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Submitted on August 1, 2001
Revised on November 12, 2001
Accepted on November 13, 2001

Increased frequency of cysteine, tyrosine and phenylalanine residues since the last universal ancestor

Dawn J. Brooks and Jacques R. Fresco

Princeton University, Princeton, NJ 08540

Corresponding Author: jrfresco{at}princeton.edu

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 sequence positions 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.


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