Presence of base excision repair enzymes in the wheat aleurone and their activation in cells undergoing programmed cell death

Bissenbaev, Amangeldy K.; Ищенко, А. А.; Taipakova, Sabira; Saparbaev, Murat

doi:10.1016/j.plaphy.2011.07.017

Cited by 12 publications

(7 citation statements)

References 35 publications

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“…Exogenous GA is involved in advancing the PCD process of aleurone layers in rice (Zhang et al, 2018;Wu et al, 2016), barley (Bethke et al, 1999) and wheat (Bissenbaev et al, 2011;Xie et al, 2014), contributing to the germination of cereal seeds. To verify whether endogenous Fig.…”

Section: Osvpe3 Is Mainly Regulated By Endogenous Ga In the Aleurone mentioning

confidence: 99%

OsVPE3 Mediates GA-induced Programmed Cell Death in Rice Aleurone Layers via Interacting with Actin Microfilaments

Zhang

Xiao

Deng

et al. 2020

Rice

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Background: Vacuolar processing enzymes (VPEs) have been identified as the enzymes that regulate vacuole-mediated programmed cell death (PCD) in plants. The mechanism that VPE regulates the PCD in rice aleurone layers remains unknown. Results: The aleurone layers treated with distilled water exerted caspase-1 and VPE activity, both of which were inhibited by the caspase-1 specific inhibitor Ac-YVAD-CMK but not by the caspase-3 specific inhibitor Ac-DEVD-CHO. However, the caspase-1 and caspase-3 inhibitors weakened the activity of caspase-3. Combined with the effects of endogenous gibberellin (GA) on the induction of OsVPEs, we suggest that the OsVPE3 in the aleurone layers, which exhibits caspase-1-like activity, is a key molecule in GA-induced PCD via regulating the protease with caspase-3-like activity. Many studies have confirmed that vacuolar fusion is an important feature of vacuole-mediated PCD in plants. In this experiment, the process of vacuole fusion was accompanied by changes in the structure of actin filaments (AFs), specifically, their depolymerization and polymerization. The process of vacuolar fusion was accelerated or delayed by the promotion or inhibition of the depolymerization of AFs, respectively. Here, the inhibition of OsVPE3 blocked the depolymerization of AFs and delayed the fusion of vacuoles, indicating that OsVPE3 can regulate the fusion of vacuoles in rice aleurone layers via mediating AFs. Furthermore, the depolymerization of AFs contributed to the up-regulation of OsVPE3 gene expression and VPE activity, resulting in accelerated PCD in rice aleurone layers. However, the inhibitor of VPE reversed the effects of AF depolymerization on the activity of VPE, then postponing the process of PCD, implying that AF can involve in GA-induced PCD of rice aleurone layers by mediating OsVPE3. Conclusions: Together, activation of OsVPE3 and depolymerization of AFs shortened the process of vacuolation and PCD in rice aleurone layers, and OsVPE3 interacted with AFs during regulation.

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Section: Osvpe3 Is Mainly Regulated By Endogenous Ga In the Aleurone mentioning

confidence: 99%

OsVPE3 Mediates GA-induced Programmed Cell Death in Rice Aleurone Layers via Interacting with Actin Microfilaments

Zhang

Xiao

Deng

et al. 2020

Rice

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“…In addition, this redox system may control the level of hydrogen peroxide in the nucleus, thus having a potential signaling function. Besides nuclear-localized detoxification systems, wheat aleurone cells also display a set of gibberellin-induced glycosylases participating in the base excision repair pathway to remove non-bulky DNA base lesions generated by ROS (Bissenbaev et al, 2011). Under the oxidant conditions generated in germinating seeds, the 1-Cys Prx undergoes a progressive inactivation by overoxidation of its catalytic cysteine residue (Pulido et al, 2009).…”

Section: Redox Regulation Of Pcd In Developing and Germinating Cerealmentioning

confidence: 99%

Programmed cell death (PCD): an essential process of cereal seed development and germination

2014

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The life cycle of cereal seeds can be divided into two phases, development and germination, separated by a quiescent period. Seed development and germination require the growth and differentiation of new tissues, but also the ordered disappearance of cells, which takes place by a process of programmed cell death (PCD). For this reason, cereal seeds have become excellent model systems for the study of developmental PCD in plants. At early stages of seed development, maternal tissues such as the nucellus, the pericarp, and the nucellar projections undergo a progressive degeneration by PCD, which allows the remobilization of their cellular contents for nourishing new filial tissues such as the embryo and the endosperm. At a later stage, during seed maturation, the endosperm undergoes PCD, but these cells remain intact in the mature grain and their contents will not be remobilized until germination. Thus, the only tissues that remain alive when seed development is completed are the embryo axis, the scutellum and the aleurone layer. In germinating seeds, both the scutellum and the aleurone layer play essential roles in producing the hydrolytic enzymes for the mobilization of the storage compounds of the starchy endosperm, which serve to support early seedling growth. Once this function is completed, scutellum and aleurone cells undergo PCD; their contents being used to support the growth of the germinated embryo. PCD occurs with tightly controlled spatial-temporal patterns allowing coordinated fluxes of nutrients between the different seed tissues. In this review, we will summarize the current knowledge of the tissues undergoing PCD in developing and germinating cereal seeds, focussing on the biochemical features of the process. The effect of hormones and redox regulation on PCD control will be discussed.

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“…Our results show for the first time that the purified TaApe1L protein contains at least the following DNA repair activities: AP endonuclease, 3′-repair phosphodiesterase, 3′-phosphatase and 3′→5′ exonuclease. Importantly, TaApe1L lacks any NIR activity on DNA substrates containing oxidatively damaged bases, suggesting that other Arp-like and Ape2-like AP endonucleases may catalyze NIR activity observed previously in the extracts of wheat aleurone cells [20]. Interestingly, the wheat enzyme requires specific reaction conditions.…”

Section: Discussionmentioning

confidence: 78%

“…So far only the uracil-DNA glycosylase from wheat germ has been characterized biochemically [19]. More recently, we have identified an AP endonuclease activity in extracts from wheat aleurone layer cells that cleaves DNA duplexes containing a synthetic AP site and alpha-anomer of 2′-deoxyadenosine (αdA) residue suggesting that the BER and NIR pathways are evolutionary conserved in wheat [20]. Based on the available DNA sequence data we have isolated and cloned T. aestivum cDNA gene encoding a putative AP endonuclease, referred here as TaApe1L, which is homologous to human major AP endonuclease 1 (APE1) and A. thaliana AtApe1L.…”

Section: Introductionmentioning

confidence: 99%

Cloning and Characterization of a Wheat Homologue of Apurinic/Apyrimidinic Endonuclease Ape1L

et al. 2014

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BackgroundApurinic/apyrimidinic (AP) endonucleases are key DNA repair enzymes involved in the base excision repair (BER) pathway. In BER, an AP endonuclease cleaves DNA at AP sites and 3′-blocking moieties generated by DNA glycosylases and/or oxidative damage. A Triticum aestivum cDNA encoding for a putative homologue of ExoIII family AP endonucleases which includes E. coli Xth, human APE1 and Arabidopsis thaliana AtApe1L has been isolated and its protein product purified and characterized.Methodology/Principal FindingsWe report that the putative wheat AP endonuclease, referred here as TaApe1L, contains AP endonuclease, 3′-repair phosphodiesterase, 3′-phosphatase and 3′→5′ exonuclease activities. Surprisingly, in contrast to bacterial and human AP endonucleases, addition of Mg2+ and Ca2+ (5–10 mM) to the reaction mixture inhibited TaApe1L whereas the presence of Mn2+, Co2+ and Fe2+ cations (0.1–1.0 mM) strongly stimulated all its DNA repair activities. Optimization of the reaction conditions revealed that the wheat enzyme requires low divalent cation concentration (0.1 mM), mildly acidic pH (6–7), low ionic strength (20 mM KCl) and has a temperature optimum at around 20°C. The steady-state kinetic parameters of enzymatic reactions indicate that TaApe1L removes 3′-blocking sugar-phosphate and 3′-phosphate groups with good efficiency (k cat/K M = 630 and 485 μM−1·min−1, respectively) but possesses a very weak AP endonuclease activity as compared to the human homologue, APE1.Conclusions/SignificanceTaken together, these data establish the DNA substrate specificity of the wheat AP endonuclease and suggest its possible role in the repair of DNA damage generated by endogenous and environmental factors.

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Presence of base excision repair enzymes in the wheat aleurone and their activation in cells undergoing programmed cell death

Cited by 12 publications

References 35 publications

OsVPE3 Mediates GA-induced Programmed Cell Death in Rice Aleurone Layers via Interacting with Actin Microfilaments

OsVPE3 Mediates GA-induced Programmed Cell Death in Rice Aleurone Layers via Interacting with Actin Microfilaments

Programmed cell death (PCD): an essential process of cereal seed development and germination

Cloning and Characterization of a Wheat Homologue of Apurinic/Apyrimidinic Endonuclease Ape1L

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