Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1998190 | Molecular Cell | 2006 | 4 Pages |
Abstract
A recent issue of Molecular Cell reported that the typical nucleic acid binding surfaces of the RRM and winged-helix motifs, although present in the RNA binding protein La, are not used to engage its best-characterized ligand, 3′ UUU-OH. Instead, La uses edgewise and backsides of these motifs for UUU-OH recognition, leaving open their typical surfaces for other potential interactions. These observations provide a framework for appreciating the various activities attributed to this ubiquitous nuclear phosphoprotein, which include its principal function, snRNA 3′ end protection, in addition to mRNA-related and RNA chaperone-like activities, as well as DNA and chromatin-associated activity.
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Authors
Richard J. Maraia, Mark A. Bayfield,