Mostrar el registro sencillo del ítem
dc.contributor.author
Tossounian, Maria Armineh
dc.contributor.author
Baczynska, Maria
dc.contributor.author
Dalton, William
dc.contributor.author
Newell, Charlie
dc.contributor.author
Ma, Yilin
dc.contributor.author
Das, Sayoni
dc.contributor.author
Semelak, Jonathan Alexis
dc.contributor.author
Estrin, Dario Ariel
dc.contributor.author
Filonenko, Valeriy
dc.contributor.author
Trujillo, Madia
dc.contributor.author
Peak Chew, Sew Yeu
dc.contributor.author
Skehel, Mark
dc.contributor.author
Fraternali, Franca
dc.contributor.author
Orengo, Christine
dc.contributor.author
Gout, Ivan
dc.date.available
2023-09-01T16:13:04Z
dc.date.issued
2022-07
dc.identifier.citation
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
dc.identifier.uri
http://hdl.handle.net/11336/210184
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
MDPI
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
COA STABILIZATION INTERACTIONS
dc.subject
COALATION
dc.subject
COENZYME A
dc.subject
MIXED-DISULFIDE
dc.subject
OXIDATIVE STRESS
dc.subject
THIOLATION
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-07-10T11:02:09Z
dc.identifier.eissn
2076-3921
dc.journal.volume
11
dc.journal.number
7
dc.journal.pagination
1-18
dc.journal.pais
Suiza
dc.description.fil
Fil: Tossounian, Maria Armineh. Colegio Universitario de Londres; Reino Unido
dc.description.fil
Fil: Baczynska, Maria. Colegio Universitario de Londres; Reino Unido
dc.description.fil
Fil: Dalton, William. Colegio Universitario de Londres; Reino Unido
dc.description.fil
Fil: Newell, Charlie. Colegio Universitario de Londres; Reino Unido
dc.description.fil
Fil: Ma, Yilin. Colegio Universitario de Londres; Reino Unido
dc.description.fil
Fil: Das, Sayoni. Colegio Universitario de Londres; Reino Unido
dc.description.fil
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
dc.description.fil
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
dc.description.fil
Fil: Filonenko, Valeriy. No especifíca;
dc.description.fil
Fil: Trujillo, Madia. Universidad de la Republica; Uruguay
dc.description.fil
Fil: Peak Chew, Sew Yeu. No especifíca;
dc.description.fil
Fil: Skehel, Mark. No especifíca;
dc.description.fil
Fil: Fraternali, Franca. No especifíca;
dc.description.fil
Fil: Orengo, Christine. Colegio Universitario de Londres; Reino Unido
dc.description.fil
Fil: Gout, Ivan. Colegio Universitario de Londres; Reino Unido
dc.journal.title
Antioxidants
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/antiox11071362
Archivos asociados