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pubmed-article:9531475pubmed:abstractTextHuman proliferation-associated protein p120 has previously been shown to localize to the nucleolus, and several functional domains of p120 have been elucidated. By using a nitrocellulose filter binding assay and a Northwestern blotting procedure this study shows that recombinant p120 binds to an rRNA fragment in vitro with a dissociation constant of 4 nM. The specific RNA-binding region of p120 (residues 1-57) was identified with glutathione S-transferase-fused p120 deletion constructs and Northwestern blotting procedures. This RNA-binding region of p120, which includes the nucleolar localization signal of p120, is similar to the arginine-rich RNA-binding regions found in other RNA-binding proteins such as HIV Rev and Tat. Experiments in vivo with HeLa cell nucleolar extracts showed that p120 was associated with the 60-80S pre-ribosomal particles. This association is disrupted by treatment with either RNase A or buffer of high ionic strength. These results suggest that p120 might be involved in rRNA/ribosome maturation, consistent with the role of the yeast homologue Nop2p in rRNA biogenesis.lld:pubmed
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pubmed-article:9531475pubmed:articleTitleNucleolar protein p120 contains an arginine-rich domain that binds to ribosomal RNA.lld:pubmed
pubmed-article:9531475pubmed:affiliationDepartment of Pharmacology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030, USA.lld:pubmed
pubmed-article:9531475pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9531475pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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