R bodies

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Jessica Polka's electron micrograph of negatively stained purified type 51 R bodies in their extended (low pH) state Extended R bodies.jpg
Jessica Polka's electron micrograph of negatively stained purified type 51 R bodies in their extended (low pH) state

R bodies (from refractile bodies, also R-bodies) are polymeric protein inclusions formed inside the cytoplasm of bacteria. [1] Initially discovered in kappa particles, bacterial endosymbionts of the ciliate Paramecium , R bodies (and genes encoding them) have since been discovered in a variety of taxa. [2]

Contents

Morphology, assembly, and extension

At neutral pH, type 51 R bodies resemble a coil of ribbon approximately 500 nm in diameter and approximately 400 nm deep. [1] Encoded by a single operon containing four open reading frames, [3] [4] R bodies are formed from two small structural proteins, RebA and RebB. [5] A third protein, RebC, is required for the covalent assembly of these two structural proteins into higher-molecular weight products, visualized as a ladder on an SDS-PAGE gel. [5]

At low pH, Type 51 R bodies undergo a dramatic structural rearrangement. Much like a paper yo-yo, the ribbon extends (from the center) to form hollow tube with pointed ends that can reach up to 20μm in length. [6]

Other types of R bodies from different bacterial species vary in their size, ribbon morphology, and triggers for extension. [1]

Function

When kappa particles shed from a killer paramecium are ingested, R bodies extend within the acidic food vacuole of the predatory paramecium, distending and rupturing the membrane. [7] This liberates the contents of the food vacuole into the cytoplasm of the paramecium. [7] While feeding kappa particles to sensitive paramecium results in the death of paramecium, feeding purified R bodies or R bodies recombinantly expressed in E. coli is not toxic. [3] [8] Thus, R bodies are thought to function as a toxin delivery system.

R bodies are also capable of rupturing E. coli spheroplasts, demonstrating that they can rupture membranes in a foreign context, and they can be engineered to extend at a variety of different pH levels. [9]

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References

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  9. Polka, Jessica K.; Silver, Pamela A. (2016-04-15). "A Tunable Protein Piston That Breaks Membranes to Release Encapsulated Cargo" (PDF). ACS Synthetic Biology. 5 (4): 303–311. doi: 10.1021/acssynbio.5b00237 . PMID   26814170.