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Título:

Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions

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Autor:

Tossounian, Maria-Armineh
Baczynska, María
Dalton, William
Newell, Charlie
Yilin, Ma
Das, Sayoni
Semelak, Jonathan Alexis
Estrin, Darío
Filonenko, Valeriy
Trujillo, Madia
Sew Yeu, Peak-Chew
Skehel, Mark
Fraternali, Franca
Orengo, Christine
Gout, Iván

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Artículo

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Palabras clave:

CoA stabilization interactions
CoAlation
Coenzyme A
Mixed-disulfide
Oxidative stress
Thiolation

Descriptores:

COENZIMA A
ESTRÉS OXIDATIVO
ANTIOXIDANTES
METABOLISMO
CROMATOGRAFÍA LIQUIDA
ANTICUERPOS
ESPECTROMETRÍA DE MASAS EN TÁNDEM
ELEMENTOS ESTRUCTURALES DE LAS PROTEÍNAS

Año de publicación:

2022

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Resumen:

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.

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MDPI

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Antioxidants. 2022;11(7)

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Citación:

Tossounian M, Baczynska M, Dalton W y otros. Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions. Antioxidants [en línea]. 2022;11(7). 18 p.

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Licencia Creative Commons Atribución (CC - By 4.0)

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