[No authors listed]
The human U2BⳠprotein is one of the unique proteins that comprise the U2 snRNP, but it is also a representative of the U1A/U2BⳠprotein family. In the U2 snRNP, it is bound to Stem-Loop IV (SLIV) of the U2 snRNA. We find that in vitro it binds not only to human SLIV, but also to Stem-Loop II (SLII) from human U1 snRNA and to Drosophila U2 snRNA SLIV. The thermodynamics of these binding interactions show a striking similarity, leading to the conclusion that U2BⳠhas a relaxed specificity for its RNA targets. The binding properties of U2BⳠare distinct from those of human U1A and of Drosophila SNF, despite its high homology to those proteins, and so provide important new information on how this protein family has modulated its target preferences. Copyright © 2011 Elsevier B.V. All rights reserved.
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