Function

Protein Hfq (Hfq) (Host Factor for Qβ) or RNA-binding protein Hfq is stimulating base-pairing between sRNA and target mRNA by binding both RNAs via three RNA-binding surfaces. Hfq is found in enteric bacteria[1]. SAP binds in a calcium-dependent fashion to a variety of ligands.

Relevance

Since Hfq is required for gene regulation and infectivity of some Gram-negative bacteria its mutations can eliminate infectivity of Lyme disease caused by the bacteria Borellia burgdorferi, for example[2].

Structural highlights

shows the nucleotide phosphate group bridging two Ca+2 ions and forming hydrogen bonds to Asn, Gln and Try residues of SAP [3].


Structure of human pentameric SAP (green, grey, pink, yellow, magenta) complex with AMP and Ca+2 ions (green) (PDB code 4ht9)

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3D Structures of protein Hfq3D Structures of protein Hfq

Updated on 22-February-2021


ReferencesReferences

  1. Morita T, Aiba H. Mechanism and physiological significance of autoregulation of the Escherichia coli hfq gene. RNA. 2019 Feb;25(2):264-276. doi: 10.1261/rna.068106.118. Epub 2018 Nov 28. PMID:30487269 doi:http://dx.doi.org/10.1261/rna.068106.118
  2. Lybecker MC, Abel CA, Feig AL, Samuels DS. Identification and function of the RNA chaperone Hfq in the Lyme disease spirochete Borrelia burgdorferi. Mol Microbiol. 2010 Nov;78(3):622-35. doi: 10.1111/j.1365-2958.2010.07374.x. Epub, 2010 Sep 27. PMID:20815822 doi:http://dx.doi.org/10.1111/j.1365-2958.2010.07374.x
  3. Hohenester E, Hutchinson WL, Pepys MB, Wood SP. Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP. J Mol Biol. 1997 Jun 20;269(4):570-8. PMID:9217261 doi:10.1006/jmbi.1997.1075

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