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These two residues can comprise more than 25% of the total amino acids in some proteins of this family; in NPM3 they make up approximately 18% of the residues.
An amino acid comparison of NPM3 with these other members of the nucleophosmin/nucleoplasmin family from various metazoans reveals extensive sequence identities and similarities throughout all of NPM3 except the C-terminal 16 residues (Figure 3).
The relationship between N1/N2 and NASP can be seen in this dendrogram and appears similar in closeness to that of NPM3 and NO29.
Supporting this notion, the in vitro transcription/translation of a plasmid encoding the closely related NO29 protein produces a product, presumably unmodified, with slow mobility that is similar to the mobility of NO29 extracted from cells [ 43 ] . The smaller-sized polypeptide of the NPM3 doublet is probably a degradation product, as is observed in analyses of the NO29 protein [ 43 ] . This subcellular localization of NPM3, together with the other results here, suggests that this protein is a molecular chaperone with functions in the nucleus.
Isolation of NPM3genomic probes