| http://purl.uniprot.org/citations/32744327 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32744327 | http://www.w3.org/2000/01/rdf-schema#comment | "Cytosolic 80S ribosomes contain proteins of the mature cytosolic ribosome (r-proteins) as well as proteins with roles in ribosome biogenesis, protein folding or modification. Here, we refined the core r-protein composition in Arabidopsis thaliana by determining the abundance of different proteins during enrichment of ribosomes from cell cultures using peptide mass spectrometry. The turnover rates of 26 40S subunit r-proteins and 29 60S subunit r-proteins were also determined, showing that half of the ribosome population is replaced every 3-4 days. Three enriched proteins showed significantly shorter half-lives; a protein annotated as a ribosomal protein uL10 (RPP0D, At1g25260) with a half-life of 0.5 days and RACK1b and c with half-lives of 1-1.4 days. The At1g25260 protein is a homologue of the human Mrt4 protein, a trans-acting factor in the assembly of the pre-60S particle, while RACK1 has known regulatory roles in cell function beyond its role in the 40S subunit. Our experiments also identified 58 proteins that are not from r-protein families but co-purify with ribosomes and co-express with r-proteins; 26 were enriched more than 10-fold during ribosome enrichment. Some of these enriched proteins have known roles in translation, while others are newly proposed ribosome-associated factors in plants. This analysis provides an improved understanding of A. thaliana ribosome protein content, shows that most r-proteins turnover in unison in vivo, identifies a novel set of potential plant translatome components, and how protein turnover can help identify r-proteins involved in ribosome biogenesis or regulation in plants."xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.org/dc/terms/identifier | "doi:10.1042/bcj20200385"xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/author | "Li L."xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/author | "Millar A.H."xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/author | "Duncan O."xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/author | "Trosch J."xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/author | "Salih K.J."xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/pages | "3019-3032"xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/title | "The composition and turnover of the Arabidopsis thaliana 80S cytosolic ribosome."xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://purl.uniprot.org/core/volume | "477"xsd:string |
| http://purl.uniprot.org/citations/32744327 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/32744327 |
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