Williams Sunanda Margrett, Chatterji Dipankar
Institute of Structural and Molecular Biology, Birkbeck, University of London, Malet Street, London WC1E 7HX, United Kingdom.
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
ACS Omega. 2023 Sep 11;8(38):34299-34309. doi: 10.1021/acsomega.3c03277. eCollection 2023 Sep 26.
Iron plays a vital role in the maintenance of life, being central to various cellular processes, from respiration to gene regulation. It is essential for iron to be stored in a nontoxic and readily available form. DNA binding proteins under starvation (Dps) belong to the ferritin family of iron storage proteins and are adept at storing iron in their hollow protein shells. Existing solely in prokaryotes, these proteins have the additional functions of DNA binding and protection from oxidative stress. Iron storage proteins play a functional role in storage, release, and transfer of iron and therefore are central to the optimal functioning of iron homeostasis. Here we review the multifarious properties of Dps through relevant biochemical and structural studies with a focus on iron storage and ferroxidation. We also examine the role of Dps as a possible candidate as an iron donor to iron-sulfur (Fe-S) clusters, which are ubiquitous to many biological processes.
铁在维持生命过程中起着至关重要的作用，它是从呼吸作用到基因调控等各种细胞过程的核心要素。铁必须以无毒且易于获取的形式储存。饥饿状态下的DNA结合蛋白（Dps）属于铁储存蛋白的铁蛋白家族，擅长将铁储存在其空心蛋白壳中。这些蛋白仅存在于原核生物中，还具有DNA结合以及抵御氧化应激的额外功能。铁储存蛋白在铁的储存、释放和转运过程中发挥功能性作用，因此对于铁稳态的最佳功能至关重要。在此，我们通过相关的生化和结构研究，重点围绕铁储存和铁氧化作用，综述Dps的多种特性。我们还研究了Dps作为铁硫（Fe-S）簇铁供体潜在候选者的作用，铁硫簇在许多生物过程中普遍存在。
