<i style="mso-bidi-font-style:normal">In silico</i> analysis of the NBS protein family in <i style="mso-bidi-font-style:normal">Ectocarpus siliculosus</i>

Abstract

Nucleotide-binding site (NBS) domain containing proteins belong to one of the most well characterized family of proteins; they are found in almost all higher eukaryotes. Extensive studies have been done on the plant NBS proteins, but similar studies on the brown algae NBS proteins are not available. In the present study, authors examined <span style="mso-fareast-font-family: Calibri" lang="EN-GB">the diversity of NBS proteins in model brown algae, <i style="mso-bidi-font-style:normal">Ectocarpus siliculosus</i>. A total of twenty six NBS proteins were identified and classified into different subfamilies based on their <span style="mso-fareast-font-family:Calibri" lang="EN-GB">distinct domain organizations. Although many characteristics of the protein family are similar to those of plant species, several features are quite distinct. One such characteristic is the presence of tetratrico peptide repeat (<span style="mso-fareast-font-family: Calibri" lang="EN-GB">TPR) motifs at the C-terminal ends of these proteins. Another interesting finding is the presence of two <i style="mso-bidi-font-style: normal">E. siliculosus</i> specific conserved motifs <span style="mso-fareast-font-family:Calibri" lang="EN-GB">leading to novel combination of the NBS domain. <span style="mso-fareast-font-family:Calibri" lang="EN-GB">The remarkable structural diversity found among these proteins further strengthens the idea that diversifying selection may have played an important role in their evolution.

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