Remus Thei Dame

This study investigates how Crl regulates gene transcription in E. coli during exponential growth, both independently and in conjunction with RpoS, under varying environmental conditions.

This study investigates how H-NS and StpA regulate gene expression in E. coli under acid and osmotic stress by analyzing transcription, DNA binding, and chromatin structure at specific operons.

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.

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.

This study investigates how Mg2+ ions affect the structure and stability of hypernucleosomes formed by archaeal histones from T. kodakarensis, showing distinct effects compared to previously characterized histones.

This study presents the first cryo-EM structures of Asgard chromatin assemblies, revealing closed and open hypernucleosome conformations and their evolutionary implications.

This study investigates the DNA-binding properties of bacterial histone HBb in Bdellovibrio bacteriovorus, revealing its ability to bend DNA in a sequence-independent manner, similar to archaeal and eukaryotic histones.

The paper provides in vivo evidence that NAP-mediated chromosome re-modelling regulates transcription of the osmoresponsive proVWX operon in E. coli by destabilizing and re-establishing H-NS bridges under hyperosmotic conditions.

The paper uses AlphaFold2 to classify prokaryotic histones into 17 groups and identifies a new histone superfamily that bridges DNA instead of wrapping it.

This paper identifies Gbn, a novel GATC-binding NAP in Streptomyces, showing its impact on development and gene expression through chromatin binding and transcriptomic analysis.

This study investigates the DNA binding properties of Rok from B. subtilis and shows it functions as a DNA bridging protein, unlike other H-NS-like proteins whose DNA bridging is affected by physico-chemical conditions.