| http://purl.uniprot.org/citations/16428324 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16428324 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16428324 | http://www.w3.org/2000/01/rdf-schema#comment | "Replication protein A (RPA) is a protein complex composed of three subunits known as RPA70, RPA32, and RPA14. Generally, only one version of each of the three RPA genes is present in animals and yeast (with the exception of the human RPA32 ortholog). In rice (Oryza sativa L.), however, two paralogs of RPA70 have been reported. We screened the rice genome for RPA subunit genes, and identified three OsRPA70 (OsRPA70a, OsRPA70b and OsRPA70c), three OsRPA32 (OsRPA32-1, OsRPA32-2 and OsRPA32-3), and one OsRPA14. Through two-hybrid assays and pull down analyses, we showed that OsRPA70a interacted preferentially with OsRPA32-2, OsRPA70b with OsRPA32-1, and OsRPA70c with OsRPA32-3. OsRPA14 interacted with all OsRPA32 paralogs. Thus, rice has three types of RPA complex: OsRPA70a-OsRPA32-2-OsRPA14 (type A), OsRPA70b-OsRPA32-1-OsRPA14 (type B), and OsRPA70c-OsRPA32-3-OsRPA14 (type C). Subcellular localization analysis suggested that the type-A RPA complex is required for chloroplast DNA metabolism, whereas types B and C function in nuclear DNA metabolism."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvj014"xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvj014"xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/author | "Ishibashi T."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/author | "Ishibashi T."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/author | "Kimura S."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/author | "Kimura S."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/author | "Sakaguchi K."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/author | "Sakaguchi K."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/pages | "99-104"xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/pages | "99-104"xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/title | "A higher plant has three different types of RPA heterotrimeric complex."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/title | "A higher plant has three different types of RPA heterotrimeric complex."xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/volume | "139"xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://purl.uniprot.org/core/volume | "139"xsd:string |
| http://purl.uniprot.org/citations/16428324 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16428324 |
| http://purl.uniprot.org/citations/16428324 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16428324 |
| http://purl.uniprot.org/citations/16428324 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16428324 |
| http://purl.uniprot.org/citations/16428324 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16428324 |