| Literature DB >> 25053115 |
Edward Y Kim1, Marilyn F Slininger, Danielle Tullman-Ercek.
Abstract
Bacterial microcompartments (MCPs) are subcellular organelles that are composed of a protein shell and encapsulated metabolic enzymes. It has been suggested that MCPs can be engineered to encapsulate protein cargo for use as in vivo nanobioreactors or carriers for drug delivery. Understanding the stability of the MCP shell is critical for such applications. Here, we investigate the integrity of the propanediol utilization (Pdu) MCP shell of Salmonella enterica over time, in buffers with various pH, and at elevated temperatures. The results show that MCPs are remarkably stable. When stored at 4°C or at room temperature, Pdu MCPs retain their structure for several days, both in vivo and in vitro. Furthermore, Pdu MCPs can tolerate temperatures up to 60°C without apparent structural degradation. MCPs are, however, sensitive to pH and require conditions between pH 6 and pH 10. In nonoptimal conditions, MCPs form aggregates. However, within the aggregated protein mass, MCPs often retain their polyhedral outlines. These results show that MCPs are highly robust, making them suitable for a wide range of applications.Entities:
Keywords: bacterial microcompartments; microcompartment stability; propanediol utilization; protein encapsulation
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Year: 2014 PMID: 25053115 PMCID: PMC4286999 DOI: 10.1002/pro.2527
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725