| http://purl.uniprot.org/citations/17963727 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17963727 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17963727 | http://www.w3.org/2000/01/rdf-schema#comment | "Bacterial cold shock proteins (CSPs) are RNA chaperones that unwind RNA secondary structures. Arabidopsis COLD SHOCK DOMAIN PROTEIN2 (AtCSP2) contains a domain that is shared with bacterial CSPs. Here we showed that AtCSP2 binds to RNA and unwinds nucleic acid duplex. Heterologous expression of AtCSP2 complemented cold sensitivity of an Escherichia coli csp quadruple mutant, indicating that AtCSP2 function as a RNA chaperone in E. coli. AtCSP2 mRNA and protein levels increased during cold acclimation, but the protein accumulation was most prominent after 10 days of cold treatment. AtCSP2 promoter::GUS transgenic plants revealed that AtCSP2 is expressed only in root and shoot apical regions during vegetative growth but is expressed in reproductive organs such as pollens, ovules and embryos. These data indicated that AtCSP2 is involved in developmental processes as well as cold adaptation. Localization of AtCSP2::GFP in nucleolus and cytoplasm suggested different nuclear and cytosolic RNA targets."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2007.10.059"xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2007.10.059"xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/author | "Sasaki K."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/author | "Sasaki K."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/author | "Imai R."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/author | "Imai R."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/author | "Kim M.-H."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/author | "Kim M.-H."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/pages | "633-638"xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/pages | "633-638"xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/title | "Arabidopsis COLD SHOCK DOMAIN PROTEIN2 is a RNA chaperone that is regulated by cold and developmental signals."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/title | "Arabidopsis COLD SHOCK DOMAIN PROTEIN2 is a RNA chaperone that is regulated by cold and developmental signals."xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/volume | "364"xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://purl.uniprot.org/core/volume | "364"xsd:string |
| http://purl.uniprot.org/citations/17963727 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17963727 |
| http://purl.uniprot.org/citations/17963727 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17963727 |
| http://purl.uniprot.org/citations/17963727 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17963727 |
| http://purl.uniprot.org/citations/17963727 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17963727 |