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x * 108000, calculated from the deduced amino acid sequence for AtRTL3
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x * 33000, calculated from the deduced amino acid sequence for AtRTL1
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x * 25600, amino acid sequence calculation, x * 29000, recombinant His-tagged enzyme, SDS-PAGE
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x * 52000, recombinant GST-tagged RNase III, SDS-PAGE, x * 26000, recombinant detagged enzyme, SDS-PAGE
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Mycobacterium tuberculosis variant bovis Pasteur 1173P2
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x * 52000, recombinant GST-tagged RNase III, SDS-PAGE, x * 26000, recombinant detagged enzyme, SDS-PAGE
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dimer
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dimer
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2 * 45000, subunit mass calculated from the deduced amino acid sequence for AtRTL2, native mass by gel filtration, forms highly salt resistant dimers, dimer formation through disulfide bonds, dimers can be disrupted upon DTT treatment
dimer
2 * 17100, His-tagged monomer, calculated
dimer
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2 * 25000-25300, SDS-PAGE
dimer
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2 * 25600, wild-type enzyme, SDS-PAGE
dimer
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2 * 29000, about, recombinant His-tagged enzymes, SDS-PAGE
dimer
the active form of Escherichia coli RNase III consists of an endonuclease domain (EndoND) and a double stranded RNA binding domain (dsRBD) combined in a dimer of two 25 kDa polypeptides. The RNase III dsRBD exhibits an alphabetabetabetaalpha fold, which is a common form of eukaryotic proteins that recognize dsRNA. EndoND comprises seven alpha-helices and a 310 helix. It homodimerizes through hydrophobic interactions, creating a ball-and-socket junction and a large catalytic valley
dimer
recombinant RNase IIIb-dsRBD fragment, crystal structure analysis, and gel filtration data
dimer
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2 * 20000-25000, SDS-PAGE
dimer
the RNase IIIb + dsRBD construct exists as a symmetric homodimer, crystal structure analysis and gel filtration, dimer is catalytically active
dimer
Paramecium bursaria Chlorella virus-1
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2 * 31000, recombinant enzyme, intein tag is cleaved off
dimer
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2 * 55000, amino acid sequence calculation
dimer
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homology model of mRPN1, overview
heterodimer
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heterodimer
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preparation of artificial heterodimers of RNase III, which are providing new insight on the subunit and domain interactions involved in dsRNA recognition and cleavage
homodimer
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homodimer
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three-dimensional structural model of Bm-RNase III based on homology modeling, best model structure is generated using 1o0w template from protein database, overview
homodimer
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three-dimensional structural model of Bm-RNase III based on homology modeling, best model structure is generated using 1o0w template from protein database, overview
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homodimer
the RNase III polypeptide (~220 amino acids) consists of an N-terminal catalytic domain [RIIID, about 150 amino acids (aa)] and a C-terminal dsRNA-binding domain (dsRBD, about 65 aa) joined by a short (10 aa) flexible linker. The active form of the enzyme is a homodimer, with a functionally independent catalytic site in each subunit and two dsRBDs that assist in substrate binding
homodimer
the minimal Dicer of Giardia intestinalis contains the PAZ and tandem RNase III domains, pseudodimeric RNase III domain
homodimer
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the Drosha polypeptide possesses tandem RNase III domains and a C-terminal dsRBD. The RNase III domains form an intramolecular pseudodimer with two catalytic sites. The Drosha dsRBD structure shows an alpha1-alpha1 loop element with a dynamic, extended structure
monomer
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monomer
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biochemical experiments indicate that Drosha functions as a monomer, with its ribonuclease domains forming an internal dimer structure
additional information
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model of class I endonuclease domain dimer
additional information
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model of class III endonuclease domain dimer
additional information
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domain structures of isozymes DCL1-4 are all composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, only CL-1 shows a double dsRNA binding domain and DCL3 lacks the N-terminal domain. Comparison of class I-III enzymes, overview
additional information
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consisting only of the RNase III catalytic domain
additional information
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composed of an endonuclease domain (endoND) followed by a dsRNA-binding domain (dsRBD)
additional information
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model of class III endonuclease domain dimer
additional information
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domain structure: the enzyme is composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, comparison of class I-III enzymes, overview
additional information
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model of class III endonuclease domain dimer
additional information
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Dicer-2 contains C-terminal RNase III domains, that mediate RNA cleavage, and an N-terminal helicase motif
additional information
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the RNA binding and enzymatic domains of Drosha are located on its C-terminus, the N-terminus harbors a nuclear localization signal
additional information
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domain structures: the enzyme Drosha is composed of P-rich domain, two RNase III domains, and dsRNA binding domain. The enzyme Dicer-1 is composed of truncated helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, and enzyme Dicer-2 is composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain. Comparison of class I-III enzymes, overview
additional information
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model of class I endonuclease domain dimer
additional information
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the enzyme consists of a catalytic and a substrate binding domain
additional information
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the enzyme contains a conserved dsRNA-binding and a conserved catalytic domain
additional information
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the enzyme contains a dsRNA binding and a catalytic subdomain
additional information
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domain structure: the enzyme is composed of RNase III domain and dsRNA binding domain, comparison of class I-III enzymes, overview
additional information
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model of class III endonuclease domain dimer
additional information
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domain structure: the enzyme Dicer is composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, while enzyme Drosha is composed of P-rich domain, RS-rich domain, two RNase III domains, and dsRNA binding domain, comparison of class I-III enzymes, overview
additional information
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inability of the Drosha dsRBD to form a stable complex on its own with dsRNA. Dicer structure analysis, overview
additional information
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domain structure: the enzyme Dicer is composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, comparison of class I-III enzymes, overview
additional information
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deletion mutant RNT1DELTA2-198 also behaves as a dimer
additional information
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enzyme contains the conserved dsRNA binding and nuclease domains, the dsRBD self-interacts with the N-terminal domain to stabilize the enzyme homodimer
additional information
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domain structure: the enzyme is composed of N-terminal domain, RNase III domain and dsRNA binding domain, comparison of class I-III enzymes, overview
additional information
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the enzyme binds siRNA as a dimer