| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5371397 | Biophysical Chemistry | 2011 | 8 Pages |
The human U2Bâ³ protein is one of the unique proteins that comprise the U2 snRNP, but it is also a representative of the U1A/U2Bâ³ protein 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 U2Bâ³ has a relaxed specificity for its RNA targets. The binding properties of U2Bâ³ are 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.
Graphical abstractDownload full-size imageResearch highlights⺠snRNP protein U2BⳠbinds hairpins from U2 and U1 snRNA. ⺠RNA stemloop IV has evolved to inhibit U1A protein binding. ⺠The observed heat capacity could be due to conformational changes coupled to binding.
