Abstract:Protein acetylation and succinylation are the most crucial protein post-translational modifications (PTMs) involved in the regulation of plant growth and development. In this study, we present the first lysine-acetylation and lysine-succinylation proteome analysis of seedling leaves in Brachypodium distachyon L (Bd). Using high accuracy nano LC-MS/MS combined with affinity purification, we identified a total of 636 lysine-acetylated sites in 353 proteins and 605 lysine-succinylated sites in 262 proteins. These… Show more
“…Although a number of proteins in the pathways of carbon fixation, photosynthesis and oxidative phosphorylation were found to be succinylated in both common wheat (Additional file 1: Figure S4b, Additional file 2: Table S6) and B. distachyon [13], few common proteins were identified between them. Moreover, succinylated proteins associated with peroxisome were only identified in common wheat (Additional file 1: Figure S4b, Additional file 2: Table S6), and modified proteins related to microbial metabolism in diverse environments and biosynthesis of antibiotics were only found in B. distachyon [13]. These results suggest that lysine succinylation plays both common and specific roles in different plant species.Fig.…”
BackgroundProtein lysine succinylation is an important post-translational modification and plays a critical regulatory role in almost every aspects of cell metabolism in both eukaryotes and prokaryotes. Common wheat is one of the major global cereal crops. However, to date, little is known about the functions of lysine succinylation in this plant. Here, we performed a global analysis of lysine succinylation in wheat and examined its overlap with lysine acetylation.ResultsIn total, 330 lysine succinylated modification sites were identified in 173 proteins. Bioinformatics analysis showed that the modified proteins are distributed in multiple subcellular compartments and are involved in a wide variety of biological processes such as photosynthesis and the Calvin-Benson cycle, suggesting an important role for lysine succinylation in these processes. Five putative succinylation motifs were identified. A protein interaction network analysis revealed that diverse interactions are modulated by protein succinylation. Moreover, 21 succinyl-lysine sites were found to be acetylated at the same position, and 33 proteins were modified by both acetylation and succinylation, suggesting an extensive overlap between succinylation and acetylation in common wheat. Comparative analysis indicated that lysine succinylation is conserved between common wheat and Brachypodium distachyon.ConclusionsThese results suggest that lysine succinylation is involved in diverse biological processes, especially in photosynthesis and carbon fixation. This systematic analysis represents the first global analysis of lysine succinylation in common wheat and provides an important resource for exploring the physiological role of lysine succinylation in this cereal crop and likely in all plants.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-017-3698-2) contains supplementary material, which is available to authorized users.
“…Although a number of proteins in the pathways of carbon fixation, photosynthesis and oxidative phosphorylation were found to be succinylated in both common wheat (Additional file 1: Figure S4b, Additional file 2: Table S6) and B. distachyon [13], few common proteins were identified between them. Moreover, succinylated proteins associated with peroxisome were only identified in common wheat (Additional file 1: Figure S4b, Additional file 2: Table S6), and modified proteins related to microbial metabolism in diverse environments and biosynthesis of antibiotics were only found in B. distachyon [13]. These results suggest that lysine succinylation plays both common and specific roles in different plant species.Fig.…”
BackgroundProtein lysine succinylation is an important post-translational modification and plays a critical regulatory role in almost every aspects of cell metabolism in both eukaryotes and prokaryotes. Common wheat is one of the major global cereal crops. However, to date, little is known about the functions of lysine succinylation in this plant. Here, we performed a global analysis of lysine succinylation in wheat and examined its overlap with lysine acetylation.ResultsIn total, 330 lysine succinylated modification sites were identified in 173 proteins. Bioinformatics analysis showed that the modified proteins are distributed in multiple subcellular compartments and are involved in a wide variety of biological processes such as photosynthesis and the Calvin-Benson cycle, suggesting an important role for lysine succinylation in these processes. Five putative succinylation motifs were identified. A protein interaction network analysis revealed that diverse interactions are modulated by protein succinylation. Moreover, 21 succinyl-lysine sites were found to be acetylated at the same position, and 33 proteins were modified by both acetylation and succinylation, suggesting an extensive overlap between succinylation and acetylation in common wheat. Comparative analysis indicated that lysine succinylation is conserved between common wheat and Brachypodium distachyon.ConclusionsThese results suggest that lysine succinylation is involved in diverse biological processes, especially in photosynthesis and carbon fixation. This systematic analysis represents the first global analysis of lysine succinylation in common wheat and provides an important resource for exploring the physiological role of lysine succinylation in this cereal crop and likely in all plants.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-017-3698-2) contains supplementary material, which is available to authorized users.
“…In animals, succinate can indirectly stabilize the 1a subunit of the transcriptional regulator hypoxia-inducible factor, and succinylation, which relies on succinyl-CoA as substrate, regulates TCA cycle and glycolytic enzymes (Mills and O'Neill, 2014). Interestingly, proteins active in the TCA cycle and glycolysis have also been found succinylated in tomato (Solanum lycopersicum), wheat (Triticum durum), rice (Oryza sativa), and Brachypodium, suggesting a conserved role of succinate and succinyl-CoA in the regulation of metabolic processes (He et al, 2016;Jin and Wu, 2016;Zhen et al, 2016;Zhang et al, 2017c). Other posttranslational modifications such as protein phosphorylation (e.g.…”
Section: Posttranslational Modification Of Proteinsmentioning
ORCID IDs: 0000-0001-5369-7911 (S.W.); 0000-0003-4024-968X (O.V.A.); 0000-0003-0796-8308 (M.S.).Cells of complex organisms typically rely on mitochondria for energy provision. The amount of energy required to sustain cellular activity can vary strongly depending on external conditions. Vice versa, constraints on respiratory activity due to metabolic status or stress insult require mitochondrial signaling to coordinate cellular physiology with the function of the organelle. In this update, we review recent insights into plant mitochondrial energy signaling in the light of their significance to stress acclimation. First, we focus on the characteristic adjustments of the nuclear transcriptome that occur after pharmacological inhibition of the mitochondrial electron transport chain as the output of mitochondrial retrograde signaling. Second, we discuss the proteins that have recently been identified as regulators of the transcript responses and the emerging picture of their action as a signaling network. We then pose the question of how well our current models of inducing mitochondrial dysfunction relate to conditions that plants face naturally. We reason that low-oxygen stress shows striking similarities with electron transport inhibitors with respect to their impact on mitochondrial energy physiology upstream, as well as the cellular transcriptomic response. Finally, we highlight and discuss changes in mitochondrial physiology that are common to both stimuli as candidates for upstream signals. The aim of this update is to better define the physiological context in which mitochondrial signaling operates to provide new directions for future research.
RESPONSES TO MITOCHONDRIAL ENERGY SIGNALING AT THE TRANSCRIPT LEVEL
“…During germination, rice seed undergoes dynamic rearrangements of metabolism and succinylation status if its proteome changes [75]. It was shown that, in rice seedlings, succinylated proteins are enriched in functional categories such as citrate cycle, glycolysis/gluconeogenesis, ribosome, and carbon fixation with notably high coverage in pathways involved in the conversion of glucose to pyruvate [76]. The seedling leaves of Brachypodium distachyon , a grass family plant also exhibited the PTM in carbon metabolism pathways [76].…”
Section: Systems For Post-translational Modifications In Crops Undmentioning
confidence: 99%
“…It was shown that, in rice seedlings, succinylated proteins are enriched in functional categories such as citrate cycle, glycolysis/gluconeogenesis, ribosome, and carbon fixation with notably high coverage in pathways involved in the conversion of glucose to pyruvate [76]. The seedling leaves of Brachypodium distachyon , a grass family plant also exhibited the PTM in carbon metabolism pathways [76]. According to the comparison of succinylated proteins across species by Zhen et al, a high degree of conservation of succinylation was suggested among eukaryotes including humans, E. coli , and plants [75].…”
Section: Systems For Post-translational Modifications In Crops Undmentioning
confidence: 99%
“…Extensive characterization of the tomato succinylome identified that several sites of histone H3 (K14, K56, K79, and K122) are targets for succinylation [77]. Because these are sites that were also modified in other organisms including humans, mice, Drosophila melanogaster , and Saccharomyces cerevisiae , evolutionarily conserved protein succinylation is assumed to be a central regulatory mechanism of biological processes [76]. Elucidating elaborate regulation of important metabolic pathways by PTMs is crucial for plant adaptation to stressors and enhancement of functionality of crops.…”
Section: Systems For Post-translational Modifications In Crops Undmentioning
The efficiency of stress-induced adaptive responses of plants depends on intricate coordination of multiple signal transduction pathways that act coordinately or, in some cases, antagonistically. Protein post-translational modifications (PTMs) can regulate protein activity and localization as well as protein–protein interactions in numerous cellular processes, thus leading to elaborate regulation of plant responses to various external stimuli. Understanding responses of crop plants under field conditions is crucial to design novel stress-tolerant cultivars that maintain robust homeostasis even under extreme conditions. In this review, proteomic studies of PTMs in crops are summarized. Although the research on the roles of crop PTMs in regulating stress response mechanisms is still in its early stage, several novel insights have been retrieved so far. This review covers techniques for detection of PTMs in plants, representative PTMs in plants under abiotic stress, and how PTMs control functions of representative proteins. In addition, because PTMs under abiotic stresses are well described in soybeans under submergence, recent findings in PTMs of soybean proteins under flooding stress are introduced. This review provides information on advances in PTM study in relation to plant adaptations to abiotic stresses, underlining the importance of PTM study to ensure adequate agricultural production in the future.
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