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• W2156801770 abstract "The STAR family comprises ribonucleic acid (RNA)-binding proteins that play key roles in RNA-regulatory processes. RNA recognition is achieved by a KH domain with an additional α-helix (QUA2) that seems to extend the RNA-binding surface to six nucleotides for SF1 (Homo sapiens) and seven nucleotides for GLD-1 (Caenorhabditis elegans). To understand the structural basis of this probable difference in specificity, we determined the solution structure of GLD-1 KH-QUA2 with the complete consensus sequence identified in the tra-2 gene. Compared to SF1, the GLD-1 KH-QUA2 interface adopts a different conformation resulting indeed in an additional sequence-specific binding pocket for a uracil at the 5′end. The functional relevance of this binding pocket is emphasized by our bioinformatics analysis showing that GLD-1 binding sites with this 5′end uracil are more predictive for the functional response of the messenger RNAs to gld-1 knockout. We further reveal the importance of the KH-QUA2 interface in vitro and that its alteration in vivo affects the level of translational repression dependent on the sequence of the GLD-1 binding motif. In conclusion, we demonstrate that the QUA2 domain distinguishes GLD-1 from other members of the STAR family and contributes more generally to the modulation of RNA-binding affinity and specificity of KH domain containing proteins." @default.
• W2156801770 created "2016-06-24" @default.
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• W2156801770 date "2014-05-16" @default.
• W2156801770 modified "2023-10-12" @default.
• W2156801770 title "Structural and functional implications of the QUA2 domain on RNA recognition by GLD-1" @default.
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• W2156801770 doi "https://doi.org/10.1093/nar/gku445" @default.
• W2156801770 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4081071" @default.
• W2156801770 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24838563" @default.
• W2156801770 hasPublicationYear "2014" @default.
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