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    DETERMINATION OF THE EFFECTS OF BIOTIC STRESS CAUSED BY Puccinia Malvacearum IN Malva Sylvestris BY SOME BIOCHEMICAL AND PHYSIOLOGICAL PARAMETERS
    (Parlar Scientific Publications (P S P), 2021) Temel, Mehmet; Yigit, Emel; Kabaktepe, Sanli; Akbulut, Gulcin Beker
    In this study, the effects of Puccinia malvacearum, an important rust fungus in the phylum Basidiomycota, on Malva sylvestris (mallow) were investigated. Changes in pigment content, dry weight, malondialdehyde (MDA), which is an important marker of lipid peroxidation, total phenolic content, peroxidase (POD) and ascorbate peroxidase (APX) enzymes were investigated in groups infected with rust fungi and those that were not. In the infected group, an increase in pigment content was observed in samples obtained in June and July. The increase in MDA content in infected groups was also considered an indicator that caused oxidative stress in M. sylvestris. In addition, a decrease in POD activity and an increase in phenolic content were observed in the infected group. APX activity was also increased in the infected groups. Additionally, changes in the dry weight content were observed in the infected groups. Our findings showed that M. sylvestris gave important physiological and biochemical responses to oxidative stress caused by P. malvacearum. It is thought that the data obtained in this study will contribute to the elucidation of resistance mechanisms in plants exposed to fungal infection.
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    Structural Modeling and Functional Evaluation of Pectate Lyase Protein from Prunus armeniaca
    (Springer, 2023) Akbulut, Gulcin Beker
    Prunus armeniaca (P. armeniaca) is a stone fruit that is widely consumed around the world with its appealing and delicious taste. Pectate lyases (Pels) cleave the alpha-1,4-glycosidic bond of polygalacturonic acid. Pels have a role in the development, ripening, and in providing intracellular entry by disrupting the integrity of the cell wall of pathogenic microorganisms. The three-dimensional structures of proteins and enzymes provide important data on their functional properties and catalytic roles. The protein structure of any Prunus is unknown. In this study, P. armeniaca protein homology models were modeled using ProMod3 and trRosetta deep learning algorithms in order to elucidate the molecular mechanism of ripening and cell wall degradation processes in which pectate lyase (Pel) plays a role. Substrate binding patterns were demonstrated by molecular docking. The (Pel) homology models from P. armeniaca were within x-ray quality limits. The three-dimensional structure of P. armeniaca pectate lyase (PaPel) has been shown to have an unusual beta-folding formation that we have encountered in other Pels. We determined that (RXPXXR302)-R-297 and (WIDH233)-W-230 residues preserved in known Pels were preserved in Pel from P. armeniaca. The (NVHI171)-N-168 and (NVHI192)-N-189 repeat sites in the vicinity of the catalytic site may be responsible for substrate stability. The lowest binding energy for the substrate was -4.18 kcal.mol(-1). The data presented in this study may provide an important model for elucidating the catalytic mechanism of development, ripening, and cell wall destruction processes of Prunus Pel.