S45: Protein nano-compartments for synthetic biology

Monday, August 12, 2013: 1:30 PM
Nautilus 1-2 (Sheraton San Diego)
Mark Held, Maureen B. Quin, Emily Schmidt and Claudia Schmidt-Dannert, Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN
Bacterial microcompartments (BMC) are intracellular protein shells which are formed in a wide range of prokaryotic lineages.  In some cases, these specialized cellular compartments fix carbon dioxide, while in others they crystallize metallic compounds or are designed to extract usable energy from sources such as ethanolamine or 1,2-propanediol, which are produced by their host’s gastrointestinal tract.  All BMC operons characterized to date contain three major components which are inherent to BMC form and function.  These include genes coding for: (i) structural components, (ii) metabolic enzymes, and (iii) additional factors with largely unknown function.  The characterization of these specialized protein shells has accelerated recently with crystal structures of numerous shell proteins now solved, and several, plausible means of encapsulating cargo proteins into BMCs identified.  In a recent breakthrough, our lab successfully produced recombinant Ethanolamine utilization (Eut) BMCs in E. coli solely through the expression of a single, structural protein (EutS).  We also illustrated that a BMC-specific targeting sequence was able to localize an enhanced GFP molecule to the interior of these compartments.  These findings have laid the groundwork for ongoing work in our group which is focused on utilizing cutting-edge synthetic biology to answer both fundamental and applied questions related to the form and function of recombinant BMCs.  We are actively pursuing exciting research avenues into structural and metabolic engineering, which will vastly expand the application and engineering potential of these protein nano-compartments.