Next Article in Journal
Biophysical and In Silico Studies of the Interaction between the Anti-Viral Agents Acyclovir and Penciclovir, and Human Serum Albumin
Previous Article in Journal
Lanthanide Photoluminescence in Heterometallic Polycyanidometallate-Based Coordination Networks
Previous Article in Special Issue
Understanding of MYB Transcription Factors Involved in Glucosinolate Biosynthesis in Brassicaceae
Article

The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions

1
School of Life Sciences, Immanuel Kant Baltic Federal University, 236016 Kaliningrad, Russia
2
Institute of Cell Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia
3
Department of Biophysics and Biotechnology, Voronezh State University, 394018 Voronezh, Russia
4
Department of Cell Biology, Pushchino State Institute of Natural Sciences, 142290 Pushchino, Russia
5
Department of Structural and Functional genomics, Pushchino Scientific Center, 142290 Pushchino, Russia
*
Author to whom correspondence should be addressed.
Molecules 2017, 22(11), 1904; https://doi.org/10.3390/molecules22111904
Received: 13 October 2017 / Revised: 29 October 2017 / Accepted: 2 November 2017 / Published: 5 November 2017
(This article belongs to the Special Issue Metallopeptides)
The Dps protein of Escherichia coli, which combines ferroxidase activity and the ability to bind DNA, is effectively used by bacteria to protect their genomes from damage. Both activities depend on the integrity of this multi-subunit protein, which has an inner cavity for iron oxides; however, the diversity of its oligomeric forms has only been studied fragmentarily. Here, we show that iron ions stabilize the dodecameric form of Dps. This was found by electrophoretic fractionation and size exclusion chromatography, which revealed several oligomers in highly purified protein samples and demonstrated their conversion to dodecamers in the presence of 1 mM Mohr’s salt. The transmission electron microscopy data contradicted the assumption that the stabilizing effect is given by the optimal core size formed in the inner cavity of Dps. The charge state of iron ions was evaluated using Mössbauer spectroscopy, which showed the presence of Fe3O4, rather than the expected Fe2O3, in the sample. Assuming that Fe2+ can form additional inter-subunit contacts, we modeled the interaction of FeO and Fe2O3 with Dps, but the binding sites with putative functionality were predicted only for Fe2O3. The question of how the dodecameric form can be stabilized by ferric oxides is discussed. View Full-Text
Keywords: Escherichia coli; Dps proteins; oligomerization; ferroxidase; transmission electron microscopy; Mössbauer spectroscopy; molecular docking Escherichia coli; Dps proteins; oligomerization; ferroxidase; transmission electron microscopy; Mössbauer spectroscopy; molecular docking
Show Figures

Figure 1

MDPI and ACS Style

Antipov, S.; Turishchev, S.; Purtov, Y.; Shvyreva, U.; Sinelnikov, A.; Semov, Y.; Preobrazhenskaya, E.; Berezhnoy, A.; Shusharina, N.; Novolokina, N.; Vakhtel, V.; Artyukhov, V.; Ozoline, O. The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions. Molecules 2017, 22, 1904. https://doi.org/10.3390/molecules22111904

AMA Style

Antipov S, Turishchev S, Purtov Y, Shvyreva U, Sinelnikov A, Semov Y, Preobrazhenskaya E, Berezhnoy A, Shusharina N, Novolokina N, Vakhtel V, Artyukhov V, Ozoline O. The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions. Molecules. 2017; 22(11):1904. https://doi.org/10.3390/molecules22111904

Chicago/Turabian Style

Antipov, Sergey, Sergey Turishchev, Yuriy Purtov, Uliana Shvyreva, Alexander Sinelnikov, Yuriy Semov, Elena Preobrazhenskaya, Andrey Berezhnoy, Natalia Shusharina, Natalia Novolokina, Viktor Vakhtel, Valeriy Artyukhov, and Olga Ozoline. 2017. "The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions" Molecules 22, no. 11: 1904. https://doi.org/10.3390/molecules22111904

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop