| http://purl.uniprot.org/citations/33404921 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33404921 | http://www.w3.org/2000/01/rdf-schema#comment | "DSS1 is a small protein, highly conserved across different species. As a member of the intrinsically disordered protein family, DSS1 interacts with different protein partners, thus forming complexes involved in diverse biological mechanisms: DNA repair, regulation of protein homeostasis, mRNA export, etc. Additionally, DSS1 has a novel intriguing role in the post-translational protein modification named DSSylation. Oxidatively damaged proteins are targeted for removal with DSS1 and then degraded by proteasome. Yet, DSS1 involvement in the maintenance of genome integrity through homologous recombination is the only function well studied in Arabidopsis research. The fact that animal DSS1 shows wide multifunctionality imposes a need to investigate the additional roles of two Arabidopsis thaliana DSS1 homologs. Having in mind the universality of various biological processes, we considered the possibility of plant DSS1 involvement in cellular homeostasis maintenance during stress exposure. Using real-time PCR and immunoblot analysis, we investigated the profiles of DSS1 gene and protein expression under oxidative stress. We grew and selected the homozygous Arabidopsis mutant line, carrying the T-DNA intron insertion in the DSS1(V) gene. The mutant line was phenotypically described during plant development, and its sensitivity to oxidative stress was characterized. This is the first report which indicates that plant DSS1 gene expression has an altered profile under the influence of oxidative stress. dss1(V)-/- plants showed an increased sensitivity to oxidative stress, germinated faster than WT, but generally showed developmental delay in further stages. Our results indicate that the DSS1 protein could be a crucial player in the molecular mechanisms underlying plant abiotic stress responses."xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.org/dc/terms/identifier | "doi:10.1007/s00709-020-01598-7"xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/author | "Samardzic J.T."xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/author | "Nesic S.B."xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/author | "Nikolic I.P."xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/author | "Timotijevic G.S."xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/name | "Protoplasma"xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/pages | "779-792"xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/title | "Intrinsically disordered protein AtDSS1(V) participates in plant defense response to oxidative stress."xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://purl.uniprot.org/core/volume | "258"xsd:string |
| http://purl.uniprot.org/citations/33404921 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/33404921 |
| http://purl.uniprot.org/citations/33404921 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/33404921 |
| http://purl.uniprot.org/uniprot/Q9FL96#attribution-7D8770BEFA09E32DF9F4D60E66E53B7E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/F4I886#attribution-7D8770BEFA09E32DF9F4D60E66E53B7E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/#_F4I886-mappedCitation-33404921 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/#_Q2PDG4-mappedCitation-33404921 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/#_Q2PDG5-mappedCitation-33404921 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/#_Q9FL96-mappedCitation-33404921 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/#_Q9XIR8-mappedCitation-33404921 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/F4I886 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/Q2PDG4 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/Q9FL96 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/33404921 |
| http://purl.uniprot.org/uniprot/Q2PDG5 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/33404921 |