Production and Characterization of Synthetic Carboxysome Shells with Incorporated Luminal Proteins

Plant Physiology
Fei CaiCheryl A Kerfeld

Abstract

Spatial segregation of metabolism, such as cellular-localized CO2 fixation in C4 plants or in the cyanobacterial carboxysome, enhances the activity of inefficient enzymes by selectively concentrating them with their substrates. The carboxysome and other bacterial microcompartments (BMCs) have drawn particular attention for bioengineering of nanoreactors because they are self-assembling proteinaceous organelles. All BMCs share an architecturally similar, selectively permeable shell that encapsulates enzymes. Fundamental to engineering carboxysomes and other BMCs for applications in plant synthetic biology and metabolic engineering is understanding the structural determinants of cargo packaging and shell permeability. Here we describe the expression of a synthetic operon in Escherichia coli that produces carboxysome shells. Protein domains native to the carboxysome core were used to encapsulate foreign cargo into the synthetic shells. These synthetic shells can be purified to homogeneity with or without luminal proteins. Our results not only further the understanding of protein-protein interactions governing carboxysome assembly, but also establish a platform to study shell permeability and the structural basis of the function of...Continue Reading

Citations

Jul 28, 2016·Applied Microbiology and Biotechnology·Maureen B QuinClaudia Schmidt-Dannert
Jun 9, 2016·Cold Spring Harbor Perspectives in Biology·Jessica K PolkaPamela A Silver
Jun 27, 2019·Biochemical Society Transactions·Sara Planamente, Stefanie Frank
Aug 22, 2017·Frontiers in Microbiology·Eric J YoungDaniel C Ducat
May 31, 2018·Scientific Reports·Christopher M JakobsonNiall M Mangan
Jun 21, 2018·Frontiers in Plant Science·Yi FangLu-Ning Liu
Oct 23, 2018·Nano Letters·Andrew R HagenCheryl A Kerfeld

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