After a wonderful four day, @giglionelab.bsky.social wraps up #proteintermini2026 Grazie, Carmela for a fantastic meeting and we look forward to Heidelberg in 2028!

Pleased to have contributed to this exciting work by @beckmannlab.bsky.social on the mechanism of co-translational acetylation of histones!

Glad to be part of this great work from @beckmannlab.bsky.social, led by @guan316.bsky.social and @timodenk.bsky.social, exploring the mechanics of co-translational acetylation of histones by NAA40.

How are histones acetylated as they emerge from the ribosome? We show that NAA40 cooperates with the NAC complex to enable co-translational acetylation of H2A/H4, revealing NAC as a coordinator of nascent protein modification. Read more about our collaboration with @kirmizislab.bsky.social #cryoEM

📢 Our new paper is out! @kirmizislab.bsky.social H2A.X is N-terminally acetylated by NAA40–a novel histone mod responsive to UV irradiation. Thanks to all authors @bonalditiziana.bsky.social @drksquare.bsky.social, anonymous reviewers and @springernature.com #Epigenetics&Chromatin Editorial team.