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Journal ArticleDOI

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

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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Presence of tRNA-dependent pathways correlates with high cysteine content in methanogenic Archaea

TL;DR: These findings suggest that cysteine plays an important role in early forms of life and that methanogenic Archaea generates special Cysteine clusters associated with primitive metabolic reactions.
Journal ArticleDOI

A Universal Trend among Proteomes Indicates an Oily Last Common Ancestor

TL;DR: Data is presented that indicates a steady decline (oil escape) in proteome hydrophobicity over species evolvedness evident in 272 diverse proteomes, which indicates a highly hydrophobic (oily) last common ancestor (LCA).
Journal ArticleDOI

Proteome-wide prediction of novel DNA/RNA-binding proteins using amino acid composition and periodicity in the hyperthermophilic archaeon Pyrococcus furiosus

TL;DR: Using the hyperthermophilic archaeon Pyrococcus furiosus as a model species, the support vector machine (SVM) method was used to discriminate DNA/RNA-binding proteins from proteins with other functions, using amino acid composition and periodicities as feature vectors.
Journal ArticleDOI

Genome-Wide Survey of Natural Selection on Functional, Structural, and Network Properties of Polymorphic Sites in Saccharomyces paradoxus

TL;DR: It is found that selection pressures previously detected over long evolutionary timescales have also shaped the evolution of S. paradoxus, presenting the first global survey of selection acting on various functional properties in this yeast.
Journal ArticleDOI

Validation of Molecular Dynamics Simulations for Prediction of Three-Dimensional Structures of Small Proteins

TL;DR: It is suggested that normal MD simulations can roughly predict short protein structures and 200-ns simulations are frequently sufficient for estimating the secondary structures of protein (approximately 20 residues).
References
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Journal ArticleDOI

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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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