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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2001-12-13
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pubmed:databankReference |
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pubmed:abstractText |
Aquifex aeolicus Ribonuclease III (Aa-RNase III) belongs to the family of Mg(2+)-dependent endonucleases that show specificity for double-stranded RNA (dsRNA). RNase III is conserved in all known bacteria and eukaryotes and has 1-2 copies of a 9-residue consensus sequence, known as the RNase III signature motif. The bacterial RNase III proteins are the simplest, consisting of two domains: an N-terminal endonuclease domain, followed by a double-stranded RNA binding domain (dsRBD). The three-dimensional structure of the dsRBD in Escherichia coli RNase III has been elucidated; no structural information is available for the endonuclease domain of any RNase III.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1225-36
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pubmed:dateRevised |
2005-12-26
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pubmed:meshHeading |
pubmed-meshheading:11738048-Amino Acid Sequence,
pubmed-meshheading:11738048-Binding Sites,
pubmed-meshheading:11738048-Crystallography, X-Ray,
pubmed-meshheading:11738048-Dimerization,
pubmed-meshheading:11738048-Endoribonucleases,
pubmed-meshheading:11738048-Escherichia coli Proteins,
pubmed-meshheading:11738048-Ligands,
pubmed-meshheading:11738048-Manganese,
pubmed-meshheading:11738048-Models, Molecular,
pubmed-meshheading:11738048-Molecular Sequence Data,
pubmed-meshheading:11738048-Mutation,
pubmed-meshheading:11738048-Nucleic Acid Conformation,
pubmed-meshheading:11738048-Protein Binding,
pubmed-meshheading:11738048-Protein Conformation,
pubmed-meshheading:11738048-Protein Folding,
pubmed-meshheading:11738048-Protein Structure, Secondary,
pubmed-meshheading:11738048-Protein Structure, Tertiary,
pubmed-meshheading:11738048-RNA, Double-Stranded,
pubmed-meshheading:11738048-Ribonuclease III,
pubmed-meshheading:11738048-Sequence Homology, Amino Acid
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pubmed:year |
2001
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pubmed:articleTitle |
Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage.
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pubmed:affiliation |
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
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pubmed:publicationType |
Journal Article
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