| Literature DB >> 16427005 |
Richard J Maraia1, Mark A Bayfield.
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.Entities:
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Year: 2006 PMID: 16427005 DOI: 10.1016/j.molcel.2006.01.004
Source DB: PubMed Journal: Mol Cell ISSN: 1097-2765 Impact factor: 17.970