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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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Occurrence of protein disulfide bonds in different domains of life: a comparison of proteins from the Protein Data Bank

TL;DR: Higher capacity for the SS bond formation and isomerization in Eukarya when compared with Archaea and Bacteria is emphasized, which could be explained by the need for additional protein stabilization in hyperthermophiles.
Journal ArticleDOI

Apparent Trends of Amino Acid Gain and Loss in Protein Evolution Due to Nearly Neutral Variation

TL;DR: It is shown that unequal patterns of gains and losses for particular pairs of amino acids are consistent with a simple neutral model at equilibrium amino acid frequencies, and these patterns are explainable by the nearly neutral model.
Journal ArticleDOI

Adsorption of Amino Acids (Ala, Cys, His, Met) on Zeolites: Fourier Transform Infrared and Raman Spectroscopy Investigations

TL;DR: The most important finding of this work is that the relative concentrations of each amino acid to alanine (X/Ala) are close to 1.00, an important result with regard to prebiotic chemistry because it could be a solution for the paradox.
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Photochirogenesis: Photochemical Models on the Origin of Biomolecular Homochirality

TL;DR: Recent studies on enantioselective photolysis of racemic amino acids by circularly polarized light and experiments on the asymmetric photochemical synthesis of amino acids from only one C and one N containing molecules by simulating interstellar environments are highlighted.
Journal ArticleDOI

Strategies of Bacterial Over Expression of Membrane Transporters Relevant in Human Health: The Successful Case of the Three Members of OCTN Subfamily

TL;DR: The strategy of dealing with related proteins revealed to be finally successful for over expressing all the three subfamily members of the OCTN subfamily, indicating that several factors play different critical roles in bacterial expression of the three proteins.
References
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Journal ArticleDOI

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TL;DR: The sensitivity of the commonly used progressive multiple sequence alignment method has been greatly improved and modifications are incorporated into a new program, CLUSTAL W, which is freely available.
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A Simple Sequentially Rejective Multiple Test Procedure

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Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana

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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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