期刊
STRUCTURE
卷 19, 期 7, 页码 999-1010出版社
CELL PRESS
DOI: 10.1016/j.str.2011.03.022
关键词
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资金
- NIH [GM37254, GM61518]
- Whitcome Fellowship
- Ruth L.Kirschtein National Research Service Award [GM007185]
dsRBDs often bind dsRNAs with some specificity, yet the basis for this is poorly understood. Rnt1p, the major RNase Ill in Saccharomyces cerevisiae, cleaves RNA substrates containing hairpins capped by A/uGNN tetraloops, using its dsRBD to recognize a conserved tetraloop fold. However, the identification of a Rnt1p substrate with an AAGU tetraloop raised the question of whether Rnt1p binds to this noncanonical substrate differently than to A/uGNN tetraloops. The solution structure of Rnt1p dsRBD bound to an AAGU-capped hairpin reveals that the tetraloop undergoes a structural rearrangement upon binding to Rnt1p dsRBD to adopt a backbone conformation that is essentially the same as the AGAA tetraloop, and indicates that a conserved recognition mode is used for all Rnt1p substrates. Comparison of free and RNA-bound Rnt1p dsRBD reveals that tetraloop-specific binding requires a conformational change in helix alpha 1. Our findings provide a unified model of binding site selection by this dsRBD.
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