Nerve cell connections (synapses) change during repeated day-to-day use to allow us to carry out clever behaviour by learning from experience. This flexible nerve-cell ability uses genes that were captured in earlier eras, and which are re-purposed by natural selection to provide mechanisms for currently useful thinking skills.
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The neuronal protein Arc is a critical mediator of synaptic plasticity. Arc originated in tetrapods and flies through domestication of retrotransposon Gag genes. Recent studies have suggested that Arc mediates intercellular mRNA transfer and like Gag, can form capsid-like structures.
Here we report that Drosophila proteins dArc1 and dArc2 assemble virus-like capsids. We determine the capsid structures to 2.8 Å and 3.7 Å resolution, respectively, finding similarity to capsids of retroviruses and retrotransposons. Differences between dArc1 and dArc2 capsids, including the presence of a structured zinc-finger pair in dArc1, are consistent with differential RNA-binding specificity. Our data support a model in which ancestral capsid-forming and RNA-binding properties of Arc remain under positive selection pressure and have been repurposed to function in neuronal signalling.
- New Results
- Structures of virus-like capsids formed by the Drosophila neuronal Arc proteins
- Simon Erlendsson, Dustin R. Morado, Jason D. Shepherd, John A. G. Briggs
- doi: https://doi.org/10.1101/697193
- This article is a preprint and has not been peer-reviewed [what does this mean?].
See also
The tetrapod neuronal protein ARC and its D. melanogaster homologue, dARC1, have important but differing roles in neuronal development. Both are thought to originate through exaptation of ancient Ty3/Gypsy retrotransposon Gag genes, with their novel function relying on an original capacity for self-assembly and encapsidation of nucleic acids. Here, we present the crystal structure of dARC1 CA and examine the relationship between dARC1, mammalian ARC and the CA protein of circulating retroviruses. We show that whilst the overall architecture is highly related to that of orthoretroviral and spumaretroviral CA, there are significant deviations in both N- and C-terminal domains, potentially affecting recruitment of partner proteins and particle assembly. The degree of sequence and structural divergence suggests that Ty3/Gypsy Gag has been exapted on two separate occasions and that, although mammalian ARC and dARC1 share functional similarity, the structures have undergone different adaptations after appropriation into the tetrapod and insect genomes.
- New Results
- Structure of D. melanogaster ARC1 reveals a repurposed molecule with characteristics of retroviral Gag
- Matthew A. Cottee, Suzanne C. Letham, George R. Young, Jonathan P. Stoye, Ian A. Taylor
- doi: https://doi.org/10.1101/691972
- This article is a preprint and has not been peer-reviewed [what does this mean?].
(Note to readers: The original title numbers in this Natural GMOs series were corrected in a trivial post update)
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