Extreme variations in the ratios of non-synonymous to synonymous nucleotide substitution rates in signal peptide evolution

Garcia Maroto, Federico and Castagnaro, Atilio and Sanchez de la Hoz, Pilar and Maraña, Carmen and Carbonero Zalduegui, Pilar and García Olmedo, Francisco (1991). Extreme variations in the ratios of non-synonymous to synonymous nucleotide substitution rates in signal peptide evolution. "Febs Letters", v. 287 (n. 1-2); pp. 67-70. ISSN 0014-5793. https://doi.org/10.1016/0014-5793(91)80017-W.

Description

Title: Extreme variations in the ratios of non-synonymous to synonymous nucleotide substitution rates in signal peptide evolution
Author/s:
  • Garcia Maroto, Federico
  • Castagnaro, Atilio
  • Sanchez de la Hoz, Pilar
  • Maraña, Carmen
  • Carbonero Zalduegui, Pilar
  • García Olmedo, Francisco
Item Type: Article
Título de Revista/Publicación: Febs Letters
Date: August 1991
ISSN: 0014-5793
Volume: 287
Subjects:
Freetext Keywords: α-Amylase/trypsin inhibitor; Thaumatin II; Thionin; Plastocyanin; Signal peptide evolution
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Nucleotide sequences encoding signal peptidcs from the precursors of α-amylase/trypsin inhibitors from cereals are homologous to those corresponding to the precursors of thaumatin II and of plastocyanins. Non-synonymous (KA) and synonymous (KS) rates of nucleotide substitutions have been calculated for all possible binary combinations. Extreme variation in KA/KS ratios has been observed, from the 0.167 average found within the plastocyanin family to an average of 1.90 calculated for the inhibitors/thaumatin II transition. A similar calculation has been carried out for the signal peptide sequences of thionins. which are unrelated to those of the α-amylase trypsin inhibitor family, and an average KA/KS of 0.12 has been obtained. This variation can be largely explained in terms of an empirical index of stability related to amino acid composition and seems to be independent of functional constraints.

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