The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans

The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans

Surface (S)-layers are cryptic structures that coat the external surface of the bacterial cell in many species. The paracrystalline regularity of the S-layer is due to the self-assembling of one or more protein units. The property of self-assembling seems to be mediated by specific topologies of the...

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Main Authors: Domenica Farci, Giulia Guadalupi, Katarzyna Bierła, Ryszard Lobinski, Dario Piano
Format: Article
Language:English
Published: Frontiers Media S.A. 2019-06-01
Series:Frontiers in Microbiology
Subjects:
Deinococcus radiodurans
DR_2577
metal-binding domain
oligomerization
SlpA
S-layer deinoxanthin binding complex
Online Access:https://www.frontiersin.org/article/10.3389/fmicb.2019.01450/full
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spelling doaj-8fce3f63dcbe4376895df423590074b82020-11-24T21:29:17ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2019-06-011010.3389/fmicb.2019.01450459972The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radioduransDomenica Farci0Domenica Farci1Giulia Guadalupi2Katarzyna Bierła3Ryszard Lobinski4Dario Piano5Dario Piano6Department of Plant Physiology, Warsaw University of Life Sciences - SGGW, Warsaw, PolandLaboratory of Photobiology and Plant Physiology, Department of Life and Environmental Sciences University of Cagliari, Cagliari, ItalyLaboratory of Photobiology and Plant Physiology, Department of Life and Environmental Sciences University of Cagliari, Cagliari, ItalyLaboratory of Analitycal and Bioinorganic Chemistry and Environment, UMR5254 Institute of Analytical and Physical Chemistry for the Environment and Materials (IPREM), Pau, FranceLaboratory of Analitycal and Bioinorganic Chemistry and Environment, UMR5254 Institute of Analytical and Physical Chemistry for the Environment and Materials (IPREM), Pau, FranceDepartment of Plant Physiology, Warsaw University of Life Sciences - SGGW, Warsaw, PolandLaboratory of Photobiology and Plant Physiology, Department of Life and Environmental Sciences University of Cagliari, Cagliari, ItalySurface (S)-layers are cryptic structures that coat the external surface of the bacterial cell in many species. The paracrystalline regularity of the S-layer is due to the self-assembling of one or more protein units. The property of self-assembling seems to be mediated by specific topologies of the S-layer proteins as well as the presence of specific ions that provide support in building and stabilizing the bi-dimensional S-layer organization. In the present study, we have investigated the self-assembling mechanism of the main S-layer protein of Deinococcus radiodurans (DR_2577) finding an unusual role played by Fe3+ and Cu2+ in the oligomerization of this protein. These findings may trace a structural and functional metallo-mediated convergence between the role of these metals in the assembling of the S-layer and their well-known roles in protecting against oxidative stress in D. radiodurans.https://www.frontiersin.org/article/10.3389/fmicb.2019.01450/fullDeinococcus radioduransDR_2577metal-binding domainoligomerizationSlpAS-layer deinoxanthin binding complex
collection DOAJ
language English
format Article
sources DOAJ
author Domenica Farci
Domenica Farci
Giulia Guadalupi
Katarzyna Bierła
Ryszard Lobinski
Dario Piano
Dario Piano
spellingShingle Domenica Farci
Domenica Farci
Giulia Guadalupi
Katarzyna Bierła
Ryszard Lobinski
Dario Piano
Dario Piano
The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans
Frontiers in Microbiology
Deinococcus radiodurans
DR_2577
metal-binding domain
oligomerization
SlpA
S-layer deinoxanthin binding complex
author_facet Domenica Farci
Domenica Farci
Giulia Guadalupi
Katarzyna Bierła
Ryszard Lobinski
Dario Piano
Dario Piano
author_sort Domenica Farci
title The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans
title_short The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans
title_full The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans
title_fullStr The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans
title_full_unstemmed The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans
title_sort role of iron and copper on the oligomerization dynamics of dr_2577, the main s-layer protein of deinococcus radiodurans
publisher Frontiers Media S.A.
series Frontiers in Microbiology
issn 1664-302X
publishDate 2019-06-01
description Surface (S)-layers are cryptic structures that coat the external surface of the bacterial cell in many species. The paracrystalline regularity of the S-layer is due to the self-assembling of one or more protein units. The property of self-assembling seems to be mediated by specific topologies of the S-layer proteins as well as the presence of specific ions that provide support in building and stabilizing the bi-dimensional S-layer organization. In the present study, we have investigated the self-assembling mechanism of the main S-layer protein of Deinococcus radiodurans (DR_2577) finding an unusual role played by Fe3+ and Cu2+ in the oligomerization of this protein. These findings may trace a structural and functional metallo-mediated convergence between the role of these metals in the assembling of the S-layer and their well-known roles in protecting against oxidative stress in D. radiodurans.
topic Deinococcus radiodurans
DR_2577
metal-binding domain
oligomerization
SlpA
S-layer deinoxanthin binding complex
url https://www.frontiersin.org/article/10.3389/fmicb.2019.01450/full
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