Publicação
Dps from Deinococcus radiodurans : oligomeric forms of Dps1 with distinct cellular functions and Dps2 involved in metal storage
| dc.contributor.author | Santos, Sandra P. | |
| dc.contributor.author | Mitchell, Edward P. | |
| dc.contributor.author | Franquelim, Henri G. | |
| dc.contributor.author | Castanho, Miguel A. R. B. | |
| dc.contributor.author | Abreu, Isabel A. | |
| dc.contributor.author | Romão, Célia V. | |
| dc.date.accessioned | 2016-03-30T11:22:27Z | |
| dc.date.available | 2016-03-30T11:22:27Z | |
| dc.date.issued | 2015 | |
| dc.description | © 2015 FEBS | pt_PT |
| dc.description.abstract | The DNA binding proteins from starved cells from Deinococcus radiodurans, Dps1-DR2263 and Dps2-DRB0092, have a common overall structure of hollow spherical dodecamers. Their involvement in the homeostasis of intracellular metal and DNA protection was addressed. Our results show that DrDps proteins are able to oxidize ferrous to ferric iron by oxygen or hydrogen peroxide. The iron stored inside the hollow sphere cavity is fully released. Furthermore, these proteins are able to store and release manganese, suggesting they can play a role in manganese homeostasis as well. The interaction of DrDps with DNA was also addressed. Even though DrDps1 binds both linear and coiled DNA, DrDps2 preferentially binds to coiled DNA, forming different protein–DNA complexes, as clearly shown by atomic force microscopy. DrDps1 (dimer and dodecamer) and DrDps2 can protect DNA against reactive oxygen species, although the protection occurs at different Fe to protein ratios. The difference between DrDps could be the result of the DrDps1 higher iron oxidation rate in the presence of hydrogen peroxide and its higher affinity to bind DNA than in DrDps2. Using cellular extracts obtained from D. radiodurans cultures, we showed that DrDps1 oligomers observed in in vitro conditions are also present in vivo. This indicates that DrDps1 has a structural dynamic plasticity that allows its oligomeric state to change between dimer, trimer and dodecamer. This in turn suggests the existence of a regulation mechanism that modulates the oligomer equilibrium and is dependent on growth stages and environmental conditions. | pt_PT |
| dc.description.sponsorship | This work was financed by Fundação para a Ciência e Tecnologia through the following Grants: PTDC/BIA-PRO/100365/2008 (C.V.R.), PTDC/QUI-BIQ/100007/2008 (I.A.A.) and PEst-OE/EQB/LA0004/2011. S.P.S. is recipient of PhD Grant PEst-OE/EQB/LA0004/2011. I.A.A. and C.V.R. are recipients of the grants SFRH/BPD/78314/2011 and SFRH/BPD/94050/2013, respectively. | pt_PT |
| dc.identifier.citation | FEBS Journal 282 (2015) 4307–4327 | pt_PT |
| dc.identifier.doi | doi:10.1111/febs.13420 | pt_PT |
| dc.identifier.issn | 1742-464X | |
| dc.identifier.uri | http://hdl.handle.net/10451/23164 | |
| dc.language.iso | eng | pt_PT |
| dc.peerreviewed | yes | pt_PT |
| dc.publisher | Wiley | pt_PT |
| dc.relation | Oxidative stress response mechanisms in Deinococcus radiodruans | |
| dc.relation.publisherversion | http://febs.onlinelibrary.wiley.com/hub/journal/10.1111/(ISSN)1742-4658/ | pt_PT |
| dc.subject | DNA | pt_PT |
| dc.subject | Manganese | pt_PT |
| dc.subject | Oligomeric state | pt_PT |
| dc.subject | Oxidative stress | pt_PT |
| dc.subject | Reactive oxygen species | pt_PT |
| dc.title | Dps from Deinococcus radiodurans : oligomeric forms of Dps1 with distinct cellular functions and Dps2 involved in metal storage | pt_PT |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.awardTitle | Oxidative stress response mechanisms in Deinococcus radiodruans | |
| oaire.awardURI | info:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-PRO%2F100365%2F2008/PT | |
| oaire.awardURI | info:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI-BIQ%2F100007%2F2008/PT | |
| oaire.awardURI | info:eu-repo/grantAgreement/FCT/SFRH/SFRH/BPD/78314/2011/PT | |
| oaire.awardURI | info:eu-repo/grantAgreement/FCT/SFRH/SFRH/BPD/94050/2013/PT | |
| oaire.citation.title | FEBS Journal | pt_PT |
| oaire.fundingStream | 3599-PPCDT | |
| oaire.fundingStream | 3599-PPCDT | |
| oaire.fundingStream | SFRH | |
| oaire.fundingStream | SFRH | |
| project.funder.identifier | http://doi.org/10.13039/501100001871 | |
| project.funder.identifier | http://doi.org/10.13039/501100001871 | |
| project.funder.identifier | http://doi.org/10.13039/501100001871 | |
| project.funder.identifier | http://doi.org/10.13039/501100001871 | |
| project.funder.name | Fundação para a Ciência e a Tecnologia | |
| project.funder.name | Fundação para a Ciência e a Tecnologia | |
| project.funder.name | Fundação para a Ciência e a Tecnologia | |
| project.funder.name | Fundação para a Ciência e a Tecnologia | |
| rcaap.rights | closedAccess | pt_PT |
| rcaap.type | article | pt_PT |
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