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Updated: Sep 23, 2026

Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution
Published on: January 16, 2017
The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA
Laurent Volpon1, Carine Lievre, Michael J Osborne
1Department of Biochemistry, McGill University, Montreal, Quebec, H3G 1Y6, Canada.
Abstract:
The structure of the recombinant Escherichia coli protein YbcJ, a representative of a conserved family of bacterial proteins (COG2501), was determined by nuclear magnetic resonance. The fold of YbcJ identified it as a member of the larger family of S4-like RNA binding domains. These domains bind to structured RNA, such as that found in tRNA, rRNA, and a pseudoknot of mRNA. The structure of YbcJ revealed a highly conserved patch of basic residues, comprising amino acids K26, K38, R55, K56, and K59, which likely participate in RNA binding.
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