Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium

The emergent human pathogen Mycoplasma genitalium, with one of the smallest genomes among cells capable of growing in axenic cultures, presents a flask-shaped morphology due to a protrusion of the cell membrane, known as the terminal organelle, that is involved in cell adhesion and motility and is a...

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Autores: Martinelli, Luca, Garcia-Morales, Luis, Querol Murillo, Enrique|||0000-0002-3658-3434, Fita, Ignacio|||0000-0002-7521-2679, Calisto, Bárbara Luísa Machado
Tipo de recurso: artículo
Fecha de publicación:2016
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:225198
Acceso en línea:https://ddd.uab.cat/record/225198
https://dx.doi.org/urn:doi:10.1371/journal.ppat.1005533
Access Level:acceso abierto
Palabra clave:Adhesins, Bacterial
Bacterial adhesion
Bacterial proteins
Cell adhesion
Cell movement
Cytoskeleton
Mutation
Mycoplasma genitalium
Organelles
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spelling Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitaliumMartinelli, LucaGarcia-Morales, LuisQuerol Murillo, Enrique|||0000-0002-3658-3434Fita, Ignacio|||0000-0002-7521-2679Calisto, Bárbara Luísa MachadoAdhesins, BacterialBacterial adhesionBacterial proteinsCell adhesionCell movementCytoskeletonMutationMycoplasma genitaliumOrganellesThe emergent human pathogen Mycoplasma genitalium, with one of the smallest genomes among cells capable of growing in axenic cultures, presents a flask-shaped morphology due to a protrusion of the cell membrane, known as the terminal organelle, that is involved in cell adhesion and motility and is an important virulence factor of this microorganism. The terminal organelle is supported by a cytoskeleton complex of about 300 nm in length that includes three substructures: the terminal button, the rod and the wheel complex. The crystal structure of the MG491 protein, a proposed component of the wheel complex, has been determined at ~3 Å resolution. MG491 subunits are composed of a 60-residue N-terminus, a central three-helix-bundle spanning about 150 residues and a C-terminal region that appears to be quite flexible and contains the region that interacts with MG200, another key protein of the terminal organelle. The MG491 molecule is a tetramer presenting a unique organization as a dimer of asymmetric pairs of subunits. The asymmetric arrangement results in two very different intersubunit interfaces between the central three-helix-bundle domains, which correlates with the formation of only ~50% of the intersubunit disulfide bridges of the single cysteine residue found in MG491 (Cys87). Moreover, M. genitalium cells with a point mutation in the MG491 gene causing the change of Cys87 to Ser present a drastic reduction in motility (as determined by microcinematography) and important alterations in morphology (as determined by electron microscopy), while preserving normal levels of the terminal organelle proteins. Other variants of MG491, designed also according to the structural information, altered significantly the motility and/or the cell morphology. Together, these results indicate that MG491 plays a key role in the functioning, organization and stabilization of the terminal organelle.Piñol Ribas, Jaume 22016-01-0120162016-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/225198https://dx.doi.org/urn:doi:10.1371/journal.ppat.1005533reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengMinisterio de Economía y Competitividad https://doi.org/10.13039/501100003329 BIO2013-48704RMinisterio de Economía y Competitividad https://doi.org/10.13039/501100003329 BFU2013-50176-EXMinisterio de Economía y Competitividad https://doi.org/10.13039/501100003329 BFU2012-36827open accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:2251982026-06-06T12:50:31Z
dc.title.none.fl_str_mv Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium
title Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium
spellingShingle Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium
Martinelli, Luca
Adhesins, Bacterial
Bacterial adhesion
Bacterial proteins
Cell adhesion
Cell movement
Cytoskeleton
Mutation
Mycoplasma genitalium
Organelles
title_short Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium
title_full Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium
title_fullStr Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium
title_full_unstemmed Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium
title_sort Structure-guided mutations in the terminal organelle protein MG491 cause major motility and morphologic alterations on mycoplasma genitalium
dc.creator.none.fl_str_mv Martinelli, Luca
Garcia-Morales, Luis
Querol Murillo, Enrique|||0000-0002-3658-3434
Fita, Ignacio|||0000-0002-7521-2679
Calisto, Bárbara Luísa Machado
author Martinelli, Luca
author_facet Martinelli, Luca
Garcia-Morales, Luis
Querol Murillo, Enrique|||0000-0002-3658-3434
Fita, Ignacio|||0000-0002-7521-2679
Calisto, Bárbara Luísa Machado
author_role author
author2 Garcia-Morales, Luis
Querol Murillo, Enrique|||0000-0002-3658-3434
Fita, Ignacio|||0000-0002-7521-2679
Calisto, Bárbara Luísa Machado
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Piñol Ribas, Jaume
dc.subject.none.fl_str_mv Adhesins, Bacterial
Bacterial adhesion
Bacterial proteins
Cell adhesion
Cell movement
Cytoskeleton
Mutation
Mycoplasma genitalium
Organelles
topic Adhesins, Bacterial
Bacterial adhesion
Bacterial proteins
Cell adhesion
Cell movement
Cytoskeleton
Mutation
Mycoplasma genitalium
Organelles
description The emergent human pathogen Mycoplasma genitalium, with one of the smallest genomes among cells capable of growing in axenic cultures, presents a flask-shaped morphology due to a protrusion of the cell membrane, known as the terminal organelle, that is involved in cell adhesion and motility and is an important virulence factor of this microorganism. The terminal organelle is supported by a cytoskeleton complex of about 300 nm in length that includes three substructures: the terminal button, the rod and the wheel complex. The crystal structure of the MG491 protein, a proposed component of the wheel complex, has been determined at ~3 Å resolution. MG491 subunits are composed of a 60-residue N-terminus, a central three-helix-bundle spanning about 150 residues and a C-terminal region that appears to be quite flexible and contains the region that interacts with MG200, another key protein of the terminal organelle. The MG491 molecule is a tetramer presenting a unique organization as a dimer of asymmetric pairs of subunits. The asymmetric arrangement results in two very different intersubunit interfaces between the central three-helix-bundle domains, which correlates with the formation of only ~50% of the intersubunit disulfide bridges of the single cysteine residue found in MG491 (Cys87). Moreover, M. genitalium cells with a point mutation in the MG491 gene causing the change of Cys87 to Ser present a drastic reduction in motility (as determined by microcinematography) and important alterations in morphology (as determined by electron microscopy), while preserving normal levels of the terminal organelle proteins. Other variants of MG491, designed also according to the structural information, altered significantly the motility and/or the cell morphology. Together, these results indicate that MG491 plays a key role in the functioning, organization and stabilization of the terminal organelle.
publishDate 2016
dc.date.none.fl_str_mv 2
2016-01-01
2016
2016-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/225198
https://dx.doi.org/urn:doi:10.1371/journal.ppat.1005533
url https://ddd.uab.cat/record/225198
https://dx.doi.org/urn:doi:10.1371/journal.ppat.1005533
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 BIO2013-48704R
Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 BFU2013-50176-EX
Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 BFU2012-36827
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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