scispace - formally typeset
Journal ArticleDOI

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

Reads0
Chats0
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.

read more

Content maybe subject to copyright    Report

Citations
More filters
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Journal ArticleDOI

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
More filters
Journal ArticleDOI

Leafy gall formation by Rhodococcus fascians.

TL;DR: Rhodococcus fascians infects a wide range of plants, initiating the formation of leafy galls that consist of centers of shoot amplification and shoot growth inhibition as discussed by the authors.
Journal ArticleDOI

Problems with parsimony in sequences of biased base composition

TL;DR: The analysis demonstrates that parsimony can be misleading even when levels of sequence divergence are as low as 10%; parsimony incorrectly infers an excess of common to rare changes.
Journal ArticleDOI

Increased Frequency of Cysteine, Tyrosine, and Phenylalanine Residues Since the Last Universal Ancestor

TL;DR: Evidence is presented here that cysteine, tyrosine, and phenylalanine residues have substantially increased in frequency since the three primary lineages diverged more than three billion years ago, suggesting their late introduction into the genetic code.
Journal ArticleDOI

Classification and nomenclature of Agrobacterium and Rhizobium – a reply to Farrand et al. (2003)

TL;DR: A critique of the proposal of Young et al. (2001) to revise the nomenclature and classification of Rhizobium and an attempt is made to unravel the confusion underpinning their discussion with a consideration of the relationship between formal and special-purpose nomenClatures.
Book ChapterDOI

Directional mutational pressure affects the amino acid composition and hydrophobicity of proteins in bacteria

TL;DR: The dnaA gene in bacteria was used as an example to show that the amino acid composition of a protein can be dramatically affected by mutational pressure, and that surprisingly, deleting relatively closely-related genera may increase rather than decrease the correlation between genomic GC content and amino Acid composition.
Related Papers (5)