Abstract
Rapid increase of intracellular synthesis of specific histone-like Dps protein that binds DNA to protect the genome against deleterious factors leads to in cellulo crystallization—one of the most curious processes in the area of life science at the moment. However, the actual structure of the Dps–DNA co-crystals remained uncertain in the details for more than two decades. Cryo-electron tomography and small-angle X-ray scattering revealed polymorphous modifications of the co-crystals depending on the buffer parameters. Two different types of the Dps–DNA co-crystals are formed in vitro: triclinic and cubic. Three-dimensional reconstruction revealed DNA and Dps molecules in cubic co-crystals, and the unit cell parameters of cubic lattice were determined consistently by both methods.
Highlights
During the last two decades, the formation of protective Dps–DNA complexes in stress-induced cells has attracted the attention of many scientific groups, among which the most famous and remarkable are works of A
The response to stress of living cells is expressed in their transition to the stationary phase and rapid increase of intracellular synthesis of specific histone-like Dps protein (DNA-binding protein from starved cells), which binds DNA to protect the genome against such deleterious factors as thermal stress, irradiation, toxicity, chemical shock, and oxidative stress
This study demonstrated, for the first time, polymorphous behavior of Dps–DNA crystallization in vitro resulting in formation of cubic and triclinic structures depending on buffer parameters and local ion concentration
Summary
During the last two decades, the formation of protective Dps–DNA complexes in stress-induced cells has attracted the attention of many scientific groups, among which the most famous and remarkable are works of A. The response to stress of living cells is expressed in their transition to the stationary phase and rapid increase of intracellular synthesis of specific histone-like Dps protein (DNA-binding protein from starved cells), which binds DNA to protect the genome against such deleterious factors as thermal stress, irradiation, toxicity, chemical shock, and oxidative stress. Dps is a multifunctional histone-like protein which combines the ferroxidase activity and the ability to bind DNA nonspecifically. The bacterial histone-like proteins are associated with a nucleoid, maintaining structural integrity and being involving in such DNA-dependent processes as transcription, recombination, replication, or any other. Dps is the only DNA-binding protein that is produced only in the stationary phase E. coli [4], and it demonstrates the sequence nonspecific DNA binding activity [7,8]
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