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The Cold Shock Domain of YB-1 Segregates RNA from DNA by Non-Bonded Interactions

The human YB-1 protein plays multiple cellular roles, of which many are dictated by its binding to RNA and DNA through its Cold Shock Domain (CSD). Using molecular dynamics simulation approaches validated by experimental assays, the YB1 CSD was found to interact with nucleic acids in a sequence-depe...

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Detalles Bibliográficos
Autores principales: Kljashtorny, Vladislav, Nikonov, Stanislav, Ovchinnikov, Lev, Lyabin, Dmitry, Vodovar, Nicolas, Curmi, Patrick, Manivet, Philippe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4493011/
https://www.ncbi.nlm.nih.gov/pubmed/26147853
http://dx.doi.org/10.1371/journal.pone.0130318
Descripción
Sumario:The human YB-1 protein plays multiple cellular roles, of which many are dictated by its binding to RNA and DNA through its Cold Shock Domain (CSD). Using molecular dynamics simulation approaches validated by experimental assays, the YB1 CSD was found to interact with nucleic acids in a sequence-dependent manner and with a higher affinity for RNA than DNA. The binding properties of the YB1 CSD were close to those observed for the related bacterial Cold Shock Proteins (CSP), albeit some differences in sequence specificity. The results provide insights in the molecular mechanisms whereby YB-1 interacts with nucleic acids.