Structural insights into RapZ-mediated regulation of bacterial amino-sugar metabolism.

In phylogenetically diverse bacteria, the conserved protein RapZ plays a central role in RNA-mediated regulation of amino-sugar metabolism. RapZ contributes to the control of glucosamine phosphate biogenesis by selectively presenting the regulatory small RNA GlmZ to the essential ribonuclease RNase E for inactivation. Here, we report the crystal structures of full length Escherichia coli RapZ at 3.40 Å and 3.25 Å, and its isolated C-terminal domain at 1.17 Å resolution. The structural data confirm that the N-terminal domain of RapZ possesses a kinase fold, whereas the C-terminal domain bears closest homology to a subdomain of 6-phosphofructokinase, an important enzyme in the glycolytic pathway. RapZ self-associates into a domain swapped dimer of dimers, and in vivo data support the importance of quaternary structure in RNA-mediated regulation of target gene expression. Based on biochemical, structural and genetic data, we suggest a mechanism for binding and presentation by RapZ of GlmZ and the closely related decoy sRNA, GlmY. We discuss a scenario for the molecular evolution of RapZ through re-purpose of enzyme components from central metabolism. © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

Citation

Grecia M Gonzalez, Svetlana Durica-Mitic, Steven W Hardwick, Martin C Moncrieffe, Marcus Resch, Piotr Neumann, Ralf Ficner, Boris Görke, Ben F Luisi. Structural insights into RapZ-mediated regulation of bacterial amino-sugar metabolism. Nucleic acids research. 2017 Oct 13;45(18):10845-10860

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PMID: 28977623

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