http://purl.uniprot.org/citations/15840649 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15840649 | http://www.w3.org/2000/01/rdf-schema#comment | "53BP1 protein is re-localized to the sites of DNA damage after ionizing radiation (IR) and is involved in DNA-damage-checkpoint signal transduction. We examined the dynamics of GFP-53BP1 in living cells. The protein starts to accumulate at the sites of DNA damage 2-3 minutes after damage induction. Fluorescence recovery after photobleaching experiments showed that GFP-53BP1 is highly mobile in non-irradiated cells. Upon binding to the IR-induced nuclear foci, the mobility of 53BP1 reduces greatly. The minimum (M) domain of 53BP1 essential for targeting to IR induced foci consists of residues 1220-1703. GFP-M protein forms foci in mouse embryonic fibroblast cells lacking functional endogenous 53BP1. The M domain contains a tandem repeat of Tudor motifs and an arginine- and glycine-rich domain (RG stretch), which are often found in proteins involved in RNA metabolism, the former being essential for targeting. RNase A treatment dissociates 53BP1 from IR-induced foci. In HeLa cells, dissociation of the M domain without the RG stretch by RNase A treatment can be restored by re-addition of nuclear RNA in the early stages of post-irradiation. 53BP1 immunoprecipitates contain some RNA molecules. Our results suggest a possible involvement of RNA in the binding of 53BP1 to chromatin damaged by IR."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.02336"xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/author | "Adachi Y."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/author | "Melton D.W."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/author | "Robertson K."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/author | "Khalili S."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/author | "Selfridge J."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/author | "Ritchie A.M."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/author | "Jullien D."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/author | "Pryde F."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/name | "J Cell Sci"xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/pages | "2043-2055"xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/title | "53BP1 exchanges slowly at the sites of DNA damage and appears to require RNA for its association with chromatin."xsd:string |
http://purl.uniprot.org/citations/15840649 | http://purl.uniprot.org/core/volume | "118"xsd:string |
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