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Mouse Npm3 is located approximately 5 kb upstream of the Fgf8 gene in the same transcriptional orientation [ 20 21 ] . To determine if human NPM3 is similarly located and to identify genomic clones of NPM3, we analyzed FGF8-containing human genomic lambda clones [ 22 ] by Southern blotting using a mouse Npm3 cDNA probe.
NPM3 protein localizes to the nucleus
A nucleic acid binding domain in the C-terminus of nucleophosmin is also lacking in NPM3 and nucleoplasmin, but the known functions of nucleoplasmin in nucleosome assembly and sperm decondensation suggest that this protein, and possibly NPM3, can accomplish intermolecular reactions involving nucleic acids in other ways, perhaps by associating with other proteins that have this binding activity.
Previous analysis of Npm3 expression in mouse tissues also showed generally equal and strong expression in the tissues tested with especially strong expression in testis [ 21 ] . However, in the mouse, the brain, rather than the lung, displayed the lowest Npm3 RNA levels.
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.
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