Centre Algatech

Institute of Michrobiology, Academy of Sciences of the Czech Republic
Mgr. Vendula Krynická, PhD.
Name:Mgr. Vendula Krynická, PhD.
Laboratory of Photosynthesis
Josef Komenda`s group
Phone:+420 384 340 444
E-mail:krynicka(at)alga.cz
Position:Associate Scientist

Vendula Krynická

ORCID: 0000-0002-1887-5986

H-index: 8

Curriculum vitae

Research interest and current research work

Vendula Krynická (VK) focuses on regulatory processes during acclimation of the cyanobacterium Synechocystis PCC 6803 to various environmental stresses, including whole-cell transcriptome and proteome responses. She is particularly interested in the role of FtsH proteases in maintaining cellular homeostasis under stress. She found that FtsHs are crucial for the function of photosystem II under high light and oxidative stress (Krynická et al., 2023, Bečková et al., 2017). It plays an essential role in photosystem II biogenesis and quality control, which contributes significantly to the robustness of the photosystem (Konik et al., 2024Krynická et al., 2023). She also showed that the essential FtsH1/3 complex plays a central role in the transcriptional response to nutrient deficiency (Krynická et al., 2019). By regulating the level of a corresponding transcription factor, it maintains cellular homeostasis during iron, phosphate, carbon and nitrogen starvation in Synechocystis (Krynická et al., 2019). It enhances the cellular response of the NtcA global pathway during nitrogen starvation. VK is currently studying the regulatory processes governing the NtcA pathway and the involvement of FtsH1/3 in its regulation. She is exploring novel methods to reprogram this pathway in Synechocystis, aiming for potential applications in biotechnology. To achieve this goal, she is expanding her expertise in protein modelling.

In 2023 VK finished the GA CR Junior project  and currently she leads a research group within the Photomachines.

 

The role of the thylakoid FtsHs in photoprotection of the PSII complex. Under HL and UV stress, the fast inactivation of PSII is accompanied by the damage of the D1 protein (D1*) leading to the destabilization of CP43 binding within PSII. This destabilization allows access of FtsH2/3 to the damaged D1, which is then quickly degraded and replaced by the newly synthesized D1 (new D1). Subsequently, the CP43 antenna is reconnected to the repaired RC47. This repair of PSII occurs in the presence of high-light inducible proteins (Hlips), which protect PSII intermediates from oxidative damage by quenching the energy from the excited Chl. When the PSII repair is completed, the Hlips are released from the complex and their level is regulated by the FtsH4 protease (Krynická and Komenda, 2024).

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