Why don't plants have diabetes? Systems for scavenging reactive carbonyls in photosynthetic organisms

Shimakawa, Ginga; Suzuki, Muneyasu; Yamamoto, E.; Saito, Ryota; Iwamoto, Tatsuya; Nishi, Akiko; Miyake, Chikahiro

doi:10.1042/bst20130273

Cited by 32 publications

(21 citation statements)

References 36 publications

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“…Interestingly, the latter gene is physically located between a DNA repair gene (encoding RAD51) and a tRNA modification gene on scaffold 2777 in the A. digitifera draft assembly ( Figure 4—figure supplement 4 ). Glyoxalase I belongs to a system that carries out the detoxification of reactive carbonyls (RC), such as highly cytotoxic methylglyoxal, produced by sugar metabolism and the Calvin cycle ( Shimakawa et al, 2014 ). Methylglyoxal production in plastids increases with light intensity ( Takagi et al, 2014 ).…”

Section: Discussionmentioning

confidence: 99%

“…Methylglyoxal production in plastids increases with light intensity ( Takagi et al, 2014 ). Another gene encoding a putative RC scavenger ( Shimakawa et al, 2014 ) is short-chain dehydrogenase/reductase (SDR) that was derived in corals from an algal source ( Figure 4—figure supplement 5 ). Other alga-derived HGTs were from species containing plastids of red algal secondary endosymbiotic origin (i.e., chlorophyll c -containing lineages such as stramenopiles) ( Table 1 ).…”

Section: Discussionmentioning

confidence: 99%

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Comparative genomics explains the evolutionary success of reef-forming corals

Bhattacharya

Agrawal

Aranda

et al. 2016

eLife

185

175

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Transcriptome and genome data from twenty stony coral species and a selection of reference bilaterians were studied to elucidate coral evolutionary history. We identified genes that encode the proteins responsible for the precipitation and aggregation of the aragonite skeleton on which the organisms live, and revealed a network of environmental sensors that coordinate responses of the host animals to temperature, light, and pH. Furthermore, we describe a variety of stress-related pathways, including apoptotic pathways that allow the host animals to detoxify reactive oxygen and nitrogen species that are generated by their intracellular photosynthetic symbionts, and determine the fate of corals under environmental stress. Some of these genes arose through horizontal gene transfer and comprise at least 0.2% of the animal gene inventory. Our analysis elucidates the evolutionary strategies that have allowed symbiotic corals to adapt and thrive for hundreds of millions of years.DOI: http://dx.doi.org/10.7554/eLife.13288.001

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Comparative genomics explains the evolutionary success of reef-forming corals

Bhattacharya

Agrawal

Aranda

et al. 2016

eLife

185

175

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“…Methylglyoxal is thus constantly produced in the plants during glycolysis reactions and in the Calvin cycle of photosynthesis (Figure 1) [11,20]. Under abiotic stress conditions such as salinity, drought, and cold stress, concentrations of MG in plant cells are reported to increase rapidly from 35–75 μM under normal conditions to 200 μM (2- to 6-fold) [21,22].…”

Section: Methylglyoxal Detoxification System In Plantsmentioning

confidence: 99%

Glyoxalase Goes Green: The Expanding Roles of Glyoxalase in Plants

Sankaranarayanan

Jamshed

Abhinandan

et al. 2017

IJMS

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The ubiquitous glyoxalase enzymatic pathway is involved in the detoxification of methylglyoxal (MG), a cytotoxic byproduct of glycolysis. The glyoxalase system has been more extensively studied in animals versus plants. Plant glyoxalases have been primarily associated with stress responses and their overexpression is known to impart tolerance to various abiotic stresses. In plants, glyoxalases exist as multigene families, and new roles for glyoxalases in various developmental and signaling pathways have started to emerge. Glyoxalase-based MG detoxification has now been shown to be important for pollination responses. During self-incompatibility response in Brassicaceae, MG is required to target compatibility factors for proteasomal degradation, while accumulation of glyoxalase leads to MG detoxification and efficient pollination. In this review, we discuss the importance of glyoxalase systems and their emerging biological roles in plants.

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“…Bechtold et al (28) in their pioneering work confirmed the presence of glycation products in exhaustive hydrolysates of plant leaf proteins. Continuing these studies, Shimakawa et al (29) proposed the endogenic sources of AGEs in plants and some corresponding anti-glycative mechanisms protecting the plants from deleterious effects of accumulated AGEs. Because of the high levels of carbohydrates, transition metals, and molecular oxygen in plant tissues, high levels of monosaccharide autoxidation (6) and therefore essential in vivo ␣-dicarbonyl and reactive oxygen species (ROS) production can be expected.…”

mentioning

confidence: 99%

Global proteomic analysis of advanced glycation end products in the Arabidopsis proteome provides evidence for age-related glycation hot spots

Bilova

Paudel

Shilyaev

et al. 2017

Journal of Biological Chemistry

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Glycation is a post-translational modification resulting from the interaction of protein amino and guanidino groups with carbonyl compounds. Initially, amino groups react with reducing carbohydrates, yielding Amadori and Heyns compounds. Their further degradation results in formation of advanced glycation end products (AGEs), also originating from α-dicarbonyl products of monosaccharide autoxidation and primary metabolism. In mammals, AGEs are continuously formed during the life of the organism, accumulate in tissues, are well-known markers of aging, and impact age-related tissue stiffening and atherosclerotic changes. However, the role of AGEs in age-related molecular alterations in plants is still unknown. To fill this gap, we present here a comprehensive study of the age-related changes in the glycated proteome, including the proteins affected and specific glycation sites therein. We also consider the qualitative and quantitative changes in glycation patterns in terms of the general metabolic background, pathways of AGE formation, and the status of plant anti-oxidative/anti-glycative defense. Although the patterns of glycated proteins were only minimally influenced by plant age, the abundance of 96 AGE sites in 71 proteins was significantly affected in an age-dependent manner and clearly indicated the existence of age-related glycation hot spots in the plant proteome. Homology modeling revealed glutamyl and aspartyl residues in close proximity (less than 5 Å) to these sites in three aging-specific and eight differentially glycated proteins, four of which were modified in catalytic domains. Thus, the sites of glycation hot spots might be defined by protein structure that indicates, at least partly, site-specific character of glycation.

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Why don't plants have diabetes? Systems for scavenging reactive carbonyls in photosynthetic organisms

Cited by 32 publications

References 36 publications

Comparative genomics explains the evolutionary success of reef-forming corals

Comparative genomics explains the evolutionary success of reef-forming corals

Glyoxalase Goes Green: The Expanding Roles of Glyoxalase in Plants

Global proteomic analysis of advanced glycation end products in the Arabidopsis proteome provides evidence for age-related glycation hot spots

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