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Multimerization and DNA-binding activity of Insv Insv protein sequences required for DNA binding. DNA binding by the Elba BEN domain proteins, Elba1 and Elba2, requires a third protein, Elba3, to link them together [].In contrast, we found that Insv expressed by in vitro translation in rabbit reticulocyte lysates is able to bind CCAATTGG palindrome without the addition of any co-factors [].
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Based on the structure, we identified amino acids important for the TPR-BEN domain interaction, and for the functional interaction of the full-length proteins. Our data reveal a proposed new function for BEND3 in association with PICH, and the first example of a specific protein-protein interaction mediated by a BEN domain.
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We recently reported that Drosophila Insensitive (Insv) promotes sensory organ development and has activity as a nuclear corepressor for the Notch transcription factor Suppressor of Hairless [Su(H)]. Insv lacks domains of known biochemical function but contains a single BEN domain (i.e., a "BEN-solo.
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Enter the Function you want to domain into the editor. The domain calculator allows you to take a simple or complex function and find the domain in both interval and set notation instantly. Step 2: Click the blue arrow to submit and see the result! The domain calculator allows to find the domain of functions and expressions and receive results.
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Boundaries (insulators) in the Drosophila bithorax complex (BX-C) delimit autonomous regulatory domains that orchestrate the parasegment (PS)-specific expression of the BX-C homeotic genes.
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We recently reported that Drosophila Insensitive (Insv) promotes sensory organ development and has activity as a nuclear corepressor for the Notch transcription factor Suppressor of Hairless [Su(H)]. Insv lacks domains of known biochemical function but contains a single BEN domain (i.e., a "BEN-solo" protein). Our chromatin immunoprecipitation (ChIP) sequencing (ChIP-seq) analysis.
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To find the domain of a function, consider any restrictions on the input values that would make the function undefined, including dividing by zero, taking the square root of a negative number, or taking the logarithm of a negative number. Remove these values from the set of all possible input values to find the domain of the function.
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Contextual analysis suggests that the BEN domain mediates protein-DNA and protein-protein interactions during chromatin organization and transcription. The presence of BEN domains in a poxviral early virosomal protein and in polydnaviral proteins also suggests a possible role for them in organization of viral DNA during replication or.
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Importantly, despite many hints that mammalian BEN domains access DNA, little is known about their underlying structural features that permit sequence-specific recognition. In this study, we demonstrate direct sequence-specific binding activities of mammalian BEN proteins NACC1, NACC2, and BEND3. We reveal overlapping site preferences of the.
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The Fab-7 boundary. (A) Map of the Abd-B region of the bithorax complex. The relative location of the Abd-B regulatory domains—iab-5, iab-6, iab-7, and iab-8—and the segments that they specify in the adult male fly are indicated in the panel.Also shown are the positions of the boundary elements—Mcp, Fab-6, Fab-7, and Fab-8—and the Abd-B transcription unit.
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We report a previously uncharacterized α-helical module, the BEN domain, in diverse animal proteins such as BANP/SMAR1, NAC1 and the Drosophila mod (mdg4) isoform C, in the chordopoxvirus virosomal protein E5R and in several proteins of polydnaviruses. Contextual analysis suggests that the BEN domain mediates protein-DNA and protein-protein.
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The structural deorphanization of LIN-14 as a BEN domain-containing protein provides new vistas on both LIN-14 protein function as well as BEN domain proteins in general. Since many BEN domain proteins are involved in controlling chromatin architecture, it is conceivable that, in addition to transcriptional regulation, LIN-14 may also play a.
