Details

Autor(en) / Beteiligte

• Orban, Katie
• Finkel, Steven E
• Maupin-Furlow, Julie A.

Titel

Dps Is a Universally Conserved Dual-Action DNA-Binding and Ferritin Protein

Ist Teil von

• Journal of bacteriology, 2022-05, Vol.204 (5), p.e0003622-e0003622

Ort / Verlag

United States: American Society for Microbiology

Erscheinungsjahr

2022

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• The DNA-binding protein from starved cells, Dps, is a universally conserved prokaryotic ferritin that, in many species, also binds DNA. Dps homologs have been identified in the vast majority of bacterial species and several archaea. Dps also may play a role in the global regulation of gene expression, likely through chromatin reorganization. Dps has been shown to use both its ferritin and DNA-binding functions to respond to a variety of environmental pressures, including oxidative stress. One mechanism that allows Dps to achieve this is through a global nucleoid restructuring event during stationary phase, resulting in a compact, hexacrystalline nucleoprotein complex called the biocrystal that occludes damaging agents from DNA. Due to its small size, hollow spherical structure, and high stability, Dps is being developed for applications in biotechnology.