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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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Use of a multi-way method to analyze the amino acid composition of a conserved group of orthologous proteins in prokaryotes.

TL;DR: The Tucker3 model can be used to study the amino acid variability within and between species by taking into consideration the tridimensionality of the data set and it is found that the main factor behind the aminoacid composition of proteins is independent of the organism or protein function analyzed.
Journal ArticleDOI

Condensation Effects on Electron Chiral Asymmetries in the Photoionization of Serine: From Free Molecules to Nanoparticles

TL;DR: In this paper, angle-resolved valence photoelectron spectroscopy was used to investigate structural changes at the molecular level, occurring at the onset of condensation, which can be probed by angle-resolution valence spectrograms.
Journal ArticleDOI

Reconstruction and Characterization of Thermally Stable and Catalytically Active Proteins Comprising an Alphabet of 13 Amino Acids

TL;DR: Rec reconstructed three convergent sequences of an ancestral nucleoside diphosphate kinase, each comprising a 10 amino acid “alphabet,” and found that two of these variants folded into soluble and stable tertiary structures, providing experimental support for the idea that robust protein scaffolds can be built with a subset of the current 20 amino acids.
Journal ArticleDOI

Reduced alphabet of prebiotic amino acids optimally encodes the conformational space of diverse extant protein folds.

TL;DR: The results suggest that prebiotic sequences are amenable to mutations that significantly lower native conformational energies and increase discrimination amidst incorrect folds, and may have assisted the genesis of functional proto-enzymes prior to the expansion of the full amino acid alphabet.
Journal ArticleDOI

Fibrinogen function achieved through multiple covalent states.

TL;DR: It is demonstrated that fibrinogen exists and functions as multiple covalent forms and is required for a robustfibrin matrix that withstands the mechanical forces of flowing blood and resists premature fibrinolysis.
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.
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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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