Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer

Autores
Bromberg, Yana; Aptekmann, Ariel; Mahlich, Yannick; Cook, Linda; Senn, Stefan; Miller, Maximillian; Nanda, Vikas; Ferreiro, Diego; Falkowski, Paul G.
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Biological redox reactions drive planetary biogeochemical cycles. Using a novel, structure-guided sequence analysis of proteins, we explored the patterns of evolution of enzymes responsible for these reactions. Our analysis reveals that the folds that bind transition metal?containing ligands have similar structural geometry and amino acid sequences across the full diversity of proteins. Similarity across folds reflects the availability of key transition metals over geological time and strongly suggests that transition metal?ligand binding had a small number of common peptide origins. We observe that structures central to our similarity network come primarily from oxidoreductases, suggesting that ancestral peptides may have also facilitated electron transfer reactions. Last, our results reveal that the earliest biologically functional peptides were likely available before the assembly of fully functional protein domains over 3.8 billion years ago.
Fil: Bromberg, Yana. Rutgers University; Estados Unidos
Fil: Aptekmann, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Mahlich, Yannick. Rutgers University; Estados Unidos
Fil: Cook, Linda. University of Princeton; Estados Unidos
Fil: Senn, Stefan. Rutgers University; Estados Unidos
Fil: Miller, Maximillian. Rutgers University; Estados Unidos
Fil: Nanda, Vikas. Rutgers University; Estados Unidos
Fil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Falkowski, Paul G.. Rutgers University; Estados Unidos
Materia
peptides
metal binding
origin of life
evolution
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/214840
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Quantifying structural relationships of metal-binding sites suggests origins of biological electron transferBromberg, YanaAptekmann, ArielMahlich, YannickCook, LindaSenn, StefanMiller, MaximillianNanda, VikasFerreiro, DiegoFalkowski, Paul G.peptidesmetal bindingorigin of lifeevolutionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Biological redox reactions drive planetary biogeochemical cycles. Using a novel, structure-guided sequence analysis of proteins, we explored the patterns of evolution of enzymes responsible for these reactions. Our analysis reveals that the folds that bind transition metal?containing ligands have similar structural geometry and amino acid sequences across the full diversity of proteins. Similarity across folds reflects the availability of key transition metals over geological time and strongly suggests that transition metal?ligand binding had a small number of common peptide origins. We observe that structures central to our similarity network come primarily from oxidoreductases, suggesting that ancestral peptides may have also facilitated electron transfer reactions. Last, our results reveal that the earliest biologically functional peptides were likely available before the assembly of fully functional protein domains over 3.8 billion years ago.Fil: Bromberg, Yana. Rutgers University; Estados UnidosFil: Aptekmann, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Mahlich, Yannick. Rutgers University; Estados UnidosFil: Cook, Linda. University of Princeton; Estados UnidosFil: Senn, Stefan. Rutgers University; Estados UnidosFil: Miller, Maximillian. Rutgers University; Estados UnidosFil: Nanda, Vikas. Rutgers University; Estados UnidosFil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Falkowski, Paul G.. Rutgers University; Estados UnidosScience Advances is the American Association for the Advancement of Science2022-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/214840Bromberg, Yana; Aptekmann, Ariel; Mahlich, Yannick; Cook, Linda; Senn, Stefan; et al.; Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer; Science Advances is the American Association for the Advancement of Science; Science Advances; 8; 2; 1-2022; 1-142375-2548CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.science.org/doi/10.1126/sciadv.abj3984info:eu-repo/semantics/altIdentifier/doi/10.1126/sciadv.abj3984info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-03-31T14:45:38Zoai:ri.conicet.gov.ar:11336/214840instacron: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:34982026-03-31 14:45:38.424CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
title Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
spellingShingle Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
Bromberg, Yana
peptides
metal binding
origin of life
evolution
title_short Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
title_full Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
title_fullStr Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
title_full_unstemmed Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
title_sort Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
dc.creator.none.fl_str_mv Bromberg, Yana
Aptekmann, Ariel
Mahlich, Yannick
Cook, Linda
Senn, Stefan
Miller, Maximillian
Nanda, Vikas
Ferreiro, Diego
Falkowski, Paul G.
author Bromberg, Yana
author_facet Bromberg, Yana
Aptekmann, Ariel
Mahlich, Yannick
Cook, Linda
Senn, Stefan
Miller, Maximillian
Nanda, Vikas
Ferreiro, Diego
Falkowski, Paul G.
author_role author
author2 Aptekmann, Ariel
Mahlich, Yannick
Cook, Linda
Senn, Stefan
Miller, Maximillian
Nanda, Vikas
Ferreiro, Diego
Falkowski, Paul G.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv peptides
metal binding
origin of life
evolution
topic peptides
metal binding
origin of life
evolution
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Biological redox reactions drive planetary biogeochemical cycles. Using a novel, structure-guided sequence analysis of proteins, we explored the patterns of evolution of enzymes responsible for these reactions. Our analysis reveals that the folds that bind transition metal?containing ligands have similar structural geometry and amino acid sequences across the full diversity of proteins. Similarity across folds reflects the availability of key transition metals over geological time and strongly suggests that transition metal?ligand binding had a small number of common peptide origins. We observe that structures central to our similarity network come primarily from oxidoreductases, suggesting that ancestral peptides may have also facilitated electron transfer reactions. Last, our results reveal that the earliest biologically functional peptides were likely available before the assembly of fully functional protein domains over 3.8 billion years ago.
Fil: Bromberg, Yana. Rutgers University; Estados Unidos
Fil: Aptekmann, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Mahlich, Yannick. Rutgers University; Estados Unidos
Fil: Cook, Linda. University of Princeton; Estados Unidos
Fil: Senn, Stefan. Rutgers University; Estados Unidos
Fil: Miller, Maximillian. Rutgers University; Estados Unidos
Fil: Nanda, Vikas. Rutgers University; Estados Unidos
Fil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Falkowski, Paul G.. Rutgers University; Estados Unidos
description Biological redox reactions drive planetary biogeochemical cycles. Using a novel, structure-guided sequence analysis of proteins, we explored the patterns of evolution of enzymes responsible for these reactions. Our analysis reveals that the folds that bind transition metal?containing ligands have similar structural geometry and amino acid sequences across the full diversity of proteins. Similarity across folds reflects the availability of key transition metals over geological time and strongly suggests that transition metal?ligand binding had a small number of common peptide origins. We observe that structures central to our similarity network come primarily from oxidoreductases, suggesting that ancestral peptides may have also facilitated electron transfer reactions. Last, our results reveal that the earliest biologically functional peptides were likely available before the assembly of fully functional protein domains over 3.8 billion years ago.
publishDate 2022
dc.date.none.fl_str_mv 2022-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/214840
Bromberg, Yana; Aptekmann, Ariel; Mahlich, Yannick; Cook, Linda; Senn, Stefan; et al.; Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer; Science Advances is the American Association for the Advancement of Science; Science Advances; 8; 2; 1-2022; 1-14
2375-2548
CONICET Digital
CONICET
url http://hdl.handle.net/11336/214840
identifier_str_mv Bromberg, Yana; Aptekmann, Ariel; Mahlich, Yannick; Cook, Linda; Senn, Stefan; et al.; Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer; Science Advances is the American Association for the Advancement of Science; Science Advances; 8; 2; 1-2022; 1-14
2375-2548
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.science.org/doi/10.1126/sciadv.abj3984
info:eu-repo/semantics/altIdentifier/doi/10.1126/sciadv.abj3984
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Science Advances is the American Association for the Advancement of Science
publisher.none.fl_str_mv Science Advances is the American Association for the Advancement of Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.822162

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