The biosynthesis of flavin cofactors in Listeria monocytogenes

55 Pags.- 7 Figs.- Suppl. Mat. (9 Figs.- 5 Tabls.). The definitive version is available at: https://www.sciencedirect.com/science/journal/00222836

Bibliographic Details
Authors: Sebastián Valverde, María, Arilla-Luna, Sonia, Bellalou, Jacques, Yruela Guerrero, Inmaculada, Medina Trullenque, Milagros
Format: article
Status:Versión aceptada para publicación
Publication Date:2019
Country:España
Institution:Consejo Superior de Investigaciones Científicas (CSIC)
Repository:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/185106
Online Access:http://hdl.handle.net/10261/185106
Access Level:Open access
Keyword:FMN and FAD biosynthesis
riboflavin kinase
FMN:ATP adenylyltransferase
FAD synthase
Listeria monocytogenes
id ES_e20757c282985ddf5eb81e1c0fdef3d3
oai_identifier_str oai:digital.csic.es:10261/185106
network_acronym_str ES
network_name_str España
repository_id_str
spelling The biosynthesis of flavin cofactors in Listeria monocytogenesSebastián Valverde, MaríaArilla-Luna, SoniaBellalou, JacquesYruela Guerrero, InmaculadaMedina Trullenque, MilagrosFMN and FAD biosynthesisriboflavin kinaseFMN:ATP adenylyltransferaseFAD synthaseListeria monocytogenes55 Pags.- 7 Figs.- Suppl. Mat. (9 Figs.- 5 Tabls.). The definitive version is available at: https://www.sciencedirect.com/science/journal/00222836Listeria monocytogenes is riboflavin auxotrophic, but it has two genes envisaged to transform riboflavin into FMN and FAD after its uptaked by specialized transporters. One encodes a bifunctional type I FAD synthase (FADS, herein LmFADS-1), while the other produces a protein similar to type I at the FMN:ATP adenylyltransferase (FMNAT) site but with a shorter C-terminal that lacks any riboflavin kinase (RFK) motif. This second protein is rare among bacteria and has been named FADS type II (LmFADS-2). Here we present a biochemical and biophysical study of LmFADS-1 and LmFADS-2 by integrating kinetic and thermodynamic data together with sequence and structural prediction methods to evaluate their occurrence in Listeria, as well as their function and molecular properties. Despite LmFADS-1 similarities to other type I FADSs, (i) its RFK activity has not riboflavin substrate inhibition and occurs under reducing and oxidizing conditions, (ii) its FMNAT activity requires strong reducing environment, and (iii) binding of reaction products, but not substrates, favors binding of the second ligand. LmFADS-2 produces FAD under oxidizing and reducing environments, but its C-terminus module function remains unknown. Listeria species conserve both FADSs, being sequence identity high within L. monocytogenes strains. Our data exemplify alternative strategies for FMN and FAD biosynthesis and homeostasis, envisaging that in Listeria two FADSs might be required to fulfill the supply of flavin cofactors under niches that can go from saprophytism to virulence. As FADSs are attractive antimicrobial targets, understanding of FADSs traits in different species is essential to help in the discovery of specific antimicrobials.This work has been supported by the Spanish Ministry of Economy, Industry and Competitiveness (MINECO) (BIO2016-75183-P AEI/FEDER, UE to M.M.) and the Government of Aragón-FEDER (E35_17R to M.M.).Peer reviewedElsevierMinisterio de Economía, Industria y Competitividad (España)European CommissionGobierno de AragónYruela Guerrero, Inmaculada [0000-0003-3608-4720]Medina Trullenque, Milagros [0000-0001-8743-0182]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201920192019info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/185106reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.1016/j.jmb.2019.05.029Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1851062026-05-22T06:33:51Z
dc.title.none.fl_str_mv The biosynthesis of flavin cofactors in Listeria monocytogenes
title The biosynthesis of flavin cofactors in Listeria monocytogenes
spellingShingle The biosynthesis of flavin cofactors in Listeria monocytogenes
Sebastián Valverde, María
FMN and FAD biosynthesis
riboflavin kinase
FMN:ATP adenylyltransferase
FAD synthase
Listeria monocytogenes
title_short The biosynthesis of flavin cofactors in Listeria monocytogenes
title_full The biosynthesis of flavin cofactors in Listeria monocytogenes
title_fullStr The biosynthesis of flavin cofactors in Listeria monocytogenes
title_full_unstemmed The biosynthesis of flavin cofactors in Listeria monocytogenes
title_sort The biosynthesis of flavin cofactors in Listeria monocytogenes
dc.creator.none.fl_str_mv Sebastián Valverde, María
Arilla-Luna, Sonia
Bellalou, Jacques
Yruela Guerrero, Inmaculada
Medina Trullenque, Milagros
author Sebastián Valverde, María
author_facet Sebastián Valverde, María
Arilla-Luna, Sonia
Bellalou, Jacques
Yruela Guerrero, Inmaculada
Medina Trullenque, Milagros
author_role author
author2 Arilla-Luna, Sonia
Bellalou, Jacques
Yruela Guerrero, Inmaculada
Medina Trullenque, Milagros
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía, Industria y Competitividad (España)
European Commission
Gobierno de Aragón
Yruela Guerrero, Inmaculada [0000-0003-3608-4720]
Medina Trullenque, Milagros [0000-0001-8743-0182]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv FMN and FAD biosynthesis
riboflavin kinase
FMN:ATP adenylyltransferase
FAD synthase
Listeria monocytogenes
topic FMN and FAD biosynthesis
riboflavin kinase
FMN:ATP adenylyltransferase
FAD synthase
Listeria monocytogenes
description 55 Pags.- 7 Figs.- Suppl. Mat. (9 Figs.- 5 Tabls.). The definitive version is available at: https://www.sciencedirect.com/science/journal/00222836
publishDate 2019
dc.date.none.fl_str_mv 2019
2019
2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/185106
url http://hdl.handle.net/10261/185106
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1016/j.jmb.2019.05.029
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869422347739463680
score 15,811543

Similar Items