PMID- 36658780
OWN - NLM
STAT- MEDLINE
DCOM- 20230131
LR  - 20230220
IS  - 1469-896X (Electronic)
IS  - 0961-8368 (Print)
IS  - 0961-8368 (Linking)
VI  - 32
IP  - 2
DP  - 2023 Feb
TI  - Controlled modulation of the dynamics of the Deinococcus grandis Dps N-terminal 
      tails by divalent metals.
PG  - e4567
LID - 10.1002/pro.4567 [doi]
LID - e4567
AB  - DNA-binding proteins from starved cells (Dps) are small multifunctional nanocages 
      expressed by prokaryotes in acute oxidative stress conditions or during the 
      starvation-induced stationary phase, as a bacterial defense mechanism. Dps 
      proteins protect bacterial DNA from damage by either direct binding or by 
      removing precursors of reactive oxygen species from solution. The DNA-binding 
      properties of most Dps proteins studied so far are related to their unordered, 
      flexible, N- and C-terminal extensions. In a previous work, we revealed that the 
      N-terminal tails of Deinoccocus grandis Dps shift from an extended to a compact 
      conformation depending on the ionic strength of the buffer and detected a novel 
      high-spin ferrous iron center in the proximal ends of those tails. In this work, 
      we further explore the conformational dynamics of the protein by probing the 
      effect of divalent metals binding to the tail by comparing the metal-binding 
      properties of the wild-type protein with a binding site-impaired D34A variant 
      using size exclusion chromatography, dynamic light scattering, synchrotron 
      radiation circular dichroism, and small-angle X-ray scattering. The N-terminal 
      ferrous species was also characterized by Mossbauer spectroscopy. The results 
      herein presented reveal that the conformation of the N-terminal tails is altered 
      upon metal binding in a gradual, reversible, and specific manner. These 
      observations may point towards the existence of a regulatory process for the 
      DNA-binding properties of Dps proteins through metal binding to their N- and/or 
      C-terminal extensions.
CI  - (c) 2023 The Authors. Protein Science published by Wiley Periodicals LLC on behalf 
      of The Protein Society.
FAU - Guerra, Joao P L
AU  - Guerra JPL
AUID- ORCID: 0000-0001-5441-9446
AD  - UCIBIO - Applied Molecular Biosciences Unit, Department of Chemistry, NOVA School 
      of Science and Technology | FCT NOVA, Universidade NOVA de Lisboa, Caparica, 
      Portugal.
AD  - Associate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of 
      Science and Technology | FCT NOVA, Universidade NOVA de Lisboa, Caparica, 
      Portugal.
FAU - Blanchet, Clement E
AU  - Blanchet CE
AUID- ORCID: 0000-0003-3432-8496
AD  - European Molecular Biology Laboratory, Hamburg Outstation, Hamburg, Germany.
FAU - Vieira, Bruno J C
AU  - Vieira BJC
AUID- ORCID: 0000-0002-6536-9875
AD  - Centro de Ciencias e Tecnologias Nucleares, DECN, Instituto Superior Tecnico, 
      Universidade de Lisboa, Bobadela LRS, Portugal.
FAU - Waerenborgh, Joao C
AU  - Waerenborgh JC
AUID- ORCID: 0000-0001-6171-4099
AD  - Centro de Ciencias e Tecnologias Nucleares, DECN, Instituto Superior Tecnico, 
      Universidade de Lisboa, Bobadela LRS, Portugal.
FAU - Jones, Nykola C
AU  - Jones NC
AUID- ORCID: 0000-0002-4081-6405
AD  - ISA, Department of Physics and Astronomy, Aarhus University, Aarhus, Denmark.
FAU - Hoffmann, Soren Vronning
AU  - Hoffmann SV
AUID- ORCID: 0000-0002-8018-5433
AD  - ISA, Department of Physics and Astronomy, Aarhus University, Aarhus, Denmark.
FAU - Pereira, Alice S
AU  - Pereira AS
AUID- ORCID: 0000-0001-5567-6073
AD  - UCIBIO - Applied Molecular Biosciences Unit, Department of Chemistry, NOVA School 
      of Science and Technology | FCT NOVA, Universidade NOVA de Lisboa, Caparica, 
      Portugal.
AD  - Associate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of 
      Science and Technology | FCT NOVA, Universidade NOVA de Lisboa, Caparica, 
      Portugal.
FAU - Tavares, Pedro
AU  - Tavares P
AUID- ORCID: 0000-0002-7398-2661
AD  - UCIBIO - Applied Molecular Biosciences Unit, Department of Chemistry, NOVA School 
      of Science and Technology | FCT NOVA, Universidade NOVA de Lisboa, Caparica, 
      Portugal.
AD  - Associate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of 
      Science and Technology | FCT NOVA, Universidade NOVA de Lisboa, Caparica, 
      Portugal.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Protein Sci
JT  - Protein science : a publication of the Protein Society
JID - 9211750
RN  - 0 (Bacterial Proteins)
RN  - 0 (DNA, Bacterial)
RN  - Deinococcus grandis
SB  - IM
MH  - Amino Acid Sequence
MH  - *Bacterial Proteins/chemistry
MH  - *Deinococcus/chemistry/genetics/metabolism
MH  - DNA, Bacterial/metabolism
PMC - PMC9885476
OTO - NOTNLM
OT  - DNA-binding protein from starved cells (Dps)
OT  - Mossbauer spectroscopy
OT  - N-terminal tail extensions
OT  - biological small-angle X-ray scattering
OT  - conformational dynamics
OT  - metal binding
OT  - mini-ferritin
COIS- The authors declare no conflict of interest.
EDAT- 2023/01/21 06:00
MHDA- 2023/02/01 06:00
PMCR- 2023/02/01
CRDT- 2023/01/20 01:02
PHST- 2023/01/10 00:00 [revised]
PHST- 2022/09/11 00:00 [received]
PHST- 2023/01/14 00:00 [accepted]
PHST- 2023/01/21 06:00 [pubmed]
PHST- 2023/02/01 06:00 [medline]
PHST- 2023/01/20 01:02 [entrez]
PHST- 2023/02/01 00:00 [pmc-release]
AID - PRO4567 [pii]
AID - 10.1002/pro.4567 [doi]
PST - ppublish
SO  - Protein Sci. 2023 Feb;32(2):e4567. doi: 10.1002/pro.4567.