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The SOUL family of heme-binding proteins: structure and function 15 years later

2021Journal article Restricted access
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dc.contributor.authorGoodfellow, Brian J.
dc.contributor.authorFreire, Filipe
dc.contributor.authorCarvalho, Ana Luísa
dc.contributor.authorAveiro, Susana
dc.contributor.authorCharbonnier, Peggy
dc.contributor.authorMoulis, Jean-Marc
dc.contributor.authorDelgado, Leonildo
dc.contributor.authorFerreira, Gloria C.
dc.contributor.authorRodrigues, João E.
dc.contributor.authorPoussin-Courmontagne, Pierre
dc.contributor.authorBirck, Catherine
dc.contributor.authorMcEwen, Alastair
dc.contributor.authorMacedo, Anjos L.
dc.date.accessioned2021-11-03T20:38:33Z
dc.date.available2021-11-03T20:38:33Z
dc.date.issued2021
dc.description.abstractThe SOUL, or heme-binding protein HBP/SOUL, family represents a group of evolutionary conserved putative heme-binding proteins that contains a number of members in animal, plant and bacterial species. The structures of the murine form of HEBP1, or p22HBP, and the human form of HEBP2, or SOUL, have been determined in 2006 and 2011 respectively. In this work we discuss the structures of HEBP1 and HEBP2 in light of new X-ray data for heme bound murine HEBP1. The interaction between tetrapyrroles and HEBP1, initially proven to be hydrophobic in nature, was thought to also involve electrostatic interactions between heme propionate groups and positively charged amino acid side chains. However, the new X-ray structure, and results from murine HEBP1 variants and human HEBP1, confirm the hydrophobic nature of the heme-HEBP1 interaction, resulting in K-d values in the low nanomolar range, and rules out any electrostatic stabilization. Results from NMR relaxation time measurements for human HEBP1 describe a rigid globular protein with no change in motional regime upon heme binding. X-ray structures deposited in the PDB for human HEBP2 are very similar to each other and to the new heme-bound murine HEBP1 X-ray structure (backbone rmsd ca. 1 A). Results from a HSQC spectrum centred on the histidine side chain N delta-proton region for HEBP2 confirm that HEBP2 does not bind heme via H42 as no chemical shift differences were observed upon heme addition for backbone NH and Nd protons. A survey of the functions attributed to HEBP1 and HEBP2 over the last 20 years span a wide range of cellular pathways. Interestingly, many of them are specific to higher eukaryotes, particularly mammals and a potential link between heme release under oxidative stress and human HEBP1 is also examined using recent data. However, at the present moment, trying to relate function to the involvement of heme or tetrapyrrole binding, specifically, makes little sense with our current biological knowledge and can only be applied to HEBP1, as HEBP2 does not interact with heme. We suggest that it may not be justified to call this very small family of proteins, heme-binding proteins. The family may be more correctly called "the SOUL family of proteins related to cellular fate" as, even though only HEBP1 binds heme tightly, both proteins may be involved in cell survival and/or proliferation.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1016/j.ccr.2021.214189pt_PT
dc.identifier.issn0010-8545
dc.identifier.urihttp://hdl.handle.net/10400.1/17286
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relationESTUDO INTEGRADO POR RMN E CRISTALOGRAFIA DE RAIOS-X NA ANÁLISE DAS INTERACÇÕES MOLECULARES EM PROTEÍNAS DE LIGAÇÃO AO HEMO
dc.relationSTRUCTURAL AND FUNCTIONAL STUDIES OF SITE-SPECIFIC MUTANTS OF THE P22 HEME-BINDING/TRANSPORTING PROTEIN
dc.relationApplied Molecular Biosciences Unit
dc.relationInstitute for Health and Bioeconomy
dc.relationCICECO-Aveiro Institute of Materials
dc.subjectHEBP1pt_PT
dc.subjectHEBP2pt_PT
dc.subjectSOUL proteinpt_PT
dc.subjectNMR spectroscopypt_PT
dc.subjectX-ray crystallographypt_PT
dc.subjectFunctionpt_PT
dc.subjectStructurept_PT
dc.titleThe SOUL family of heme-binding proteins: structure and function 15 years laterpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleESTUDO INTEGRADO POR RMN E CRISTALOGRAFIA DE RAIOS-X NA ANÁLISE DAS INTERACÇÕES MOLECULARES EM PROTEÍNAS DE LIGAÇÃO AO HEMO
oaire.awardTitleSTRUCTURAL AND FUNCTIONAL STUDIES OF SITE-SPECIFIC MUTANTS OF THE P22 HEME-BINDING/TRANSPORTING PROTEIN
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleInstitute for Health and Bioeconomy
oaire.awardTitleCICECO-Aveiro Institute of Materials
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F30239%2F2006/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F64519%2F2009/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876-PPCDTI/PTDC%2FQUI%2F64203%2F2006/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/LA%2FP%2F0140%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50011%2F2020/PT
oaire.citation.startPage214189pt_PT
oaire.citation.titleCoordination Chemistry Reviewspt_PT
oaire.citation.volume448pt_PT
oaire.fundingStream5876-PPCDTI
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
person.familyNameAveiro
person.givenNameSusana
person.identifier.ciencia-idD312-07B4-DA74
person.identifier.orcid0000-0002-6651-3226
project.funder.identifierhttp://doi.org/10.13039/501100001871
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project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
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