Juha Huiskonen (@juhahuiskonen) — Bluesky Profile

2 months ago

ScienceDirect.com | Science, health and medical journals, full text articles and books.

authors.elsevier.com/sd/article/S...

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2 months ago

I am pleased to share our new paper in Molecular Cell:

“Capsid restructuring activates semi-conservative dsRNA transcription in cystovirus ɸ6.”

We visualized, in structural detail, how a double-stranded RNA virus switches from a quiescent to a transcriptionally active state.

Link in the comments

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7 months ago

Capsid Restructuring Activates Semi-Conservative dsRNA Transcription in Cystovirus ɸ6 Double-stranded (ds)RNA viruses replicate and transcribe their genome within a proteinaceous viral capsid to evade host cell defenses. While Reovirales members use conservative transcription, most dsR...

www.biorxiv.org/content/10.1...

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7 months ago

Excited to share our latest preprint "Capsid Restructuring Activates Semi-Conservative dsRNA Transcription in Cystovirus ɸ6". We show that nucleotide-triggered disassembly of the outer capsid layer is followed by expansion of the inner layer and the stepwise assembly of transcription complexes.

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8 months ago

We will make them available when the peer reviewed version of the paper is published

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8 months ago

In situ Structure of the Human Gap Junction Gap junction plaques, comprising connexin channels arranged in organized lattices, are essential for direct intercellular communication through the exchange of ions and small molecules. Previous studies have extensively characterized the structures of detergent-solubilized, purified connexin channels, leading to models of channel gating. However, these structures lack the physiological context of the native assembly and omit key intracellular regions, including the C-terminal domain. As a result, the molecular mechanisms underlying gap junction plaque assembly in cells remain poorly understood. Here, we establish human embryonic kidney cells as a model system to study gap junction architecture in situ. Using cryogenic electron tomography and focused ion beam milling, we resolve the structure of human connexin-43 gap junction plaques at 14 A resolution. Our results reveal a previously unrecognized structural role for the C-terminal domain in mediating lateral channel-channel interactions essential for plaque formation. Complementary coarse grained molecular dynamics simulations illuminate how lipids pack between adjacent connexin molecules contributing to the plaque organization and stability. By uncovering structural features absent from isolated channel studies, our integrative approach provides fundamental insight into the molecular architecture of gap junction plaques and establishes a structural framework for future investigations into their roles in health and disease. ### Competing Interest Statement The authors have declared no competing interest.

www.biorxiv.org/cgi/content/...

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8 months ago

CryoET tomogram with the gap junction (green), ribosomes (cyan) and microtubules (pink)

In our latest preprint on bioRxiv, we present the in situ structure of
the human gap junction at 14 Å resolution using cryo-ET.

The structure provides a blueprint for investigating how connexin
regulation shapes intercellular communication in health and disease.

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