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rdf:type |
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lifeskim:mentions |
umls-concept:C0035693,
umls-concept:C0043393,
umls-concept:C0073240,
umls-concept:C0376525,
umls-concept:C0521009,
umls-concept:C0596311,
umls-concept:C1330957,
umls-concept:C1514562,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1549781,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1710082,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
4
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pubmed:dateCreated |
2000-2-15
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pubmed:abstractText |
Yeast Rnt1 is a member of the double-stranded RNA (dsRNA)-specific RNase III family identified by conserved dsRNA binding (dsRBD) and nuclease domains. Comparative sequence analyses have revealed an additional N-terminal domain unique to the eukaryotic homologues of RNase III. The deletion of this domain from Rnt1 slowed growth and led to mild accumulation of unprocessed 25S pre-rRNA. In vitro, deletion of the N-terminal domain reduced the rate of RNA cleavage under physiological salt concentration. Size exclusion chromatography and cross-linking assays indicated that the N-terminal domain and the dsRBD self-interact to stabilize the Rnt1 homodimer. In addition, an interaction between the N-terminal domain and the dsRBD was identified by a two-hybrid assay. The results suggest that the eukaryotic N-terminal domain of Rnt1 ensures efficient dsRNA cleavage by mediating the assembly of optimum Rnt1-RNA ribonucleoprotein complex.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-10411134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-10432452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-10445882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-1694024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-1924358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-1989884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-2205842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-6091052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-6159890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-6754088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-7616961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-7628456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-7628457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-8493105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-8620530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-8635475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-8710510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-8743695,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-8821257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-8978031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-932008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9326493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9327565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9334335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9336844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9525640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9632264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9649442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9649443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9736623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9819388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9837720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9857205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9862984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10648595-9891049
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNT1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease III,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease III, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1104-15
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10648595-Base Sequence,
pubmed-meshheading:10648595-DNA Primers,
pubmed-meshheading:10648595-Dimerization,
pubmed-meshheading:10648595-Endoribonucleases,
pubmed-meshheading:10648595-Escherichia coli,
pubmed-meshheading:10648595-Escherichia coli Proteins,
pubmed-meshheading:10648595-Nucleic Acid Conformation,
pubmed-meshheading:10648595-RNA, Bacterial,
pubmed-meshheading:10648595-RNA, Double-Stranded,
pubmed-meshheading:10648595-RNA, Fungal,
pubmed-meshheading:10648595-Ribonuclease III,
pubmed-meshheading:10648595-Saccharomyces cerevisiae,
pubmed-meshheading:10648595-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10648595-Signal Transduction,
pubmed-meshheading:10648595-Two-Hybrid System Techniques
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pubmed:year |
2000
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pubmed:articleTitle |
The N-terminal domain that distinguishes yeast from bacterial RNase III contains a dimerization signal required for efficient double-stranded RNA cleavage.
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pubmed:affiliation |
Département de Microbiologie et d'Infectiologie, Faculté de Médecine, Université de Sherbrooke, Sherbrooke, Québec, Canada J1H 5N4.
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