Part:BBa_K4143337
T4GALA Encapsulin
Encapsulins are protein compartments that exist naturally in a variety of bacteria and archaea, and are composed of a single shell protein that self-assembles and can help to sequester and protect antimicrobial peptides when they are expressed in E.coli. Once assembled, they typically form 25–42 nm diameter icosahedral structures.
Usage and Biology
Encapsulins are protein organelles, that encapsulate cargo proteins which are "targeted to the encapsulin capsid interior via small C-terminal peptides referred to as targeting peptides." [1] They typically function to sequester harmful reactions from the rest of the cell, which means that incompatible reactions can occur in a cell at the same time. The encapsulin system is consists of the encapsulin capsid and core cargo genes, which may also be referred to as the core operon.
Encapsulins are notable for being stable once assembled which prevents the efficient release of cargo, therefore physiological conditions such as surrounding pH conditions may prompt disassembly. Notably, "disassembling and reassembling viral capsids or encapsulins requires extremes of pH or salt concentration[2], which is not conducive in an in-vitro environment, however the encapsulin we selected has triggered assembly/reassembly at pH=6.
References
[1]T. W. Giessen and P. A. Silver, “Widespread distribution of encapsulin nanocompartments reveals functional diversity,” Nature Microbiology, vol. 2, no. 6, p. 17029, Mar. 2017, doi: 10.1038/nmicrobiol.2017.29.
[2]J. A. Jones, A. S. Cristie-David, M. P. Andreas, and T. W. Giessen, “Triggered reversible disassembly of an engineered protein nanocage,” bioRxiv, p. 2021.04.19.440480, Jan. 2021, doi: 10.1101/2021.04.19.440480.
Contents
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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