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

Autor: Jean-Marc Moulis, Susana S. Aveiro, Anjos L. Macedo, Gloria C. Ferreira, Ana Luísa Carvalho, Alastair G. McEwen, Leonildo Delgado, Brian J. Goodfellow, João E. Rodrigues, Filipe Freire, Peggy Charbonnier, Catherine Birck, Pierre Poussin-Courmontagne
Přispěvatelé: CICECO, Departamento de Química, Instituto de Biologia Experimental e Tecnológica (IBET), Instituto de Tecnologia Química e Biológica António Xavier (ITQB), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA), Unidade de Ciencias Biomoleculares Aplicadas (UCIBIO), Requimte, Departamento de Química (DQ), Faculdade de Ciências e Tecnologia = School of Science & Technology (FCT NOVA), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Faculdade de Ciências e Tecnologia = School of Science & Technology (FCT NOVA), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade do Porto-Departamento de Química (DQ), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade do Porto, GreenCoLab - Associação Oceano Verde, Universidade do Algarve, Métaux et Organes (MET&OR), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), Equity Analyst Biotech & Healthcare, Morsani College of Medicine [Tampa, USA], University of South Florida [Tampa] (USF), Center for Neuroscience and Cell Biology (CNC) (CNC), University of Coimbra [Portugal] (UC)-Neuroscience Research Domain, Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Universidade do Porto = University of Porto-Departamento de Química (DQ), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade do Porto = University of Porto-Departamento de Química (DQ), Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)-Universidade Nova de Lisboa = NOVA University Lisbon (NOVA)
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: Coordination Chemistry Reviews
Coordination Chemistry Reviews, Elsevier, 2021, 448, pp.214189. ⟨10.1016/j.ccr.2021.214189⟩
Coordination Chemistry Reviews, 2021, 448, pp.214189. ⟨10.1016/j.ccr.2021.214189⟩
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
ISSN: 0010-8545
Popis: International audience; The SOUL, or heme-binding protein HBP/SOUL, family represents a group of evolutionary conservedputative heme-binding proteins that contains a number of members in animal, plant and bacterial spe-cies. 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 boundmurine HEBP1. The interaction between tetrapyrroles and HEBP1, initially proven to be hydrophobic innature, was thought to also involve electrostatic interactions between heme propionate groups and pos-itively charged amino acid side chains. However, the new X-ray structure, and results from murine HEBP1variants and human HEBP1, confirm the hydrophobic nature of the heme-HEBP1 interaction, resulting inKdvalues in the low nanomolar range, and rules out any electrostatic stabilization. Results from NMRrelaxation time measurements for human HEBP1 describe a rigid globular protein with no change inmotional regime upon heme binding.X-ray structures deposited in the PDB for human HEBP2 are very similar to each other and to the newheme-bound murine HEBP1 X-ray structure (backbone rmsd ca. 1 Å). Results from a HSQC spectrum cen-tred on the histidine side chain Nd-proton region for HEBP2 confirm that HEBP2 does not bind heme viaH42 as no chemical shift differences were observed upon heme addition for backbone NH and Ndprotons.A survey of the functions attributed to HEBP1 and HEBP2 over the last 20 years span a wide range ofcellular pathways. Interestingly, many of them are specific to higher eukaryotes, particularly mammalsand a potential link between heme release under oxidative stress and human HEBP1 is also examinedusing recent data. However, at the present moment, trying to relate function to the involvement of hemehttps://doi.org/10.1016/j.ccr.2021.2141890010-8545/Ó2021 Elsevier B.V. All rights reserved.Abbreviations:HEBP1, Heme-binding protein 1 (or p22HBP); HEBP2, Heme-binding protein 2 (or SOUL); BH3, Bcl-2 homology 3; HSQC, heteronuclear single quantumcoherence spectroscopy; TROSY, transverse relaxation optimized spectroscopy; FQ, fluorescence quenching; PPIX, protoporphyrin IX; sGC, solubleGuanylyl Cyclase; hetNOE,heteronuclear nuclear Overhauser effect; rmsd, root mean squared deviation; BMRB, biological magnetic resonance bank; VAST, vector alignment search tool; MEL, murineerythroleukemia.⇑Corresponding authors.E-mail addresses:brian.goodfellow@ua.pt(B.J. Goodfellow),mdam@fct.unl(A.L. Macedo).Coordination Chemistry Reviews 448 (2021) 214189Contents lists available atScienceDirectCoordination Chemistry Reviewsjournal homepage: www.elsevier.com/locate/ccr
Databáze: OpenAIRE
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