Maintenance of a Protein Structure in the Dynamic Evolution of TIMPs over 600 Million Years

Fabrizio Gianguzza, Salvatore Costa, Teresa Maggio, Aldo Nicosia, Marcello Tagliavia, Angela Cuttitta, Monica Salamone, Salvatore Mazzola

Risultato della ricerca: Articlepeer review

9 Citazioni (Scopus)

Abstract

Deciphering the events leading to protein evolution represents a challenge, especially for protein families showing complex evolutionary history. Among them, TIMPs represent an ancient eukaryotic protein family widely distributed in the animal kingdom. They are known to control the turnover of the extracellular matrix and are considered to arise early during metazoan evolution, arguably tuning essential features of tissue and epithelial organization. To probe the structure and molecular evolution of TIMPs within metazoans, we report the mining and structural characterization of a large data set of TIMPs over approximately 600 Myr. The TIMPs repertoire was explored starting from the Cnidaria phylum, coeval with the origins of connective tissue, to great apes and humans. Despite dramatic sequence differences compared with highest metazoans, the ancestral proteins displayed the canonical TIMP fold. Only small structural changes, represented by an α-helix located in the N-domain, have occurred over the evolution. Both the occurrence of such secondary structure elements and the relative solvent accessibility of the corresponding residues in the three-dimensional structures raises the possibility that these sites represent unconserved element prone to accept variations.
Lingua originaleEnglish
pagine (da-a)1056-1071
Numero di pagine16
RivistaGenome Biology and Evolution
Volume8
Stato di pubblicazionePublished - 2016

All Science Journal Classification (ASJC) codes

  • Ecology, Evolution, Behavior and Systematics
  • Genetics

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