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Authors’ contributions RD and DF carried out the laboratory experiments. MC and MCT designed the study and RD, MC and MCT wrote the manuscript. All authors read and approved the final manuscript.”
“Background Eukaryotic genomes are packaged into the nucleus by histones and non histone proteins. Histones are small, highly basic proteins that form a core around which the DNA is wrapped. Although chromatin is highly compacted, its structure is dynamic, allowing access to the DNA for processes such as replication, transcription, Selisistat recombination and repair [1, 2]. Nucleoid-associated proteins have been described in archaea and bacteria. These proteins resemble eukaryotic histones in their DNA binding properties,

low molecular weight, abundance and electrostatic charge. They organize and compact the prokaryotic genome and are involved in various processes, including gene expression [3, 4]. The proteins involved in DNA packaging in eukaryotic organelles have check details not been fully characterized. In the protozoa of the Trypanosomatidae family, the mitochondrial genome is contained within a specific region of the mitochondrion known as the kinetoplast. The kinetoplast DNA (kDNA) of trypanosomatids is organized into an unusual arrangement of circular molecules, catenated into a single network. Two types of DNA ring are present within the kinetoplast: maxicircles and minicircles. The maxicircles resemble the mitochondrial DNA of higher SRT1720 order eukaryotes, encoding rRNAs and subunits of the respiratory complexes [5]. The minicircles

encode guide RNAs, which modify the maxicircle transcripts by extensive insertions and/or deletions of uridylate residues to form functional open reading frames, in a process known as RNA editing [6]. The replication of kinetoplast DNA requires a repertoire of molecules, including type II topoisomerases, Thalidomide DNA polymerases, universal minicircle sequence binding proteins, primases and ribonucleases [7, 8]. The molecules involved in maintaining the highly ordered organization of kDNA in trypanosomatids remained unknown for many years. In 1965, Steinert suggested that the kinetoplast DNA was not associated with basic proteins [9]. However, Souto-Padrón and De Souza provided cytochemical evidence that the kDNA of Trypanosoma cruzi was associated with basic proteins [10, 11]. They suggested that such proteins might be involved in neutralizing the negatively charged DNA molecules in close contact within the kinetoplast matrix.