Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions

Autores
Tossounian, Maria Armineh; Baczynska, Maria; Dalton, William; Newell, Charlie; Ma, Yilin; Das, Sayoni; Semelak, Jonathan Alexis; Estrin, Dario Ariel; Filonenko, Valeriy; Trujillo, Madia; Peak Chew, Sew Yeu; Skehel, Mark; Fraternali, Franca; Orengo, Christine; Gout, Ivan
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Coenzyme A (CoA) is a key cellular metabolite known for its diverse functions in metabolism and regulation of gene expression. CoA was recently shown to play an important antioxidant role under various cellular stress conditions by forming a disulfide bond with proteins, termed CoAlation. Using anti-CoA antibodies and liquid chromatography tandem mass spectrometry (LC-MS/MS) methodologies, CoAlated proteins were identified from various organisms/tissues/cell-lines under stress conditions. In this study, we integrated currently known CoAlated proteins into mammalian and bacterial datasets (CoAlomes), resulting in a total of 2093 CoAlated proteins (2862 CoAlation sites). Functional classification of these proteins showed that CoAlation is widespread among proteins involved in cellular metabolism, stress response and protein synthesis. Using 35 published CoAlated protein structures, we studied the stabilization interactions of each CoA segment (adenosine diphosphate (ADP) moiety and pantetheine tail) within the microenvironment of the modified cysteines. Alternating polar-non-polar residues, positively charged residues and hydrophobic interactions mainly stabilize the pantetheine tail, phosphate groups and the ADP moiety, respectively. A flexible nature of CoA is observed in examined structures, allowing it to adapt its conformation through interactions with residues surrounding the CoAlation site. Based on these findings, we propose three modes of CoA binding to proteins. Overall, this study summarizes currently available knowledge on CoAlated proteins, their functional distribution and CoA–protein stabilization interactions.
Fil: Tossounian, Maria Armineh. Colegio Universitario de Londres; Reino Unido
Fil: Baczynska, Maria. Colegio Universitario de Londres; Reino Unido
Fil: Dalton, William. Colegio Universitario de Londres; Reino Unido
Fil: Newell, Charlie. Colegio Universitario de Londres; Reino Unido
Fil: Ma, Yilin. Colegio Universitario de Londres; Reino Unido
Fil: Das, Sayoni. Colegio Universitario de Londres; Reino Unido
Fil: Semelak, Jonathan Alexis. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Filonenko, Valeriy. No especifíca;
Fil: Trujillo, Madia. Universidad de la Republica; Uruguay
Fil: Peak Chew, Sew Yeu. No especifíca;
Fil: Skehel, Mark. No especifíca;
Fil: Fraternali, Franca. No especifíca;
Fil: Orengo, Christine. Colegio Universitario de Londres; Reino Unido
Fil: Gout, Ivan. Colegio Universitario de Londres; Reino Unido
Materia
COA STABILIZATION INTERACTIONS
COALATION
COENZYME A
MIXED-DISULFIDE
OXIDATIVE STRESS
THIOLATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/210184
Acceder
id CONICETDig_3ca83837fe1066b3ead6921cde126e25
oai_identifier_str oai:ri.conicet.gov.ar:11336/210184
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Profiling the Site of Protein CoAlation and Coenzyme A Stabilization InteractionsTossounian, Maria ArminehBaczynska, MariaDalton, WilliamNewell, CharlieMa, YilinDas, SayoniSemelak, Jonathan AlexisEstrin, Dario ArielFilonenko, ValeriyTrujillo, MadiaPeak Chew, Sew YeuSkehel, MarkFraternali, FrancaOrengo, ChristineGout, IvanCOA STABILIZATION INTERACTIONSCOALATIONCOENZYME AMIXED-DISULFIDEOXIDATIVE STRESSTHIOLATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Coenzyme A (CoA) is a key cellular metabolite known for its diverse functions in metabolism and regulation of gene expression. CoA was recently shown to play an important antioxidant role under various cellular stress conditions by forming a disulfide bond with proteins, termed CoAlation. Using anti-CoA antibodies and liquid chromatography tandem mass spectrometry (LC-MS/MS) methodologies, CoAlated proteins were identified from various organisms/tissues/cell-lines under stress conditions. In this study, we integrated currently known CoAlated proteins into mammalian and bacterial datasets (CoAlomes), resulting in a total of 2093 CoAlated proteins (2862 CoAlation sites). Functional classification of these proteins showed that CoAlation is widespread among proteins involved in cellular metabolism, stress response and protein synthesis. Using 35 published CoAlated protein structures, we studied the stabilization interactions of each CoA segment (adenosine diphosphate (ADP) moiety and pantetheine tail) within the microenvironment of the modified cysteines. Alternating polar-non-polar residues, positively charged residues and hydrophobic interactions mainly stabilize the pantetheine tail, phosphate groups and the ADP moiety, respectively. A flexible nature of CoA is observed in examined structures, allowing it to adapt its conformation through interactions with residues surrounding the CoAlation site. Based on these findings, we propose three modes of CoA binding to proteins. Overall, this study summarizes currently available knowledge on CoAlated proteins, their functional distribution and CoA–protein stabilization interactions.Fil: Tossounian, Maria Armineh. Colegio Universitario de Londres; Reino UnidoFil: Baczynska, Maria. Colegio Universitario de Londres; Reino UnidoFil: Dalton, William. Colegio Universitario de Londres; Reino UnidoFil: Newell, Charlie. Colegio Universitario de Londres; Reino UnidoFil: Ma, Yilin. Colegio Universitario de Londres; Reino UnidoFil: Das, Sayoni. Colegio Universitario de Londres; Reino UnidoFil: Semelak, Jonathan Alexis. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Filonenko, Valeriy. No especifíca;Fil: Trujillo, Madia. Universidad de la Republica; UruguayFil: Peak Chew, Sew Yeu. No especifíca;Fil: Skehel, Mark. No especifíca;Fil: Fraternali, Franca. No especifíca;Fil: Orengo, Christine. Colegio Universitario de Londres; Reino UnidoFil: Gout, Ivan. Colegio Universitario de Londres; Reino UnidoMDPI2022-07info: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/11336/210184Tossounian, Maria Armineh; Baczynska, Maria; Dalton, William; Newell, Charlie; Ma, Yilin; et al.; Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions; MDPI; Antioxidants; 11; 7; 7-2022; 1-182076-3921CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/antiox11071362info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:21:06Zoai:ri.conicet.gov.ar:11336/210184instacron: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 10:21:06.894CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
title Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
spellingShingle Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
Tossounian, Maria Armineh
COA STABILIZATION INTERACTIONS
COALATION
COENZYME A
MIXED-DISULFIDE
OXIDATIVE STRESS
THIOLATION
title_short Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
title_full Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
title_fullStr Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
title_full_unstemmed Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
title_sort Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
dc.creator.none.fl_str_mv Tossounian, Maria Armineh
Baczynska, Maria
Dalton, William
Newell, Charlie
Ma, Yilin
Das, Sayoni
Semelak, Jonathan Alexis
Estrin, Dario Ariel
Filonenko, Valeriy
Trujillo, Madia
Peak Chew, Sew Yeu
Skehel, Mark
Fraternali, Franca
Orengo, Christine
Gout, Ivan
author Tossounian, Maria Armineh
author_facet Tossounian, Maria Armineh
Baczynska, Maria
Dalton, William
Newell, Charlie
Ma, Yilin
Das, Sayoni
Semelak, Jonathan Alexis
Estrin, Dario Ariel
Filonenko, Valeriy
Trujillo, Madia
Peak Chew, Sew Yeu
Skehel, Mark
Fraternali, Franca
Orengo, Christine
Gout, Ivan
author_role author
author2 Baczynska, Maria
Dalton, William
Newell, Charlie
Ma, Yilin
Das, Sayoni
Semelak, Jonathan Alexis
Estrin, Dario Ariel
Filonenko, Valeriy
Trujillo, Madia
Peak Chew, Sew Yeu
Skehel, Mark
Fraternali, Franca
Orengo, Christine
Gout, Ivan
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv COA STABILIZATION INTERACTIONS
COALATION
COENZYME A
MIXED-DISULFIDE
OXIDATIVE STRESS
THIOLATION
topic COA STABILIZATION INTERACTIONS
COALATION
COENZYME A
MIXED-DISULFIDE
OXIDATIVE STRESS
THIOLATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Coenzyme A (CoA) is a key cellular metabolite known for its diverse functions in metabolism and regulation of gene expression. CoA was recently shown to play an important antioxidant role under various cellular stress conditions by forming a disulfide bond with proteins, termed CoAlation. Using anti-CoA antibodies and liquid chromatography tandem mass spectrometry (LC-MS/MS) methodologies, CoAlated proteins were identified from various organisms/tissues/cell-lines under stress conditions. In this study, we integrated currently known CoAlated proteins into mammalian and bacterial datasets (CoAlomes), resulting in a total of 2093 CoAlated proteins (2862 CoAlation sites). Functional classification of these proteins showed that CoAlation is widespread among proteins involved in cellular metabolism, stress response and protein synthesis. Using 35 published CoAlated protein structures, we studied the stabilization interactions of each CoA segment (adenosine diphosphate (ADP) moiety and pantetheine tail) within the microenvironment of the modified cysteines. Alternating polar-non-polar residues, positively charged residues and hydrophobic interactions mainly stabilize the pantetheine tail, phosphate groups and the ADP moiety, respectively. A flexible nature of CoA is observed in examined structures, allowing it to adapt its conformation through interactions with residues surrounding the CoAlation site. Based on these findings, we propose three modes of CoA binding to proteins. Overall, this study summarizes currently available knowledge on CoAlated proteins, their functional distribution and CoA–protein stabilization interactions.
Fil: Tossounian, Maria Armineh. Colegio Universitario de Londres; Reino Unido
Fil: Baczynska, Maria. Colegio Universitario de Londres; Reino Unido
Fil: Dalton, William. Colegio Universitario de Londres; Reino Unido
Fil: Newell, Charlie. Colegio Universitario de Londres; Reino Unido
Fil: Ma, Yilin. Colegio Universitario de Londres; Reino Unido
Fil: Das, Sayoni. Colegio Universitario de Londres; Reino Unido
Fil: Semelak, Jonathan Alexis. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Filonenko, Valeriy. No especifíca;
Fil: Trujillo, Madia. Universidad de la Republica; Uruguay
Fil: Peak Chew, Sew Yeu. No especifíca;
Fil: Skehel, Mark. No especifíca;
Fil: Fraternali, Franca. No especifíca;
Fil: Orengo, Christine. Colegio Universitario de Londres; Reino Unido
Fil: Gout, Ivan. Colegio Universitario de Londres; Reino Unido
description Coenzyme A (CoA) is a key cellular metabolite known for its diverse functions in metabolism and regulation of gene expression. CoA was recently shown to play an important antioxidant role under various cellular stress conditions by forming a disulfide bond with proteins, termed CoAlation. Using anti-CoA antibodies and liquid chromatography tandem mass spectrometry (LC-MS/MS) methodologies, CoAlated proteins were identified from various organisms/tissues/cell-lines under stress conditions. In this study, we integrated currently known CoAlated proteins into mammalian and bacterial datasets (CoAlomes), resulting in a total of 2093 CoAlated proteins (2862 CoAlation sites). Functional classification of these proteins showed that CoAlation is widespread among proteins involved in cellular metabolism, stress response and protein synthesis. Using 35 published CoAlated protein structures, we studied the stabilization interactions of each CoA segment (adenosine diphosphate (ADP) moiety and pantetheine tail) within the microenvironment of the modified cysteines. Alternating polar-non-polar residues, positively charged residues and hydrophobic interactions mainly stabilize the pantetheine tail, phosphate groups and the ADP moiety, respectively. A flexible nature of CoA is observed in examined structures, allowing it to adapt its conformation through interactions with residues surrounding the CoAlation site. Based on these findings, we propose three modes of CoA binding to proteins. Overall, this study summarizes currently available knowledge on CoAlated proteins, their functional distribution and CoA–protein stabilization interactions.
publishDate 2022
dc.date.none.fl_str_mv 2022-07
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/11336/210184
Tossounian, Maria Armineh; Baczynska, Maria; Dalton, William; Newell, Charlie; Ma, Yilin; et al.; Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions; MDPI; Antioxidants; 11; 7; 7-2022; 1-18
2076-3921
CONICET Digital
CONICET
url http://hdl.handle.net/11336/210184
identifier_str_mv Tossounian, Maria Armineh; Baczynska, Maria; Dalton, William; Newell, Charlie; Ma, Yilin; et al.; Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions; MDPI; Antioxidants; 11; 7; 7-2022; 1-18
2076-3921
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/antiox11071362
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
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 13.070432

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