RT @Luisjagago: Our study on Diphyllatea (CRuMs) is out! From our lovely trip to the South Pacific, we manage to get 4 new transcriptomes f….

RT @delaconcepcionj: How can protein complexes diversify without compromising their function? In our new pre-print, we explore this questio….

RT @PlantoPhagy: 🆕 & 🆒#Preprint led by @delaconcepcionj adressing a key #evocellbio question: How can individual subunits of multimeric pro….

Happy to see our paper on viral histones and the origin of the nucleosome finally out @NatureMicrobiol!. Many thanks to Tom Richards and @MertonCollege.

If you find this work and horizontal gene transfer interesting and want to get involved, get in touch! This will all be continuing next year at my new lab at @gmivienna! (10/10)

Please read the paper for more information! This was a great collaboration with Tom Richards, and many thanks to @tobias_warnecke @antoine_hocher @Luisjagago for help and discussions and @MertonCollege for support! (9/10).

So how did nucleosomes evolve? Core histones evolved by duplication. Linkers facilitated folding without chaperones, but once they evolved, histones could reversibly fragment. Finally, a ratchet occurred, locking histones in their individual states (N-terminal tail use?) (8/10)

Based on the intermediate phylogenetic position, functional characteristics, and other analyses, we argue that these viral histone repeats represent molecular relics acquired by viruses from stem-eukaryotes by HGT, providing snapshots of ancient nucleosome evolution. (7/10)

Nucleosomes require chaperones, so how are these structures forming? We thought that the histone linkers might be involved. To test this, we put linked and unlinked Xenopus histones in E.coli. Turns out animal nucleosomes can form in bacteria but linkers can help assembly! (6/10)

They can even compact the E. coli nucleoid, unlike archaeal histones! (5/10)

To understand histone repeat function, we examined the activity of histone quadruplets in E. coli. Remarkably, these histones self-assemble into nucleosome-like structures that wrap 150 bp, like eukaryotic nucleosomes, but oligomerize like archaeal histones. (4/10)

Our phylogenetic analysis of these histone repeats corroborates work by @PaulTalbert10 and @AlbertErives showing that these viral histones branch between Archaea and eukaryotes in an intermediate position suggesting an ancient origin (3/10)

We surveyed thousands of giant viral genomes and identified hundreds of viral histones including histone singlets, doublets, triplets, and quadruplets, the last of which comprise the four core histones fused in series (2/10)

Excited to share our manuscript about how we studied the function and evolution of giant viral histones to understand the origin of the nucleosome (1/10)

RT @gmivienna: We are #hiring! The Gregor Mendel Institute has a Junior Group Leader position available. We seek #researchers who will help….

So excited to be joining the GMI next year! 🫛.

RT @PlantoPhagy: Chuffed to finally have our preprint (Shuffled ATG8 interacting motifs form an ancestral bridge between #UFMylation and #a….

RT @gutmicrobiome: Our paper made the cover! . One of our beautiful Bryozoa colonies from Quadra Island in British Columbia collected by @d….

RT @gutmicrobiome: So pleased to see our paper out today in @NatureMicro! .We compared bacterial microbiomes of microscopic marine inverteb….

RT @PlantoPhagy: Here it is🥰 Our new #preprint led by L. Picchianti, @Victor_SMH, N. Zhan together with @gekaragoz lab (the first of many t….