At a glance, all members of the NPM family exhibit conserved structural motifs a N-terminal core domain, an acidic domain and a nuclear localization signal, associated with a less conserved, disorganized C-terminus region (Fig. While this family is well characterized functionally, little is known about the evolution of these genes and proteins. NPM1 belongs to a histone chaperones family, the Nucleophosmin/nucleoplasmin (NPM) family, a group that comprises multiple major functional members (NPM1, NPM2, NPM3 and the invertebrate NPM-like), and can be found amongst all Metazoan. The dendrogram reveals a clustering of sequences by type, rather than by species, and identifies NPM2 and NPM3 as polyphyletic groups c Simplified representation of the phylogenetic relationship within the NPM family. In addition, NPM members harbor nuclear-localization signals (NLS), nucleolar-localization signal (NoLS), nuclear export signal (NES) and acidic clusters ( a). Finally, only NPM1 exhibits a C-terminal aromatic stretch require for its nucleolar localization. A basic domain implicated in nucleic acid binding is common to NPM1 and NPM2, but absent in NPM3. All proteins share a core, hydrophobic domain ( blue) responsible for oligomerization and chaperone activity, followed by an acidic domain required for ribonuclease activity. b Schematic structure of NPM proteins from human (not to scale). Ac Acidic domain, NES nuclear export signal, MB putative metal binding domain, NLS nucleus localization signal, NoLS Nucleolar localization signal. The two isoforms have different expression levels and localization. NPM1.1 and NPM1.3 are two splices variants resulting from the use of alternative codons. A Superposition of NPM1 genomic structure and protein features.
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