Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae)
- Autores
- Gatica Soria, Leonardo Martin; Ceriotti, Luis Federico; Sánchez Puerta, María Virginia
- Año de publicación
- 2021
- Idioma
- inglés
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- The intimate contact between the holoparasitic plant Lophophytum mirabile (Bal- anophoraceae) and its host plant (Mimosoideae, Fabaceae) facilitates the exchange of genetic information, increasing the frequency of horizontal gene transfer (HGT). Lophophytum has revealed the unprecedented acquisition of a large number of mi- tochondrial genes from its legume host that replaced the native homologs. These foreign genes are functional and encode proteins that form multi-subunit enzyme complexes together with proteins of nuclear origin. For all these reasons, Lophophy- tum is an interesting model to study the evolution of multiprotein complexes in the mitochondria, the impact of HGT in the nuclear genome, and its co-evolution with the mitochondrial genome. Given the presence of foreign mitochondrial proteins in June 22 5:00 PM Session 8Lophophytum, it is proposed that nuclear genes that encode proteins involved in these complexes are also foreign, minimizing the incompatibilities in the assembly and functioning of these multiprotein complexes. Multiple alignments were generated from nucleotide sequences of 25 angiosperms to infer the phylogenetic relationships of 75 nuclear genes (obtained from the Lophophytum transcriptome) involved the ox- idative phosphorylation system (OXPHOS) of Lophophytum. Maximum likelihood phylogenetic analyses were ran with RAxML 8.2.11 using GTRGAMMA models along with 1,000 rapid bootstrapping pseudo-replicates. To examine gene conver- sion events within genes we used Geneconv. Based on these results, we infer that 74 subunits are native and one is foreign (SDH3) as a result of HGT from mimosoid hosts. These results reflect that the OXPHOS of Lophophytum is exceptional due to the presence of foreign (mostly encoded in the mitochondrial genome) and native (mostly encoded in the nuclear genome) subunits, generating new questions about the evolution and physiology of this parasitic plant. It is possible that the interac- tions between native and foreign proteins do not generate incompatibilities in the assembly and functioning of OXPHOS due to the low rate of evolution of mitochon- drial genes in angiosperms. In contrast, the higher divergence among angiosperm nuclear genes would cause a negative effect on OXPHOS activity if foreign genes replace the native homologs.
Fil: Gatica Soria, Leonardo Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
Fil: Ceriotti, Luis Federico. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
Fil: Sánchez Puerta, María Virginia. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina
II Virtual Meeting of Systematics, Biogeography, and Evolution
Argentina
SBE meeting 2021's organizing committe - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/174932
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Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae)Gatica Soria, Leonardo MartinCeriotti, Luis FedericoSánchez Puerta, María Virginiahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The intimate contact between the holoparasitic plant Lophophytum mirabile (Bal- anophoraceae) and its host plant (Mimosoideae, Fabaceae) facilitates the exchange of genetic information, increasing the frequency of horizontal gene transfer (HGT). Lophophytum has revealed the unprecedented acquisition of a large number of mi- tochondrial genes from its legume host that replaced the native homologs. These foreign genes are functional and encode proteins that form multi-subunit enzyme complexes together with proteins of nuclear origin. For all these reasons, Lophophy- tum is an interesting model to study the evolution of multiprotein complexes in the mitochondria, the impact of HGT in the nuclear genome, and its co-evolution with the mitochondrial genome. Given the presence of foreign mitochondrial proteins in June 22 5:00 PM Session 8Lophophytum, it is proposed that nuclear genes that encode proteins involved in these complexes are also foreign, minimizing the incompatibilities in the assembly and functioning of these multiprotein complexes. Multiple alignments were generated from nucleotide sequences of 25 angiosperms to infer the phylogenetic relationships of 75 nuclear genes (obtained from the Lophophytum transcriptome) involved the ox- idative phosphorylation system (OXPHOS) of Lophophytum. Maximum likelihood phylogenetic analyses were ran with RAxML 8.2.11 using GTRGAMMA models along with 1,000 rapid bootstrapping pseudo-replicates. To examine gene conver- sion events within genes we used Geneconv. Based on these results, we infer that 74 subunits are native and one is foreign (SDH3) as a result of HGT from mimosoid hosts. These results reflect that the OXPHOS of Lophophytum is exceptional due to the presence of foreign (mostly encoded in the mitochondrial genome) and native (mostly encoded in the nuclear genome) subunits, generating new questions about the evolution and physiology of this parasitic plant. It is possible that the interac- tions between native and foreign proteins do not generate incompatibilities in the assembly and functioning of OXPHOS due to the low rate of evolution of mitochon- drial genes in angiosperms. In contrast, the higher divergence among angiosperm nuclear genes would cause a negative effect on OXPHOS activity if foreign genes replace the native homologs.Fil: Gatica Soria, Leonardo Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; ArgentinaFil: Ceriotti, Luis Federico. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; ArgentinaFil: Sánchez Puerta, María Virginia. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; ArgentinaII Virtual Meeting of Systematics, Biogeography, and EvolutionArgentinaSBE meeting 2021's organizing committeSBE Meeting 2021's Organizing Committee2021info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/174932Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae); II Virtual Meeting of Systematics, Biogeography, and Evolution; Argentina; 2021; 1-4CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://denisjacobmachado.wixsite.com/sbe21Internacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:56:27Zoai:ri.conicet.gov.ar:11336/174932instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:56:27.685CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae) |
title |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae) |
spellingShingle |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae) Gatica Soria, Leonardo Martin |
title_short |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae) |
title_full |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae) |
title_fullStr |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae) |
title_full_unstemmed |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae) |
title_sort |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae) |
dc.creator.none.fl_str_mv |
Gatica Soria, Leonardo Martin Ceriotti, Luis Federico Sánchez Puerta, María Virginia |
author |
Gatica Soria, Leonardo Martin |
author_facet |
Gatica Soria, Leonardo Martin Ceriotti, Luis Federico Sánchez Puerta, María Virginia |
author_role |
author |
author2 |
Ceriotti, Luis Federico Sánchez Puerta, María Virginia |
author2_role |
author author |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The intimate contact between the holoparasitic plant Lophophytum mirabile (Bal- anophoraceae) and its host plant (Mimosoideae, Fabaceae) facilitates the exchange of genetic information, increasing the frequency of horizontal gene transfer (HGT). Lophophytum has revealed the unprecedented acquisition of a large number of mi- tochondrial genes from its legume host that replaced the native homologs. These foreign genes are functional and encode proteins that form multi-subunit enzyme complexes together with proteins of nuclear origin. For all these reasons, Lophophy- tum is an interesting model to study the evolution of multiprotein complexes in the mitochondria, the impact of HGT in the nuclear genome, and its co-evolution with the mitochondrial genome. Given the presence of foreign mitochondrial proteins in June 22 5:00 PM Session 8Lophophytum, it is proposed that nuclear genes that encode proteins involved in these complexes are also foreign, minimizing the incompatibilities in the assembly and functioning of these multiprotein complexes. Multiple alignments were generated from nucleotide sequences of 25 angiosperms to infer the phylogenetic relationships of 75 nuclear genes (obtained from the Lophophytum transcriptome) involved the ox- idative phosphorylation system (OXPHOS) of Lophophytum. Maximum likelihood phylogenetic analyses were ran with RAxML 8.2.11 using GTRGAMMA models along with 1,000 rapid bootstrapping pseudo-replicates. To examine gene conver- sion events within genes we used Geneconv. Based on these results, we infer that 74 subunits are native and one is foreign (SDH3) as a result of HGT from mimosoid hosts. These results reflect that the OXPHOS of Lophophytum is exceptional due to the presence of foreign (mostly encoded in the mitochondrial genome) and native (mostly encoded in the nuclear genome) subunits, generating new questions about the evolution and physiology of this parasitic plant. It is possible that the interac- tions between native and foreign proteins do not generate incompatibilities in the assembly and functioning of OXPHOS due to the low rate of evolution of mitochon- drial genes in angiosperms. In contrast, the higher divergence among angiosperm nuclear genes would cause a negative effect on OXPHOS activity if foreign genes replace the native homologs. Fil: Gatica Soria, Leonardo Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina Fil: Ceriotti, Luis Federico. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina Fil: Sánchez Puerta, María Virginia. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Biología Agrícola de Mendoza. Universidad Nacional de Cuyo. Facultad de Ciencias Agrarias. Instituto de Biología Agrícola de Mendoza; Argentina II Virtual Meeting of Systematics, Biogeography, and Evolution Argentina SBE meeting 2021's organizing committe |
description |
The intimate contact between the holoparasitic plant Lophophytum mirabile (Bal- anophoraceae) and its host plant (Mimosoideae, Fabaceae) facilitates the exchange of genetic information, increasing the frequency of horizontal gene transfer (HGT). Lophophytum has revealed the unprecedented acquisition of a large number of mi- tochondrial genes from its legume host that replaced the native homologs. These foreign genes are functional and encode proteins that form multi-subunit enzyme complexes together with proteins of nuclear origin. For all these reasons, Lophophy- tum is an interesting model to study the evolution of multiprotein complexes in the mitochondria, the impact of HGT in the nuclear genome, and its co-evolution with the mitochondrial genome. Given the presence of foreign mitochondrial proteins in June 22 5:00 PM Session 8Lophophytum, it is proposed that nuclear genes that encode proteins involved in these complexes are also foreign, minimizing the incompatibilities in the assembly and functioning of these multiprotein complexes. Multiple alignments were generated from nucleotide sequences of 25 angiosperms to infer the phylogenetic relationships of 75 nuclear genes (obtained from the Lophophytum transcriptome) involved the ox- idative phosphorylation system (OXPHOS) of Lophophytum. Maximum likelihood phylogenetic analyses were ran with RAxML 8.2.11 using GTRGAMMA models along with 1,000 rapid bootstrapping pseudo-replicates. To examine gene conver- sion events within genes we used Geneconv. Based on these results, we infer that 74 subunits are native and one is foreign (SDH3) as a result of HGT from mimosoid hosts. These results reflect that the OXPHOS of Lophophytum is exceptional due to the presence of foreign (mostly encoded in the mitochondrial genome) and native (mostly encoded in the nuclear genome) subunits, generating new questions about the evolution and physiology of this parasitic plant. It is possible that the interac- tions between native and foreign proteins do not generate incompatibilities in the assembly and functioning of OXPHOS due to the low rate of evolution of mitochon- drial genes in angiosperms. In contrast, the higher divergence among angiosperm nuclear genes would cause a negative effect on OXPHOS activity if foreign genes replace the native homologs. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/conferenceObject Reunión Book http://purl.org/coar/resource_type/c_5794 info:ar-repo/semantics/documentoDeConferencia |
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publishedVersion |
format |
conferenceObject |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/174932 Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae); II Virtual Meeting of Systematics, Biogeography, and Evolution; Argentina; 2021; 1-4 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/174932 |
identifier_str_mv |
Native and foreign proteins conform the OXPHOS complexes of Lophophytum mirabile (Balanophoraceae); II Virtual Meeting of Systematics, Biogeography, and Evolution; Argentina; 2021; 1-4 CONICET Digital CONICET |
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eng |
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eng |
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Internacional |
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SBE Meeting 2021's Organizing Committee |
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SBE Meeting 2021's Organizing Committee |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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