000128050 001__ 128050
000128050 005__ 20240319081012.0
000128050 0247_ $$2doi$$a10.1093/mtomcs/mfac077
000128050 0248_ $$2sideral$$a131395
000128050 037__ $$aART-2022-131395
000128050 041__ $$aeng
000128050 100__ $$0(orcid)0000-0002-1960-2672$$aSarasa-Buisan, Cristina$$uUniversidad de Zaragoza
000128050 245__ $$aMetal binding and oligomerization properties of FurC (PerR) from Anabaena sp. PCC7120: an additional layer of regulation?
000128050 260__ $$c2022
000128050 5060_ $$aAccess copy available to the general public$$fUnrestricted
000128050 5203_ $$aMetal and redox homeostasis in cyanobacteria is tightly controlled to preserve the photosynthetic machinery from mismetallation and minimize cell damage. This control is mainly taken by FUR (ferric uptake regulation) proteins. FurC works as the PerR (peroxide response) paralog in Anabaena sp. PCC7120. Despite its importance, this regulator remained poorly characterized. Although FurC lacks the typical CXXC motifs present in FUR proteins, it contains a tightly bound zinc per subunit. FurC: Zn stoichiometrically binds zinc and manganese in a second site, manganese being more efficient in the binding of FurC: Zn to its DNA target PprxA. Oligomerization analyses of FurC: Zn evidence the occurrence of different aggregates ranging from dimers to octamers. Notably, intermolecular disulfide bonds are not involved in FurC: Zn dimerization, dimer being the most reduced form of the protein. Oligomerization of dimers occurs upon oxidation of thiols by H2O2 or diamide and can be reversed by 1,4-Dithiothreitol (DTT). Irreversible inactivation of the regulator occurs by metal catalyzed oxidation promoted by ferrous iron. However, inactivation upon oxidation with H2O2 in the absence of iron was reverted by addition of DTT. Comparison of models for FurC: Zn dimers and tetramers obtained using AlphaFold Colab and SWISS-MODEL allowed to infer the residues forming both metal-binding sites and to propose the involvement of Cys86 in reversible tetramer formation. Our results decipher the existence of two levels of inactivation of FurC: Zn of Anabaena sp. PCC7120, a reversible one through disulfide-formed FurC: Zn tetramers and the irreversible metal catalyzed oxidation. This additional reversible regulation may be specific of cyanobacteria.
000128050 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E35-20R$$9info:eu-repo/grantAgreement/ES/MCIU/PID2019-104889GB-I00
000128050 540__ $$9info:eu-repo/semantics/openAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000128050 590__ $$a3.4$$b2022
000128050 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b158 / 285 = 0.554$$c2022$$dQ3$$eT2
000128050 592__ $$a0.765$$b2022
000128050 593__ $$aMetals and Alloys$$c2022$$dQ1
000128050 593__ $$aChemistry (miscellaneous)$$c2022$$dQ1
000128050 593__ $$aMedicine (miscellaneous)$$c2022$$dQ2
000128050 593__ $$aBiomaterials$$c2022$$dQ2
000128050 593__ $$aBiochemistry$$c2022$$dQ2
000128050 593__ $$aBiophysics$$c2022$$dQ2
000128050 594__ $$a8.4$$b2022
000128050 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000128050 700__ $$aEmonot, Etienne
000128050 700__ $$0(orcid)0000-0001-9047-0046$$aMartínez-Júlvez, Marta$$uUniversidad de Zaragoza
000128050 700__ $$0(orcid)0000-0001-6435-3540$$aSevilla, Emma$$uUniversidad de Zaragoza
000128050 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, Adrián$$uUniversidad de Zaragoza
000128050 700__ $$aCrouzy, Serge
000128050 700__ $$0(orcid)0000-0002-8181-2689$$aBes, M Teresa$$uUniversidad de Zaragoza
000128050 700__ $$aMichaud-Soret, Isabelle
000128050 700__ $$0(orcid)0000-0001-8644-4574$$aFillat, María F$$uUniversidad de Zaragoza
000128050 7102_ $$11002$$2412$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Fisiología Vegetal
000128050 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000128050 773__ $$g14, 10 (2022)$$pMetallomics$$tMetallomics$$x1756-5901
000128050 8564_ $$s391941$$uhttps://zaguan.unizar.es/record/128050/files/texto_completo.pdf$$yPostprint
000128050 8564_ $$s1308612$$uhttps://zaguan.unizar.es/record/128050/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000128050 909CO $$ooai:zaguan.unizar.es:128050$$particulos$$pdriver
000128050 951__ $$a2024-03-18-15:17:00
000128050 980__ $$aARTICLE