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

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Gonzalez, GM 
Durica-Mitic, S 
Hardwick, SW 
Moncrieffe, MC 
Resch, M 


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.



metabolism, amino sugars, endoribonucleases, phosphates, phosphotransferases, bacteria, enzymes, glucosamine, ribonucleases, rna, escherichia coli, crystal structure, dimers

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Nucleic Acids Research

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Oxford University Press
Wellcome Trust (094229/Z/10/Z)
Wellcome Trust (200873/Z/16/Z)
This work was supported by the Wellcome Trust [RG84381 to B.F.L]; and the Austrian Science Fund [P 26681-B22 and F4317 to B.G.]. GMG was supported by a Gates Cambridge Scholarship. Funding for open access charge: Wellcome Trust.