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The NMR structure of the RNA binding domain of E.coli rho factor suggests possible RNA–protein interactions

Nature Structural Biology volume 5, pages 393–399 (1998)Cite this article

Abstract

Rho protein is an essential hexameric RNA–DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding domain of rho, rho130, is presented. This structure consists of two sub-domains, an N-terminal three-helix bundle and a C-terminal β-barrel that is structurally similar to the oligosaccharide/oligonucleotide binding (OB) fold. Chemical shift changes of rho130 upon RNA binding and previous mutagenetic analyses of intact rho suggest that residues Asp 60, Phe 62, Phe 64, and Arg 66 are critical for binding and support the hypothesis that ssRNA/ssDNA binding is localized in the β-barrel sub-domain. On the basis of these studies and the tertiary structure of rho130, we propose that residues Asp 60, Phe 62, Phe 64, Arg 66, Tyr 80, Lys 105, and Arg 109 participate in RNA-protein interactions.

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Authors and Affiliations

  1. Department of Biochemistry, University of Virginia School of Medicine, Charlottesville, Virginia, 22908, USA

    Deborah M. Briercheck, Todd C. Wood, Timothy J. Allison & Gordon S. Rule

  2. Department of Chemistry, Indiana University, Bloomington, Indiana, 47405, USA

    John P. Richardson

  3. Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Ave, Pittsburgh, Pennsylvania, 15213, USA

    Gordon S. Rule

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  1. Deborah M. Briercheck
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Briercheck, D., Wood, T., Allison, T. et al. The NMR structure of the RNA binding domain of E.coli rho factor suggests possible RNA–protein interactions. Nat Struct Mol Biol 5, 393–399 (1998). https://doi.org/10.1038/nsb0598-393

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