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p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families

Abstract : We identified families of proteins characterized by the presence of a domain similar to human p23 protein, which include proteins such as Sgt1, involved in the yeast kinetochore assembly; melusin, involved in specific interactions with the cytoplasmic integrin beta1 domain; Rar1, related to pathogenic resistance in plants, and to development in animals; B5+B5R flavo-hemo cytochrome NAD(P)H oxidoreductase type B in humans and mice; and NudC, involved in nucleus migration during mitosis. We also found that p23 and the HSP20/alpha-crystallin family of heat shock proteins, which share the same three-dimensional folding, show a pattern of conserved residues that points to a common origin in the evolution of both protein domains. The p23 and HSP20/a-crystallin phylogenetic relationship and their similar role in chaperone activity suggest a common function, probably involving protein-protein interaction, for those proteins containing p23-like domains.
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https://hal.inrae.fr/hal-02683416
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Submitted on : Monday, June 1, 2020 - 3:13:51 AM
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Ja Garcia-Ranea, Gladys Mirey, Jacques Camonis, Alfonso Valencia. p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families. FEBS Letters, Wiley, 2002, 529 (2-3), pp.162-167. ⟨10.1038/ncb728⟩. ⟨hal-02683416⟩

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