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| The EMBO Journal
(1998) 17, 5449–5457, doi:10.1093/emboj/17.18.5449 |
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| Functional analysis of peptide motif for RNA microhelix binding suggests new family of RNA-binding domains |
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| Lluís Ribas de Pouplana1, Douglas Buechter2, Niranjan Y. Sardesai1 and Paul Schimmel1 |
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1 The Skaggs Institute for Chemical Biology and Departments of Molecular Biology and Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA 2 Present address: The US Surgical Corporation, 195 McDermott Road, North Haven, CT 06473, USA Received 5 June 1998; Revised 14 July 1998; Accepted 15 July 1998. |
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| Abstract |
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| RNA microhelices that recreate the acceptor stems of transfer RNAs are charged with specific amino acids. Here we identify a two-helix pair in alanyl-tRNA synthetase that is required for RNA microhelix binding. A single point mutation at an absolutely conserved residue in this motif selectively disrupts RNA binding without perturbation of the catalytic site. These results, and findings of similar motifs in the proximity of the active sites of other tRNA synthetases, suggest that two-helix pairs are widespread and provide a structural framework important for contacts with bound RNA substrates. |
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| Keywords: peptide motifs, photo-crosslinking, RNA–protein interactions |
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