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• W1948969711 endingPage "2657" @default.
• W1948969711 startingPage "2649" @default.
• W1948969711 abstract "B52, also known as SRp55, is a member of the Drosophila melanogaster SR protein family, a group of nuclear proteins that are both essential splicing factors and specific splicing regulators. Like most SR proteins, B52 contains two RNA recognition motifs in the N terminus and a C-terminal domain rich in serine-arginine dipeptide repeats. Since B52 is an essential protein and is expected to play a role in splicing a subset of Drosophila pre-mRNAs, its function is likely to be mediated by specific interactions with RNA. To investigate the RNA-binding specificity of B52, we isolated B52-binding RNAs by selection and amplification from a pool of random RNA sequences by using full-length B52 protein as the target. These RNAs contained a conserved consensus motif that constitutes the core of a secondary structural element predicted by energy minimization. Deletion and substitution mutations defined the B52-binding site on these RNAs as a hairpin loop structure covering about 20 nucleotides, which was confirmed by structure-specific enzymatic probing. Finally, we demonstrated that both RNA recognition motifs of B52 are required for RNA binding, while the RS domain is not involved in this interaction." @default.
• W1948969711 created "2016-06-24" @default.
• W1948969711 creator A5025845983 @default.
• W1948969711 creator A5041734871 @default.
• W1948969711 creator A5060183257 @default.
• W1948969711 date "1997-05-01" @default.
• W1948969711 modified "2023-09-26" @default.
• W1948969711 title "A specific RNA hairpin loop structure binds the RNA recognition motifs of the Drosophila SR protein B52" @default.
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• W1948969711 doi "https://doi.org/10.1128/mcb.17.5.2649" @default.
• W1948969711 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/232115" @default.
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• W1948969711 hasPublicationYear "1997" @default.
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