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Structural basis for recognition of AU-rich element RNA by the HuD protein
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Structural basis for recognition of AU-rich element RNA by the HuD protein
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Structural basis for recognition of AU-rich element RNA by the HuD protein
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Journal Article
Structural basis for recognition of AU-rich element RNA by the HuD protein
2001
Overview
Hu proteins bind to adenosine-uridine (AU)-rich elements (AREs) in the 3′ untranslated regions of many short-lived mRNAs, thereby stabilizing them. Here we report the crystal structures of the first two RNA recognition motif (RRM) domains of the HuD protein in complex with an 11-nucleotide fragment of a class I ARE (the c-fos ARE; to 1.8 Å), and with an 11-nucleotide fragment of a class II ARE (the tumor necrosis factor α ARE; to 2.3 Å). These structures reveal a consensus RNA recognition sequence that suggests a preference for pyrimidine-rich sequences and a requirement for a central uracil residue in the clustered AUUUA repeats found in class II AREs. Comparison to structures of other RRM domain–nucleic acid complexes reveals two base recognition pockets in all the structures that interact with bases using residues in conserved ribonucleoprotein motifs and at the C-terminal ends of RRM domains. Different conformations of nucleic acid can be bound by RRM domains by using different combinations of base recognition pockets and multiple RRM domains.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Biomedical and Life Sciences
/ Consensus Sequence - genetics
/ Humans
/ letter
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - genetics
/ Nerve Tissue Proteins - metabolism
/ Proto-Oncogene Proteins c-fos - metabolism
/ Response Elements - genetics
/ RNA-Binding Proteins - chemistry
/ RNA-Binding Proteins - genetics
