Asgard archaeal origin of microtubules
Löwe, J.; von Kügelgen, A.; Planelles-Herrero, V. J.; McAndrew, M. B. L.; Oliva, M. A.; Vosseberg, J.; Köstlbacher, S.; Dharamshi, J. E.; Appler, K. E.; MacLeod, F. I.; Nobs, S.-J.; Jorgensen, S. L.; Burns, B. P.; Baker, B. J.; Bharat, T. A. M.; Derivery, E.; Tamarit, D.; Ettema, T. J. G.
Show abstract
Eukaryotic cells change their shapes, actively segregate their DNA and contain membrane networks, facilitated by a complex cytoskeleton containing actin filaments, microtubules made from tubulin, and other components. These filaments have ancient evolutionary origins since actin- and tubulin-like proteins form prokaryotic cytoskeletons in archaea and bacteria. Bona fide eukaryotic F-actin can be traced back to crenarchaea and Asgard archaea, which are the closest known relatives of eukaryotes. A possible Asgard archaeal origin of microtubules was suggested recently with the discovery of a lokiarchaeon containing AtubAB mini microtubules that share architectural features with their eukaryotic counterparts. Using phylogenetic analyses of metagenomic data, here we report the broad occurrence of tubulins in Asgard archaea. Biochemical and structural analyses showed that one of our newly discovered heimdallarchaeial AtubAB tubulin pairs forms four-protofilament mini-microtubules that show dynamic instability and are inhibited by the tubulin drug maytansine. Our work raises the possibility that microtubule architecture and dynamics evolved in Asgard archaea prior to eukaryogenesis.
Matching journals
The top 4 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- Structure of the ciliary tip central pair reveals the unique role of the microtubule-seam binding protein SPEF1 96%
- An internally controlled system to study microtubule network diversification links tubulin evolution to the use of distinct microtubule regulators 95%
- Mechanistic basis of temperature-adaptation in microtubule dynamics across frog species 95%
Similar papers in this journal
- Changes in seam number and location induce holes within microtubules assembled from porcine brain tubulin and in Xenopus egg cytoplasmic extracts 96%
- WDR90 is a centriolar microtubule wall protein important for centriole architecture integrity. 95%
- Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.