Effect of metabolosome encapsulation peptides on enzyme activity, coaggregation, incorporation, and bacterial microcompartment formation

Rokas Juodeikis, Matthew J. Lee, Matthias Mayer, Judith Mantell, Ian R. Brown, Paul Verkade, Derek N. Woolfson, Michael B. Prentice, Stefanie Frank, Martin J. Warren

Research output: Contribution to journalArticle (Academic Journal)peer-review

5 Citations (Scopus)
47 Downloads (Pure)

Abstract

Metabolosomes, catabolic bacterial microcompartments (BMCs), are proteinaceous organelles that are associated with the breakdown of metabolites such as propanediol and ethanolamine. They are composed of an outer multicomponent protein shell that encases a specific metabolic pathway. Protein cargo found within BMCs is directed by the presence of an encapsulation peptide that appears to trigger aggregation before the formation of the outer shell. We investigated the effect of three distinct encapsulation peptides on foreign cargo in a recombinant BMC system. Our data demonstrate that these peptides cause variations in enzyme activity and protein aggregation. We observed that the level of protein aggregation generally correlates with the size of metabolosomes, while in the absence of cargo BMCs self‐assemble into smaller compartments. The results agree with a flexible model for BMC formation based around the ability of the BMC shell to associate with an aggregate formed due to the interaction of encapsulation peptides.
Original languageEnglish
Article numbere1010
Number of pages21
JournalMicrobiologyOpen
DOIs
Publication statusPublished - 13 Feb 2020

Structured keywords

  • Bristol BioDesign Institute

Keywords

  • bacterial organelles
  • cargo
  • protein aggregation
  • synthetic biology
  • targeting

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