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Functional analysis of peptide motif for RNA microhelix binding suggests new family of RNA‐binding domains
Author(s) -
de Pouplana Lluís Ribas,
Buechter Douglas,
Sardesai Niranjan Y.,
Schimmel Paul
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.18.5449
Subject(s) - biology , rna , rna binding protein , motif (music) , genetics , peptide , computational biology , evolutionary biology , biochemistry , gene , physics , acoustics
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.