This HTML5 document contains 18 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

PrefixNamespace IRI
n15http://hub.abes.fr/oup/periodical/nar/2007/volume_35/issue_4/
marcrelhttp://id.loc.gov/vocabulary/relators/
vivohttp://vivoweb.org/ontology/core#
dctermshttp://purl.org/dc/terms/
n6http://hub.abes.fr/oup/periodical/nar/2007/volume_35/issue_4/101093nargkm015/authorship/
n10http://hub.abes.fr/oup/periodical/nar/2007/volume_35/issue_4/101093nargkm015/m/
n2http://hub.abes.fr/oup/periodical/nar/2007/volume_35/issue_4/101093nargkm015/
bibohttp://purl.org/ontology/bibo/
n11http://hub.abes.fr/referentiel/ouparticlecategories/subject/
rdachttp://rdaregistry.info/Elements/c/
n8http://hub.abes.fr/oup/periodical/nar/2007/volume_35/issue_4/101093nargkm015/articletype/
hubhttp://hub.abes.fr/namespace/
n12http://hub.abes.fr/oup/periodical/nar/
rdfhttp://www.w3.org/1999/02/22-rdf-syntax-ns#
rdawhttp://rdaregistry.info/Elements/w/
n16http://hub.abes.fr/namespace/person/mail/50f7c3279e312f985fe25d40f1dd021a/
xsdhhttp://www.w3.org/2001/XMLSchema#
Subject Item
n2:w
rdf:type
bibo:Article rdac:C10001
dcterms:isPartOf
n15:w
dcterms:subject
n11:molecularbiology
dcterms:title
Caf1 regulates translocation of ribonucleotide reductase by releasing nucleoplasmic Spd1-Suc22 assembly
rdaw:P10072
n10:web n10:print
vivo:relatedBy
n6:2 n6:4 n6:1 n6:3
marcrel:aut
n2:arakiyasuhiro n2:takahashishinya n2:kontanikenji n16:9fbff1b39ad3c28dad271c3df57bc5b8
dcterms:abstract
Appropriate supply of deoxyribonucleotides by the ribonucleotide reductase (RNR) complex is essential for DNA replication and repair. One recent model for the RNR activation in Schizosaccharomyces pombe is translocation of the regulatory subunit Suc22 from the nucleoplasm to the cytoplasm. The RNR inhibitory protein Spd1, which retains Suc22 in the nucleoplasm, is rapidly degraded upon DNA-replication stress, resulting in release of Suc22 to form the active RNR complex in the cytoplasm. Here, we show that Caf1, a component of the Ccr4-Not complex, is responsible for resistance of the replication stress and control of the Suc22 translocation. Caf1 is required not only for the stress-induced translocation of Suc22 from nucleoplasm to cytoplasm but also for the degradation of nucleoplasmic Spd1. DNA-replication stress appears to allow Caf1 to interact with Suc22, resulting in release of the nucleoplasmic Spd1-Suc22 assembly. Taken together, these results suggest a novel function of Caf1 as a key regulator in the stress-induced RNR activation.
hub:articleType
n8:researcharticle
hub:isPartOfThisJournal
n12:w