| http://purl.uniprot.org/citations/11939789 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11939789 | http://www.w3.org/2000/01/rdf-schema#comment | "P58(IPK) was discovered as an inhibitor of the interferon-induced, protein kinase, PKR. Upon virus infection, PKR can, as part of the host defense system, inhibit mRNA translation by phosphorylating the alpha subunit of protein synthesis eukaryotic initiation factor 2 (eIF-2alpha). We previously found that influenza virus recruits the cellular P58(IPK) co-chaperone to inhibit PKR activity and thus facilitate viral protein synthesis. P58(IPK) contains nine tetratricopeptide repeat (TPR) motifs in addition to the highly conserved J domain found in all DnaJ chaperone family members. To define the role of molecular chaperones in regulating cell growth in addition to PKR regulation, we performed a detailed analysis of the P58(IPK) J domain. Using growth rescue assays, we found that the P58(IPK) J domain substituted for the J domains of other DnaJ proteins, including DnaJ in Escherichia coli and Ydj1 in Saccharomyces cerevisiae. This is the first time a cellular J domain from a mammalian DnaJ family member was shown to be functional in both prokaryotic DnaJ and eukaryotic Ydj1 constructs. Furthermore, point mutations within the conserved HPD residue cluster of the P58(IPK) J domain disrupted P58(IPK) J function including stimulation of ATPase activity of Hsp70. However, the P58(IPK) HPD mutants still inhibited PKR activity and thus supported cell growth in a yeast rescue assay. Overexpression of the HPD mutants of P58(IPK), similar to their wild-type counterpart, also stimulated mRNA translation in a mammalian cell system. Taken together, our data necessitate a model of P58(IPK) inhibition of PKR kinase activity and stimulation of mRNA translation, which does not require classical J domain function found in the DnaJ molecular chaperone family."xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi0121499"xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/author | "Katze M.G."xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/author | "Tan S.L."xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/author | "Yan W."xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/author | "Gale M.J. Jr."xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/pages | "4938-4945"xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/title | "Inactivation of the PKR protein kinase and stimulation of mRNA translation by the cellular co-chaperone P58(IPK) does not require J domain function."xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://purl.uniprot.org/core/volume | "41"xsd:string |
| http://purl.uniprot.org/citations/11939789 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11939789 |
| http://purl.uniprot.org/citations/11939789 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11939789 |
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| http://purl.uniprot.org/uniprot/#_P19525-mappedCitation-11939789 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11939789 |
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| http://purl.uniprot.org/uniprot/Q13217 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11939789 |
| http://purl.uniprot.org/uniprot/P19525 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11939789 |