| http://purl.uniprot.org/citations/16766689 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16766689 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16766689 | http://www.w3.org/2000/01/rdf-schema#comment | "Plastids contain tetradecameric Clp protease core complexes, with five ClpP Ser-type proteases, four nonproteolytic ClpR, and two associated ClpS proteins. Accumulation of total ClpPRS complex decreased twofold to threefold in an Arabidopsis thaliana T-DNA insertion mutant in CLPR2 designated clpr2-1. Differential stable isotope labeling of the ClpPRS complex with iTRAQ revealed a fivefold reduction in assembled ClpR2 accumulation and twofold to fivefold reductions in the other subunits. A ClpR2:(his)(6) fusion protein that incorporated into the chloroplast ClpPRS complex fully complemented clpr2-1. The reduced accumulation of the ClpPRS protease complex led to a pale-green phenotype with delayed shoot development, smaller chloroplasts, decreased thylakoid accumulation, and increased plastoglobule accumulation. Stromal ClpC1 and 2 were both recruited to the thylakoid surface in clpr2-1. The thylakoid membrane of clpr2-1 showed increased carotenoid content, partial inactivation of photosystem II, and upregulated thylakoid proteases and stromal chaperones, suggesting an imbalance in chloroplast protein homeostasis and a well-coordinated network of proteolysis and chaperone activities. Interestingly, a subpopulation of PsaF and several light-harvesting complex II proteins accumulated in the thylakoid with unprocessed chloroplast transit peptides. We conclude that ClpR2 cannot be functionally replaced by other ClpP/R homologues and that the ClpPRS complex is central to chloroplast biogenesis, thylakoid protein homeostasis, and plant development."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.org/dc/terms/identifier | "doi:10.1105/tpc.106.042861"xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.org/dc/terms/identifier | "doi:10.1105/tpc.106.042861"xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "Alonso J.M."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "Alonso J.M."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "Ecker J.R."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "Ecker J.R."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "Friso G."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "Friso G."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "Rudella A."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "Rudella A."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "van Wijk K.J."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/author | "van Wijk K.J."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/name | "Plant Cell"xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/name | "Plant Cell"xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/pages | "1704-1721"xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/pages | "1704-1721"xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/title | "Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenesis in Arabidopsis."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/title | "Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenesis in Arabidopsis."xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/volume | "18"xsd:string |
| http://purl.uniprot.org/citations/16766689 | http://purl.uniprot.org/core/volume | "18"xsd:string |