The C-terminal peptide of Aquifex aeolicus riboflavin synthase directs encapsulation of native and foreign guests by a cage-forming lumazine synthase.

The Journal of Biological Chemistry
Yusuke AzumaDonald Hilvert

Abstract

Encapsulation of specific enzymes in self-assembling protein cages is a hallmark of bacterial compartments that function as counterparts to eukaryotic organelles. The cage-forming enzyme lumazine synthase (LS) from Bacillus subtilis (BsLS), for example, encapsulates riboflavin synthase (BsRS), enabling channeling of lumazine from the site of its generation to the site of its conversion to vitamin B2 Elucidating the molecular mechanisms underlying the assembly of these supramolecular complexes could help inform new approaches for metabolic engineering, nanotechnology, and drug delivery. To that end, we investigated a thermostable LS from Aquifex aeolicus (AaLS) and found that it also forms cage complexes with the cognate riboflavin synthase (AaRS) when both proteins are co-produced in the cytosol of Escherichia coli A 12-amino acid-long peptide at the C terminus of AaRS serves as a specific localization sequence responsible for targeting the guest to the protein compartment. Sequence comparisons suggested that analogous peptide segments likely direct RS complexation by LS cages in other bacterial species. Covalent fusion of this peptide tag to heterologous guest molecules led to their internalization into AaLS assemblies both in...Continue Reading

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Citations

May 2, 2018·Chemical Society Reviews·Yusuke AzumaDonald Hilvert
Sep 14, 2017·Angewandte Chemie·Stephan Tetter, Donald Hilvert
Jul 28, 2020·Biotechnology Reports·Rudolf Ladenstein, Ekaterina Morgunova
Dec 20, 2017·Journal of the American Chemical Society·Yusuke AzumaDonald Hilvert
Jun 13, 2018·Bioconjugate Chemistry·Shuxin WangKenneth J Woycechowsky
May 24, 2019·Journal of the American Chemical Society·Thomas G W Edwardson, Donald Hilvert

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