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http://purl.uniprot.org/citations/17189474http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17189474http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17189474http://www.w3.org/2000/01/rdf-schema#comment"Rcd-1, a protein highly conserved across eukaryotes, was initially identified as a factor essential for nitrogen starvation-invoked differentiation in fission yeast, and its Saccharomyces cerevisiae homolog, CAF40, has been identified as part of the CCR4-NOT transcription complex, where it interacts with the NOT1 protein. Mammalian homologs are involved in various cellular differentiation processes including retinoic acid-induced differentiation and hematopoetic cell development. Here, we present the 2.2 A X-ray structure of the highly conserved region of human Rcd-1 and investigate possible functional abilities of this and the full-length protein. The monomer is made up of six armadillo repeats forming a solvent-accessible, positively-charged cleft 21-22 A wide that, in contrast to other armadillo proteins, stays fully exposed in the dimer. Prompted by this finding, we established that Rcd-1 can bind to single- and double-stranded oligonucleotides in vitro with the affinity of G/C/T >> A. Mutation of an arginine residue within the cleft strongly reduced or abolished oligonucleotide binding. Rcd-1's ability to bind to nucleic acids, in addition to the previously reported protein-protein interaction with NOT1, suggests a new feature in Rcd-1's role in regulation of overall cellular differentiation processes."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.org/dc/terms/identifier"doi:10.1110/ps.062600507"xsd:string
http://purl.uniprot.org/citations/17189474http://purl.org/dc/terms/identifier"doi:10.1110/ps.062600507"xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/author"Pai E.F."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/author"Pai E.F."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/author"Gillon W."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/author"Gillon W."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/author"Garces R.G."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/author"Garces R.G."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/pages"176-188"xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/pages"176-188"xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/title"Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/title"Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties."xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/17189474http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/17189474http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17189474
http://purl.uniprot.org/citations/17189474http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17189474
http://purl.uniprot.org/citations/17189474http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17189474
http://purl.uniprot.org/citations/17189474http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17189474