Identification, characterization and classification of prokaryotic nucleoid‐associated proteins
Molecular Microbiology, Volume 123, Issue 3, Page 206-217, March 2025.Nucleoid‐associated proteins (NAPs) structure DNA by either bending, wrapping, bridging, or forming protein filaments on the DNA. We review newly identified NAPs and provide a list of simple biochemical assays to study the DNA‐structuring properties of novel NAPs. Abstract Common throughout life is the need to compact and organize the genome.
Samuel Schwab, Remus T. Dame
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Chromatin and gene regulation in archaea
Molecular Microbiology, Volume 123, Issue 3, Page 218-231, March 2025.Recent data from diverse archaea with different repertoires of nucleoid‐associated proteins show a common genome‐wide chromatin organisation where chromatin maintains access to gene promoters independently of transcription activity. Abstract The chromatinisation of DNA by nucleoid‐associated proteins (NAPs) in archaea ‘formats’ the genome structure in ...
Fabian Blombach, Finn Werner
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Biotransformation of High Concentrations of Ginsenoside Substrate into Compound K by β-glycosidase from Sulfolobus solfataricus. [PDF]
Genes (Basel), 2023 Wang P, Tang C, Liu Y, Yang J, Fan D.
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NMR Structure and Biophysical Characterization of Thermophilic Single-Stranded DNA Binding Protein from Sulfolobus Solfataricus. [PDF]
Int J Mol Sci, 2022 Yang MJ, Kim J, Lee Y, Lee W, Park CJ.
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eLife, 2019 DNA replication requires that the duplex genomic DNA strands be separated; a function that is implemented by ring-shaped hexameric helicases in all Domains.
Himasha M Perera, Michael A Trakselis
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Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy. [PDF]
Acta Crystallogr F Struct Biol Commun, 2021 Zeng YC, Sobti M, Stewart AG.
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Structure of a dimer of the Sulfolobus solfataricus MCM N-terminal domain reveals a potential role in MCM ring opening. [PDF]
Acta Crystallogr F Struct Biol Commun, 2021 Meagher M, Spence MN, Enemark EJ.
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Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox.
PLoS ONE, 2013 Enzymes are proficient catalysts that enable fast rates of Michaelis-complex formation, the chemical step and products release. These different steps may require different conformational states of the active site that have distinct binding properties ...
Julien Hiblot +3 more
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Analysis of the crystal structure of an active MCM hexamer
eLife, 2014 In a previous Research article (Froelich et al., 2014), we suggested an MCM helicase activation mechanism, but were limited in discussing the ATPase domain because it was absent from the crystal structure.
Justin M Miller +3 more
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