| http://purl.uniprot.org/citations/16782053 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16782053 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16782053 | http://www.w3.org/2000/01/rdf-schema#comment | "Nuclear VCP/p97-like protein 2 (NVL2) is a member of the chaperone-like AAA-ATPase family with two conserved ATP-binding modules. Our previous studies have shown that NVL2 is localized to the nucleolus by interacting with ribosomal protein L5 and may participate in ribosome synthesis, a process involving various non-ribosomal factors including chaperones and RNA helicases. Here, we show that NVL2 is associated with pre-ribosomal particles in the nucleus. Moreover, we used yeast two-hybrid and co-immunoprecipitation assays to identify an NVL2-interacting protein that could yield insights into NVL2 function in ribosome biogenesis. We found that NVL2 interacts with DOB1, a DExD/H-box RNA helicase, whose yeast homologue functions in a late stage of the 60S subunit synthesis. DOB1 can interact with a second ATP-binding module mutant of NVL2, which shows a dominant negative effect on ribosome synthesis. In contrast, it cannot interact with a first ATP-binding module mutant, which does not show the dominant negative effect. When the dominant negative mutant of NVL2 was overexpressed in cells, DOB1 appeared to remain associated with nuclear pre-ribosomal particles. Such accumulation was not observed upon overexpression of wild-type NVL2 or a nondominant-negative mutant. Taken together, our results suggest that NVL2 might regulate the association/dissociation reaction of DOB1 with pre-ribosomal particles by acting as a molecular chaperone."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2006.06.017"xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2006.06.017"xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Hara Y."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Hara Y."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Tsuji A."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Tsuji A."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Tani K."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Tani K."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Tagaya M."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Tagaya M."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Nagahama M."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Nagahama M."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Yamazoe T."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/author | "Yamazoe T."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/pages | "1075-1082"xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/pages | "1075-1082"xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/title | "The AAA-ATPase NVL2 is a component of pre-ribosomal particles that interacts with the DExD/H-box RNA helicase DOB1."xsd:string |
| http://purl.uniprot.org/citations/16782053 | http://purl.uniprot.org/core/title | "The AAA-ATPase NVL2 is a component of pre-ribosomal particles that interacts with the DExD/H-box RNA helicase DOB1."xsd:string |