutral theoretical expectations and require no new explanation, which reinforces the need for caution in the interpretation of results derived from closely related taxa.
Journal ArticleDOI

Extended HP model for protein structure prediction.

TL;DR: This paper has experimentally shown that it is necessary to further improve the existing HPNX model and proposed a novel hHPNX model, which outperformed other models and preferred 3D face-centered-cube lattice configuration to have closest resemblance to the real folded 3D protein.
Journal ArticleDOI

Evolutionary patterns in the sequence and structure of transfer RNA: early origins of archaea and viruses.

TL;DR: Constrained analyses showed that the origin of viruses was not only ancient, but was linked to Archaea, supporting the notion that the archaeal lineage was very ancient, resulted in the first organismal divide, and predated diversification of tRNA function and specificity.
Journal ArticleDOI

Hybridization Probe for Femtomolar Quantification of Selected Nucleic Acid Sequences on a Disposable Electrode

TL;DR: Electroactive hybridization probes on gold surfaces of a disposable electrode were investigated as a technology for simple, sensitive, selective, and rapid gene identification, and target oligonucleotides could be distinguished from competing nontarget sequences based on unique "melting" profiles from the probe.
References
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A genomic perspective on protein families

TL;DR: Comparison of proteins encoded in seven complete genomes from five major phylogenetic lineages and elucidation of consistent patterns of sequence similarities allowed the delineation of 720 clusters of orthologous groups (COGs), which comprise a framework for functional and evolutionary genome analysis.
Journal ArticleDOI

Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA.

TL;DR: A large number of morphologically normal, fertile, transgenic rice plants were obtained by co-cultivation of rice tissues with Agrobacterium tumefaciens, and sequence analysis revealed that the boundaries of the T-DNA in transgenic Rice plants were essentially identical to those intransgenic dicotyledons.
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