PubMed:11565753 JSONTXT

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    PMID_GLOBAL

    {"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":215},"obj":"Sentence"},{"id":"T3","span":{"begin":216,"end":419},"obj":"Sentence"},{"id":"T4","span":{"begin":420,"end":649},"obj":"Sentence"},{"id":"T5","span":{"begin":650,"end":765},"obj":"Sentence"},{"id":"T6","span":{"begin":766,"end":980},"obj":"Sentence"},{"id":"T7","span":{"begin":981,"end":1180},"obj":"Sentence"},{"id":"T8","span":{"begin":1181,"end":1254},"obj":"Sentence"},{"id":"T9","span":{"begin":1255,"end":1401},"obj":"Sentence"}],"text":"Dbp9p, a putative ATP-dependent RNA helicase involved in 60S-ribosomal-subunit biogenesis, functionally interacts with Dbp6p.\nRibosome synthesis is a highly complex process and constitutes a major cellular activity. The biogenesis of this ribonucleoprotein assembly requires a multitude of protein trans-acting factors including several putative ATP-dependent RNA helicases of the DEAD-box and related protein families. Here we show that the previously uncharacterized Saccharomyces cerevisiae open reading frame YLR276C, hereafter named DBP9 (DEAD-box protein 9), encodes an essential nucleolar protein involved in 60S-ribosomal-subunit biogenesis. Genetic depletion of Dbp9p results in a deficit in 60S ribosomal subunits and the appearance of half-mer polysomes. This terminal phenotype is likely due to the instability of early pre-ribosomal particles, as evidenced by the low steady-state levels and the decreased synthesis of the 27S precursors to mature 25S and 5.8S rRNAs. In agreement with a role of Dbp9p in 60S subunit synthesis, we find that increased Dbp9p dosage efficiently suppresses certain dbp6 alleles and that dbp6/dbp9 double mutants show synthetic lethality. Furthermore, Dbp6p and Dbp9p weakly interact in a yeast two-hybrid assay. Altogether, our findings indicate an intimate functional interaction between Dbp6p and Dbp9p during the process of 60S-ribosomal-subunit assembly."}

    LocText

    {"project":"LocText","denotations":[{"id":"T1","span":{"begin":0,"end":5},"obj":"uniprot:Q06218"},{"id":"T2","span":{"begin":119,"end":124},"obj":"uniprot:P53734"},{"id":"T3","span":{"begin":469,"end":493},"obj":"taxonomy:4932"},{"id":"T4","span":{"begin":513,"end":520},"obj":"uniprot:Q06218"},{"id":"T5","span":{"begin":538,"end":542},"obj":"uniprot:Q06218"},{"id":"T6","span":{"begin":544,"end":562},"obj":"uniprot:Q06218"},{"id":"T7","span":{"begin":586,"end":595},"obj":"go:GO:0005730"},{"id":"T8","span":{"begin":671,"end":676},"obj":"uniprot:Q06218"},{"id":"T9","span":{"begin":1009,"end":1014},"obj":"uniprot:Q06218"},{"id":"T10","span":{"begin":1064,"end":1069},"obj":"uniprot:Q06218"},{"id":"T11","span":{"begin":1108,"end":1112},"obj":"uniprot:P53734"},{"id":"T12","span":{"begin":1130,"end":1134},"obj":"uniprot:P53734"},{"id":"T13","span":{"begin":1135,"end":1139},"obj":"uniprot:Q06218"},{"id":"T14","span":{"begin":1194,"end":1199},"obj":"uniprot:P53734"},{"id":"T15","span":{"begin":1204,"end":1209},"obj":"uniprot:Q06218"},{"id":"T16","span":{"begin":1231,"end":1236},"obj":"taxonomy:4932"},{"id":"T17","span":{"begin":1332,"end":1337},"obj":"uniprot:P53734"},{"id":"T18","span":{"begin":1342,"end":1347},"obj":"uniprot:Q06218"}],"relations":[{"id":"R1","pred":"localizeTo","subj":"T4","obj":"T7"},{"id":"R2","pred":"localizeTo","subj":"T5","obj":"T7"},{"id":"R3","pred":"localizeTo","subj":"T6","obj":"T7"},{"id":"R4","pred":"localizeTo","subj":"T8","obj":"T7"}],"namespaces":[{"prefix":"uniprot","uri":"http://identifiers.org/uniprot/"},{"prefix":"taxonomy","uri":"http://identifiers.org/taxonomy/"},{"prefix":"go","uri":"http://identifiers.org/go/"}],"text":"Dbp9p, a putative ATP-dependent RNA helicase involved in 60S-ribosomal-subunit biogenesis, functionally interacts with Dbp6p.\nRibosome synthesis is a highly complex process and constitutes a major cellular activity. The biogenesis of this ribonucleoprotein assembly requires a multitude of protein trans-acting factors including several putative ATP-dependent RNA helicases of the DEAD-box and related protein families. Here we show that the previously uncharacterized Saccharomyces cerevisiae open reading frame YLR276C, hereafter named DBP9 (DEAD-box protein 9), encodes an essential nucleolar protein involved in 60S-ribosomal-subunit biogenesis. Genetic depletion of Dbp9p results in a deficit in 60S ribosomal subunits and the appearance of half-mer polysomes. This terminal phenotype is likely due to the instability of early pre-ribosomal particles, as evidenced by the low steady-state levels and the decreased synthesis of the 27S precursors to mature 25S and 5.8S rRNAs. In agreement with a role of Dbp9p in 60S subunit synthesis, we find that increased Dbp9p dosage efficiently suppresses certain dbp6 alleles and that dbp6/dbp9 double mutants show synthetic lethality. Furthermore, Dbp6p and Dbp9p weakly interact in a yeast two-hybrid assay. Altogether, our findings indicate an intimate functional interaction between Dbp6p and Dbp9p during the process of 60S-ribosomal-subunit assembly."}