A biophysical study of DNA condensation mediated by histones and protamines

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dc.citation.volume368pt_BR
dc.contributor.authorda Silva, Emerson Rodrigo [UNIFESP]
dc.contributor.authorSouza, Bruna B.S. [UNIFESP]
dc.contributor.authorLourenço, Thiago C. [UNIFESP]
dc.contributor.authorGerbelli, Barbara B.
dc.contributor.authorOseliero Filho, Pedro L.
dc.contributor.authorOliveira, Cristiano L.P. [UNIFESP]
dc.contributor.authorMiranda, Antonio [UNIFESP]
dc.contributor.authorLatteshttp://lattes.cnpq.br/7800589206457326pt_BR
dc.date.accessioned2023-05-11T14:02:02Z
dc.date.available2023-05-11T14:02:02Z
dc.date.issued2022-12-15
dc.description.abstractThe compaction of long DNA strands into confined spaces such as the nuclei of eukaryotic cells is an essential phenomenon towards the emergence of elaborated forms of life. Histones and protamines are the major nucleoproteins involved in this task participating in the formation of chromatin in somatic and germinative cells, respectively. In addition to a fundamental understanding of critical biological processes, DNA condensation also holds strong potential in biotechnology. Herein, we investigate the mesoscale structure of complexes formed between DNA and histones or protamines. A sophisticated set of biophysical methods encompassing steady-state fluorimetry, small-angle X-ray scattering and infrared nano spectroscopy was used to unveil both the self-assembly and molecular interactions of these complexes. We explored the fluorescence of a molecular rotor, thioflavin T, to investigate the accessibility of ligands in the inter-base environment of DNA strands. AFM-based infrared spectroscopy was used for the first time to probe the vibrational signature of individual DNA/nucleoprotein nano assemblies and disclose secondary-structure features. Our results show that protamines form highly compact structures in which DNA folding hinders access to the inter-base spacing. These assemblies exhibit diversified secondary-structure conformations, with the presence of -sheets stabilizing the packing. In contrast, histone-based complexes are characterized by fibrillar nano assemblies exhibiting larger inter strands separations and access to guest molecules that intercalate between bases. The findings presented here may help the understanding of DNA condensation mediated by these two major nucleoproteins and may assist the optimization of gene vehicles based on these promising nano assemblies.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipIDFAPESP, 19/20907-7pt_BR
dc.format.extent120745pt_BR
dc.identifierhttps://www.sciencedirect.com/science/article/pii/S016773222202284Xpt_BR
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/67488
dc.languageeng
dc.publisherElsivieren
dc.relation.ispartofJournal of Molecular Liquidsen
dc.rightsinfo:eu-repo/semantics/openAccesspt_BR
dc.subjectCondensationen
dc.subjectDNA
dc.subjectNucleoproteinen
dc.subjectMesophaseen
dc.subjectChromatinen
dc.titleA biophysical study of DNA condensation mediated by histones and protaminesen
dc.typeinfo:eu-repo/semantics/articlept_BR
unifesp.campusEscola Paulista de Medicina (EPM)pt_BR
unifesp.departamentoBiofísicapt_BR
unifesp.graduateProgramCiências Biológicas (Biologia Molecular)pt_BR
unifesp.knowledgeAreaBiofísicapt_BR
unifesp.researchAreaBiofísica molecularpt_BR
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