Publications by authors named "F Culard"
MC1, a monomeric nucleoid-associated protein (NAP), is structurally unrelated to other DNA-binding proteins. The protein participates in the genome organization of several Euryarchaea species through an atypical compaction mechanism. It is also involved in DNA transcription and cellular division through unknown mechanisms.
View Article and Find Full Text PDFThe nucleoid-associated protein HU is involved in numerous DNA transactions and thus is essential in DNA maintenance and bacterial survival. The high affinity of HU for SSBs (single-strand breaks) has suggested its involvement in DNA protection, repair and recombination. SSB-containing DNA are major intermediates transiently generated by bifunctional DNA N-glycosylases that initiate the BER (base excision repair) pathway.
View Article and Find Full Text PDFHU is one of the major nucleoid-associated proteins involved in bacterial chromosome structure and in all DNA-dependent cellular activities. Similarly to eukaryotic histones, this small dimeric basic protein wraps DNA in a non-sequence specific manner, promoting DNA super-structures. In most bacteria, HU is a homodimeric protein encoded by a single gene.
View Article and Find Full Text PDFArticle Synopsis
- DNA glycosylases from the Fpg/Nei superfamily are crucial for repairing oxidized DNA bases, ensuring genome stability, but their inhibitors could be useful in cancer treatments due to synthetic lethal interactions.
- The inhibitor 2-thioxanthine (2TX) was found to target the zinc finger DNA binding domain of the Fpg glycosylase, and its mechanism involves reacting with cysteine thiolates, leading to the loss of zinc from the enzyme.
- Understanding how 2TX interacts with Fpg lays the groundwork for developing new, more effective inhibitors that could selectively target DNA glycosylases in therapeutic applications.
Article Synopsis
- - The study focuses on how the Methanogen Chromosomal protein 1 (MC1) from Euryarchaea interacts with bent DNA, contributing to our understanding of DNA packaging mechanisms in Archaea.
- - Researchers used Nuclear Magnetic Resonance (NMR) and paramagnetic probes to map the binding interactions and determine the polarity of MC1's attachment to DNA.
- - They proposed the first structural model of the DNA-MC1 complex, confirming essential amino acids for DNA binding through experiments, highlighting the role of the Arg25 side-chain in neutralizing negative charges in the DNA's structure.