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12 results on '"Yu, Bess Yi Kun"'

4. A Unique Mode of Coenzyme A Binding to the Nucleotide Binding Pocket of Human Metastasis Suppressor NME1

Author

Tossounian, Maria-Armineh, primary, Hristov, Stefan Denchev, additional, Semelak, Jonathan Alexis, additional, Yu, Bess Yi Kun, additional, Baczynska, Maria, additional, Zhao, Yuhan, additional, Estrin, Dario Ariel, additional, Trujillo, Madia, additional, Filonenko, Valeriy, additional, Gouge, Jerome, additional, and Gout, Ivan, additional

Published
2023
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5. Regulation of metastasis suppressor NME1 by a key metabolic cofactor coenzyme A

Author

Yu, Bess Yi Kun, primary, Tossounian, Maria-Armineh, additional, Hristov, Stefan Denchev, additional, Lawrence, Ryan, additional, Arora, Pallavi, additional, Tsuchiya, Yugo, additional, Peak-Chew, Sew Yeu, additional, Filonenko, Valeriy, additional, Oxenford, Sally, additional, Angell, Richard, additional, Gouge, Jerome, additional, Skehel, Mark, additional, and Gout, Ivan, additional

Published
2021
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6. Redox Regulation of the Quorum-sensing Transcription Factor AgrA by Coenzyme A

Author

Baković, Jovana, primary, Yu, Bess Yi Kun, additional, Silva, Daniel, additional, Baczynska, Maria, additional, Peak-Chew, Sew Yeu, additional, Switzer, Amy, additional, Burchell, Lynn, additional, Wigneshweraraj, Sivaramesh, additional, Vandanashree, Muralidharan, additional, Gopal, Balasubramanian, additional, Filonenko, Valeriy, additional, Skehel, Mark, additional, and Gout, Ivan, additional

Published
2021
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7. Protein CoAlation and antioxidant function of coenzyme A in prokaryotic cells

Author

Tsuchiya, Yugo, Zhyvoloup, Alexander, Baković, Jovana, Thomas, Naam, Yu, Bess Yi Kun, Das, Sayoni, Orengo, Christine, Newell, Clare, Ward, John, Saladino, Giorgio, Comitani, Federico, Gervasio, Francesco L., Malanchuk, Oksana M., Khoruzhenko, Antonina I., Filonenko, Valeriy, Peak-Chew, Sew Yeu, Skehel, Mark, and Gout, Ivan

Subjects
Neurons, Hydrolysis, Fibroblasts, Endoplasmic Reticulum, Membrane Fusion, Article, GTP Phosphohydrolases, Mice, Inbred C57BL, COS Cells, Chlorocebus aethiops, Mutation, Animals, Humans, Mutant Proteins, Guanosine Triphosphate, Hereditary Sensory and Autonomic Neuropathies, Protein Multimerization, HeLa Cells
Abstract

In all living organisms, coenzyme A (CoA) is an essential cofactor with a unique design allowing it to function as an acyl group carrier and a carbonyl-activating group in diverse biochemical reactions. It is synthesized in a highly conserved process in prokaryotes and eukaryotes that requires pantothenic acid (vitamin B5), cysteine and ATP. CoA and its thioester derivatives are involved in major metabolic pathways, allosteric interactions and the regulation of gene expression. A novel unconventional function of CoA in redox regulation has been recently discovered in mammalian cells and termed protein CoAlation. Here, we report for the first time that protein CoAlation occurs at a background level in exponentially growing bacteria and is strongly induced in response to oxidizing agents and metabolic stress. Over 12% of Staphylococcus aureus gene products were shown to be CoAlated in response to diamide-induced stress. In vitro CoAlation of S. aureus glyceraldehyde-3-phosphate dehydrogenase was found to inhibit its enzymatic activity and to protect the catalytic cysteine 151 from overoxidation by hydrogen peroxide. These findings suggest that in exponentially growing bacteria, CoA functions to generate metabolically active thioesters, while it also has the potential to act as a low-molecular-weight antioxidant in response to oxidative and metabolic stress.

Published
2018

9. Analysis of disulphide bond linkage between CoA and protein cysteine thiols during sporulation and in spores of Bacillus species

Author

Zhyvoloup, Alexander, primary, Yu, Bess Yi Kun, additional, Baković, Jovana, additional, Davis-Lunn, Mathew, additional, Tossounian, Maria-Armineh, additional, Thomas, Naam, additional, Tsuchiya, Yugo, additional, Peak-Chew, Sew Yeu, additional, Wigneshweraraj, Sivaramesh, additional, Filonenko, Valeriy, additional, Skehel, Mark, additional, Setlow, Peter, additional, and Gout, Ivan, additional

Published
2020
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10. Covalent Aurora A regulation by the metabolic integrator coenzyme A

Author

Tsuchiya, Yugo, primary, Byrne, Dominic P., additional, Burgess, Selena G., additional, Bormann, Jenny, additional, Baković, Jovana, additional, Huang, Yueyang, additional, Zhyvoloup, Alexander, additional, Yu, Bess Yi Kun, additional, Peak-Chew, Sew, additional, Tran, Trang, additional, Bellany, Fiona, additional, Tabor, Alethea B., additional, Chan, AW Edith, additional, Guruprasad, Lalitha, additional, Garifulin, Oleg, additional, Filonenko, Valeriy, additional, Vonderach, Matthias, additional, Ferries, Samantha, additional, Eyers, Claire E., additional, Carroll, John, additional, Skehel, Mark, additional, Bayliss, Richard, additional, Eyers, Patrick A., additional, and Gout, Ivan, additional

Published
2020
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11. Protein CoAlation and antioxidant function of coenzyme A in prokaryotic cells

Author

Tsuchiya, Yugo, primary, Zhyvoloup, Alexander, additional, Baković, Jovana, additional, Thomas, Naam, additional, Yu, Bess Yi Kun, additional, Das, Sayoni, additional, Orengo, Christine, additional, Newell, Clare, additional, Ward, John, additional, Saladino, Giorgio, additional, Comitani, Federico, additional, Gervasio, Francesco L., additional, Malanchuk, Oksana M., additional, Khoruzhenko, Antonina I., additional, Filonenko, Valeriy, additional, Peak-Chew, Sew Yeu, additional, Skehel, Mark, additional, and Gout, Ivan, additional

Published
2018
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12. Redox Regulation of the Quorum-sensing Transcription Factor AgrA by Coenzyme A

Author

Amy Switzer, Maria Baczynska, Balasubramanian Gopal, Sivaramesh Wigneshweraraj, Jovana Baković, Muralidharan Vandanashree, Lynn Burchell, Bess Yi Kun Yu, Mark Skehel, Ivan Gout, Valeriy Filonenko, Daniel Silva, Sew Y. Peak-Chew, Yu, Bess Yi Kun [0000-0002-4619-2226], Switzer, Amy [0000-0003-3604-426X], Wigneshweraraj, Sivaramesh [0000-0002-1418-4029], Gopal, Balasubramanian [0000-0001-9097-5052], Gout, Ivan [0000-0001-9179-8393], and Apollo - University of Cambridge Repository

Subjects
0301 basic medicine, Staphylococcus aureus, Physiology, 030106 microbiology, Clinical Biochemistry, Regulator, Virulence, protein CoAlation, RM1-950, medicine.disease_cause, Biochemistry, quorum-sensing, Article, 03 medical and health sciences, Transcriptional regulation, medicine, oxidative stress, transcriptional regulation, Molecular Biology, Transcription factor, Chemistry, Promoter, Cell Biology, biochemical phenomena, metabolism, and nutrition, Cell biology, AgrA, Quorum sensing, Response regulator, 030104 developmental biology, Therapeutics. Pharmacology
Abstract

Staphylococcus aureus (S. aureus) is an aggressive opportunistic pathogen of prominent virulence and antibiotic resistance. These characteristics are due in part to the accessory gene regulator (agr) quorum-sensing system, which allows for the rapid adaptation of S. aureus to environmental changes and thus promotes virulence and the development of pathogenesis. AgrA is the agr system response regulator that binds to the P2 and P3 promoters and upregulates agr expression. In this study, we reveal that S. aureus AgrA is modified by covalent binding of CoA (CoAlation) in response to oxidative or metabolic stress. The sites of CoAlation were mapped by liquid chromatography tandem mass spectrometry (LC–MS/MS) and revealed that oxidation-sensing Cys199 is modified by CoA. Surface plasmon resonance (SPR) analysis showed an inhibitory effect of CoAlation on the DNA-binding activity, as CoAlated AgrA had significantly lower affinity towards the P2 and P3 promoters than non-CoAlated AgrA. Overall, this study provides novel insights into the mode of transcriptional regulation in S. aureus and further elucidates the link between the quorum-sensing and oxidation-sensing roles of the agr system.

Published
2021

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