The La protein-RNA complex surfaces
- PMID: 16427005
- DOI: 10.1016/j.molcel.2006.01.004
The La protein-RNA complex surfaces
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.
Comment on
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Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen.Mol Cell. 2006 Jan 6;21(1):75-85. doi: 10.1016/j.molcel.2005.10.027. Mol Cell. 2006. PMID: 16387655 Free PMC article.
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