TY - JOUR

T1 - Uracil-DNA Glycosylase from Beta vulgaris: Properties and Response to Abiotic Stress

AU - Petrova, Daria V

AU - Zateeva, Maria V

AU - Zhang, Lijun

AU - Zhang, Jiajia

AU - Zhao, Ying

AU - Permyakova, Natalya V

AU - Zagorskaya, Alla A

AU - Zharkov, Vasily D

AU - Endutkin, Anton V

AU - Yu, Bing

AU - Ma, Chunquan

AU - Li, Haiying

AU - Zharkov, Dmitry O

AU - Grin, Inga R

N1 - This research was funded by a joint grant from the Russian Science Foundation (project 23-44-00050) and the International Cooperation and Exchange of the National Natural Science Foundation of China (project 32261133530). Partial salary supported from the Russian Ministry of Science and Higher Education is acknowledged (project 125012300657-2; structural analysis).

PY - 2025/8/24

Y1 - 2025/8/24

N2 - Uracil-DNA glycosylases (UNGs) are DNA repair enzymes responsible for the removal of uracil, a canonical RNA nucleobase, from DNA, where it appears through cytosine deamination or incorporation from the cellular dUTP pool. While human and Escherichia coli UNGs have been extensively investigated, much less is known about their plant counterparts, of which UNGs from Arabidopsis thaliana are the only studied examples. Here, we show that in sugar beet (Beta vulgaris L.), an important crop species, cold and salt stress induce the expression of the UNG gene (BvUNG) and modulate the level of the uracil-excising activity in the roots. Purified recombinant BvUNG efficiently removes uracil from DNA both in vitro and in an E. coli reporter strain but does not excise 5-hydroxyuracil, 5,6-dihydrouracil, or 5-hydroxymethyluracil. The activity is abolished by Ugi, a protein UNG inhibitor from PBS1 bacteriophage, and by a mutation of a conserved active site His residue. Structural modeling shows the presence of a disordered N-tail prone to undergo phase separation, followed by a long α helix oriented differently from its counterpart in human UNG. Overall, BvUNG is a functional uracil-DNA glycosylase that might participate in the response to abiotic stress.

AB - Uracil-DNA glycosylases (UNGs) are DNA repair enzymes responsible for the removal of uracil, a canonical RNA nucleobase, from DNA, where it appears through cytosine deamination or incorporation from the cellular dUTP pool. While human and Escherichia coli UNGs have been extensively investigated, much less is known about their plant counterparts, of which UNGs from Arabidopsis thaliana are the only studied examples. Here, we show that in sugar beet (Beta vulgaris L.), an important crop species, cold and salt stress induce the expression of the UNG gene (BvUNG) and modulate the level of the uracil-excising activity in the roots. Purified recombinant BvUNG efficiently removes uracil from DNA both in vitro and in an E. coli reporter strain but does not excise 5-hydroxyuracil, 5,6-dihydrouracil, or 5-hydroxymethyluracil. The activity is abolished by Ugi, a protein UNG inhibitor from PBS1 bacteriophage, and by a mutation of a conserved active site His residue. Structural modeling shows the presence of a disordered N-tail prone to undergo phase separation, followed by a long α helix oriented differently from its counterpart in human UNG. Overall, BvUNG is a functional uracil-DNA glycosylase that might participate in the response to abiotic stress.

KW - Uracil-DNA Glycosidase/metabolism

KW - Beta vulgaris/enzymology

KW - Stress, Physiological

KW - Uracil/metabolism

KW - Plant Proteins/metabolism

KW - Escherichia coli/genetics

KW - Models, Molecular

KW - Gene Expression Regulation, Plant

KW - Plant Roots/enzymology

UR - https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=105015894687&origin=inward

UR - https://pubmed.ncbi.nlm.nih.gov/40943147/

UR - https://www.mdpi.com/1422-0067/26/17/8221

UR - https://www.mendeley.com/catalogue/5c572568-ff83-32a8-9fb7-ca187999e492/

U2 - 10.3390/ijms26178221

DO - 10.3390/ijms26178221

M3 - Article

C2 - 40943147

VL - 26

SP - 8221

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1661-6596

IS - 17

M1 - 8221

ER -