Increased frequency of cysteine, tyrosine, and phenylalanine residues since the last universal ancestor.
Analysis of extant proteomes has the potential of revealing how amino acid frequencies within proteins have evolved over biological time. 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. This inference was derived from a comparison of amino acid frequencies within conserved and non-conserved residues of a set of proteins dating to the last universal ancestor in the face of empirical knowledge of the relative mutability of these amino acids. The under-representation of these amino acids within last universal ancestor proteins relative to their modern descendants suggests their late introduction into the genetic code. Thus, it appears that extant ancient proteins contain evidence pertaining to early events in the formation of biological systems.
Brooks
Dawn J
DJ
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
Fresco
Jacques R
JR
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D003545:Cysteine / Q000032:analysis; D030562:Databases, Protein; D019143:Evolution, Molecular; D005815:Genetic Code; D008957:Models, Genetic; D010649:Phenylalanine / Q000032:analysis; D020543:Proteome / Q000737:chemistry* / Q000235:genetics*; D013997:Time Factors; D014443:Tyrosine / Q000032:analysis
D020543:Proteome; D014443:Tyrosine; D010649:Phenylalanine; D003545:Cysteine