Brian H Carrick, Sarah L Crittenden, MaryGrace Linsley, Stephany J Costa Dos Santos, Marvin Wickens, Judith Kimble
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引用次数: 0
Abstract
Like all canonical PUF proteins, Caenorhabditis elegans FBF-2 binds to specific RNAs via tripartite recognition motifs. Here, we report that an FBF-2 mutant protein that cannot bind to RNA is nonetheless biologically active and maintains stem cells. This unexpected result challenges the conventional wisdom that RBPs must bind to RNAs to achieve biological activity. Also unexpectedly, FBF-2 interactions with partner proteins can compensate for the loss of RNA binding. FBF-2 only loses biological activity when its RNA-binding and partner interactions are both defective. These findings highlight the complementary contributions of RNA-binding and protein partner interactions to the activity of an RNA-binding protein.
期刊介绍：
RNA is a monthly journal which provides rapid publication of significant original research in all areas of RNA structure and function in eukaryotic, prokaryotic, and viral systems. It covers a broad range of subjects in RNA research, including: structural analysis by biochemical or biophysical means; mRNA structure, function and biogenesis; alternative processing: cis-acting elements and trans-acting factors; ribosome structure and function; translational control; RNA catalysis; tRNA structure, function, biogenesis and identity; RNA editing; rRNA structure, function and biogenesis; RNA transport and localization; regulatory RNAs; large and small RNP structure, function and biogenesis; viral RNA metabolism; RNA stability and turnover; in vitro evolution; and RNA chemistry.
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