ISSN:
1432-1432
Keywords:
Key words: Protein evolution — Trypsin — Tandem gene duplication — Fourier transform — Repeated segment
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract. 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/PL00006393
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