Markel Martínez-Carranza

This one is a bit of a departure from the usual and definitely a work in progress!

We found that by using ab initio reconstruction at very high res, in very small steps, we could crack some small structures that had eluded us - e.g. 39kDa iPKAc (EMPIAR-10252), below.

Read on for details... 1/x

Lab’s first paper is out!! We show the first structures of #Asgard #chromatin by #cryo-EM 🧬❄️
Asgard histones form closed and open hypernucleosomes. Closed are conserved across #Archaea, while open resemble eukaryotic H3–H4 octasomes and are Asgard-specific. More here: www.cell.com/molecular-ce...

Serial innovations by Asgard archaea shaped the DNA replication machinery of the early eukaryotic ancestor - Nature Ecology & Evolution Phylogenetic and biochemical analyses show a diversity of components of the DNA replication machinery in different Asgard archaea that contributed to the eukaryotic DNA replication machinery.

Glad to share our paper out today @NatureEcoEvo: “Serial innovations by Asgard archaea shaped the DNA replication machinery of the early eukaryotic ancestor”. www.nature.com/articles/s41... #microsky #archaeasky

Viruses and virus satellites of haloarchaea and their nanosized DPANN symbionts reveal intricate nested interactions - Nature Microbiology An exploration of the viromes of haloarchaea and their ultra-small DPANN symbionts reveals plasmid-derived satellites of viruses from both archaeal groups, highlighting the complexity of nested symbio...

Our work on viruses and virus satellites of haloarchaea and their DPANN symbionts is out today in Nature Microbiology!
@mkrupovic.bsky.social @deemteam.bsky.social @anagtz.bsky.social
www.nature.com/articles/s41...

We’ve uncovered Asgard chromatin structures formed by a Hodarchaeal histone : closed hypernucleosome conserved in archaea and an open form resembling the H3-H4 eukaryotic octasome. Fantastic work by @harshranawat.bsky.social!
www.biorxiv.org/content/10.1...
#Chromatin #Asgard #Archaea #cryoEM

So happy to have published my PhD work! What a funky phage, it was a ride. Big thanks to @beatrizbeamud.bsky.social & @jmouradesousa.bsky.social for bringing their expertise into this story. And my mentors @jmghigolab.bsky.social & @dbikard.bsky.social 💪🏼

Thank you Mart! 🙏

Huge thanks to the whole team, bringing together the NMR and crystallography platforms at @pasteur.fr, the @sauguet-lab.bsky.social and our collaborators at @ifremer.bsky.social 🙏

Our results led us to propose a mechanism by which RPA can stimulate primase activity in the lagging strand through its winged-helix domain. If you are interested in RPA-mediated molecular interactions in the replisome, check the paper linked above! 🧵(4/4)

We show that in our primer extension assays, RPA stimulates the DNA polymerase activity of the primase through its winged-helix domain. 🧵(3/4)

We present the winged-helix domain of Rpa2, which is responsible for archaeal RPA-mediated protein-protein interactions, in complex with the primase and the DNA polymerase PolD. Integrative structural biology approach combining NMR, X-ray and cryo-EM! 🧵(2/4)

Communication between DNA polymerases and Replication Protein A within the archaeal replisome - Nature Communications The single stranded DNA binding protein RPA plays a pivotal role in DNA replication. The archaeal RPA hosts a WH domain that interacts with the DNA primase and the replicative polymerase PolD. Here th...

Super happy to see this work finally out in @naturecomms.bsky.social! Great team effort revealing how single-stranded DNA binding protein RPA interacts with the DNA polymerases in the archaeal replisome 🧵(1/4)
www.nature.com/articles/s41...
@sauguet-lab.bsky.social @pasteur.fr

Interested in the plasmidverse? Then, don't think twice and join the International Society for Plasmid Biology Virtual Seminars Series. 👇

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