Source: Bioinformatics
and Biology Insight
Scientists analyzed
protein secondary structures in relation to the statistics of three nucleotide
codon positions. The purpose of this investigation was to find which properties
of the ribosome, tRNA or protein level, could explain the purine bias (Rrr) as
it is observed in coding DNA. They found that the Rrr pattern is the
consequence of a regularity (the codon structure) resulting from
physicochemical constraints on proteins and thermodynamic constraints on
ribosomal machinery.
The physicochemical
constraints on proteins mainly come from the hydropathy and molecular weight
(MW) of secondary structures as well as the energy cost of amino acid
synthesis. These constraints appear through a network of statistical
correlations, such as (i) the cost of amino acid synthesis, which is in favor
of a higher level of guanine in the first codon position, (ii) the constructive
contribution of hydropathy alternation in proteins, (iii) the spatial
organization of secondary structure in proteins according to solvent
accessibility, (iv) the spatial organization of secondary structure according
to amino acid hydropathy, (v) the statistical correlation of MW with protein
secondary structures and their overall hydropathy, (vi) the statistical
correlation of thymine in the second codon position with hydropathy and the
energy cost of amino acid synthesis, and (vii) the statistical correlation of
adenine in the second codon position with amino acid complexity and the MW of
secondary protein structures Amino acid physicochemical properties and
functional constraints on proteins
Amino acid physicochemical properties and functional
constraints on proteins constitute a code that is translated into a purine bias
within the coding DNA via tRNAs. In that sense, the Rrr pattern within coding
DNA is the effect of information transfer on nucleotide composition from
protein to DNA by selection according to the codon positions. Thus, coding DNA
structure and ribosomal machinery co-evolved to minimize the energy cost of
protein coding given the functional constraints on proteins.
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