Daria Vetoshkina

Dr. Daria Vetoshkina


Research Focus & Metrics

Academic Career Length

5Years (2022-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
7 December 2022 in Plant Physiology and Biochemistry
Verified
Journal Article
Closed access
DVDaria Vetoshkina
Daria Vetoshkina
NBNikolay Balashov
Nikolay Balashov
BIBoris Ivanov
Boris Ivanov
AAAleksandr Ashikhmin
Aleksandr Ashikhmin
MBMaria M Borisova-Mubarakshina
Maria M Borisova-Mubarakshina

31 July 2025 in Biochemistry (Moscow)
Verified
Journal Article
Closed access
PDF file
NBNikolai V. Balashov
Nikolai V. Balashov
MBMaria M. Borisova-Mubarakshina
Maria M. Borisova-Mubarakshina
DVDaria Vetoshkina
Daria Vetoshkina
One of the adaptive mechanisms used by photosynthetic organisms in response to changing light conditions is redistribution of antenna complexes between the photosystems, a process known as state transitions (ST). This mechanism allows to regulate the amount of light energy absorbed by the photosystems. Numerous studies have reported inhibition of ST at the elevated light intensity; however, the mechanism underlying this process is still debated. We evaluated the effect of H2O2 at various concentrations on the ST process in functionally active thylakoids isolated from Arabidopsis thaliana leaves and investigated which stage of this process is affected by H2O2. To assess the extent of ST, we measured low-temperature chlorophyll a fluorescence spectra (650-780 nm) and calculated the F745/F685 ratio, whose changes can serve as an indicator of ST progression. H2O2 inhibited ST under the low-intensity light conditions and, furthermore, led to a decrease in the accumulation of phosphorylated Lhcb1 and Lhcb2 proteins involved in ST. This suggests that the observed ST inhibition resulted from the suppression of STN7 kinase activity. Importantly, H2O2 in the tested concentrations did not affect the electron transport rate, indicating that the inhibition of STN7 kinase activity was not associated with suppression of the photosynthetic electron transport chain (PETC) activity. The treatment with H2O2 did not reduce the level of phosphorylated D1 protein (a product of phosphorylation by the thylakoid STN8 kinase). Taken together, these results demonstrate for the first time the mechanism by which H2O2 inhibits STN7 kinase activity and, consequently, the process of ST.

25 April 2023 in Plants
Verified
Journal Article
Open access
PDF file
ENElena Nadeeva
Elena Nadeeva
LILyudmila K. Ignatova
Lyudmila K. Ignatova
NRNatalia Rudenko
Natalia Rudenko
DVDaria Vetoshkina
Daria Vetoshkina
INIlya Naydov
Ilya Naydov
BIBoris Ivanov
Boris Ivanov
The knockout of the At2g28210 gene encoding α-carbonic anhydrase 2 (α-CA2) in Arabidopsis thaliana (Columbia) led to alterations in photosynthetic processes. The effective quantum yields of both photosystem II (PSII) and photosystem I (PSI) were higher in α-carbonic anhydrase 2 knockout plants (α-CA2-KO), and the reduction state of plastoquinone pool was lower than in wild type (WT). The electron transport rate in the isolated thylakoids measured with methyl viologen was higher in α-CA2-KO plants. The amounts of reaction centers of PSII and PSI were similar in WT and α-CA2-KO plants. The non-photochemical quenching of chlorophyll a fluorescence in α-CA2-KO leaves was lower at the beginning of illumination, but became slightly higher than in WT leaves when the steady state was achieved. The degree of state transitions in the leaves was lower in α-CA2-KO than in WT plants. Measurements of the electrochromic carotenoid absorbance shift (ECS) revealed that the light-dependent pH gradient (ΔpH) across the thylakoid membrane was lower in the leaves of α-CA2-KO plants than in WT plants. The starch content in α-CA2-KO leaves was lower than in WT plants. The expression levels of the genes encoding chloroplast CAs in α-CA2-KO changed noticeably, whereas the expression levels of genes of cytoplasmic CAs remained almost the same. It is proposed that α-CA2 may be situated in the chloroplasts.