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Schur, F. K. M.

Publications and source records attributed to Schur, F. K. M..

3 recordsLinked to original sources

Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles

Nipah virus (NiV) is a BSL-4 zoonotic paramyxovirus with [~]75% human mortality. The matrix protein (M) of NiV and other paramyxoviruses binds the inner leaflet of the cellular plasma membrane, orchestrating virion assembly by bringing together transmembrane glycoproteins (F/G) and ribonucleoprotein complexes (N). However, the interactions of these full-length proteins within membrane complexes remain elusive. Using cryo-electron tomography and subtomogram averaging of virus like particles (VLPs), we interrogated the protein:protein interactions of the main NiV structural proteins M/N/F/G. The M lattice structure determined to 7[A] revealed a novel M-dimer arrangement that yielded two distinct repeating holes. Notably, F-trimers were arranged above only one of the two holes, dependent on Fs cytoplasmic tail. G was enriched in regions of higher M-VLP curvature, while N dramatically increased M-VLP pleomorphism. This work provides novel insights into paramyxoviral protein complexes, structures, and morphology.

microbiology↗

Emergence of histone-based chromatin complexity in Asgard archaea

The emergence of the eukaryotes coincided with the diversification of histone proteins and their post-translational modifications by enzymes that constitute the core of eukaryotic chromatin. Yet the evolutionary origins of this regulatory machinery are unknown. Here, we show that the key molecular components of histone-based chromatin regulation are present in the Asgard archaea, the closest prokaryotic relatives of eukaryotes. Asgard histones are abundant and have extended N-terminal tails rich in lysine residues that can be post-translationally modified, all of which are features shared with eukaryotic histones. In line with these findings, we identify enzymes from Asgard archaea that deposit or remove lysine acetylation on histone tails in vitro. Moreover, Asgard sirtuin deacetylases (SIR2 proteins) restore chromatin silencing in yeast, demonstrating the functional compatibility of Asgard enzymes with eukaryotic histone substrates. Our findings establish that the foundations of histone-based chromatin predate eukaryogenesis and place Asgard archaea as an evolutionary intermediate in the emergence of eukaryotic chromatin.

evolutionary biology↗

Active virus-host system in a Lokiarchaeon culture

Asgard archaea are considered the closest prokaryotic relatives of eukaryotes and having a crucial role in eukaryogenesis. Only few organisms have been cultivated from this group and their viruses were previously described only through metagenomic reconstructions. Here, we report the first successful cultivation of an Asgard archaeal virus infecting a novel strain of Ca. Lokiarchaeum ossiferum B36. The 16 kbp integrated provirus is capable to excise and replicate independently leading to the formation of virus particles. Network analysis of shared protein clusters with other archaeal viruses places it in a new family, Fylgjaviridae. The host encodes a distinctive repertoire of antiviral defense systems, including Septu, Wadjet, and type II CBASS system, all different from the defense systems of the related strain Ca. L. ossiferum B35. Our cultures provide the first opportunity to study interactions of a virus-host system in Asgards and hold significant potential for developing genetic tools.

microbiology↗