This study characterizes HLp, a bacterial histone that forms tetramers and wraps ~60 base pairs of DNA, revealing a new mode of histone-DNA interaction in bacteria.

Nature Communications · Dec 11, 2025Peer-reviewedBiochemistry

Archaeal histone HTkC hypercompacts DNA

Samuel Schwab, Yimin Hu, Shingo Yamamoto, Kodai Yamaura, Naomichi Takemata, Marcus D. Hartmann, Marc K M Cajili, Bert van Erp, Haruyuki Atomi, Vikram Alva, Birte Hernandez Alvarez, Remus Thei Dame

This study shows that the archaeal histone HTkC forms highly compact DNA structures, doubling the compaction level of hypernucleosomes and highlighting its role in chromatin organization.

bioRxiv · Dec 6, 2025 · PreprintBiochemistry

Functional relevance of CASP16 nucleic acid predictions as evaluated by structure providers

Rachael C. Kretsch, Reinhard Albrecht, Ebbe Sloth Andersen, Hsuan‐Ai Chen, Wah Chiu, Rhiju Das, Jeanine Gezelle, Marcus D. Hartmann, Claudia Höbartner, Yimin Hu, Shekhar Jadhav, Philip E. Johnson, Christopher P. Jones, Deepak Koirala, Emil L. Kristoffersen, , Andriy Kryshtafovych

Structure providers for 18 CASP16 nucleic acid targets find blind predictions capture secondary structure but miss non-canonical interactions, backbone kinks, ligand sites, and intermolecular interfaces.

Proteins Structure Function and Bioinformatics · Sep 4, 2025Peer-reviewedBiophysics✦ In-depth digest