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Originally published In Press as doi:10.1074/mcp.M100001-MCP200 on November 13, 2001.
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Molecular & Cellular Proteomics 1:125-131, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

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

Dawn J. Brooks{ddagger} and Jacques R. Fresco§

From the Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544

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.

§ To whom correspondence should be addressed. Tel.: 609-258-3927; Fax: 609-258-2759; E-mail: jrfresco{at}princeton.edu.


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