The origin of trypsin: evidence for multiple gene duplications in trypsins.
The trypsin family of serine proteases is one of the most studied protein families, with a wealth of amino acid sequence information available in public databases. Since trypsin-like enzymes are widely distributed in living organisms in nature, likely evolutionary scenarios have been proposed. A novel methodology for Fourier transformation of biological sequences (FOTOBIS) is presented. The methodology is well suited for the identification of the size and extent of short repeats in protein sequences. In the present paper the trypsin family of enzymes is analyzed with FOTOBIS and strong evidence for tandem gene duplication is found. A likely evolutionary path for the development of present-day trypsins involved an intrinsic extensive tandem gene duplication of a small DNA fragment of 15-18 nucleotides, corresponding to five or six amino acids. This ancestral trypsin gene was subsequently duplicated, leading to the earliest version of a full-sized trypsin, from which the contemporary trypsins have developed.
Baptista
A M
AM
Instituto de Technologica Química e Biológica, R. da Quinta Grande 6, Apartado 127, P-2780 Oeiras, Portugal.
Jonson
P H
PH
Hough
E
E
Petersen
S B
SB
D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D005583:Fourier Analysis; D017353:Gene Deletion; D020440:Gene Duplication; D006801:Humans; D017354:Point Mutation; D011817:Rabbits; D020080:Tandem Repeat Sequences; D018911:Trinucleotide Repeats; D014357:Trypsin / Q000737:chemistry / Q000235:genetics*
D014357:Trypsin