Heat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants

Demirevska-Kepova, K.; Feller, Urs

doi:10.1007/s11738-004-0050-7

Cited by 17 publications

(12 citation statements)

References 87 publications

(73 reference statements)

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“…The catabolism of Rubisco depends on a series of endogenous and environmental factors (Nooden et al, 1997;Demirevska-Kepova and Feller, 2004;Marín-Navarro and Moreno, 2006). Only some examples for abiotic and biotic stress effects can be summarized here.…”

Section: Levels Of Rubisco and Rubisco Fragments Under Environmental mentioning

confidence: 99%

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Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated

Feller

Anders

Mae

2007

Journal of Experimental Botany

362

261

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the predominant protein in photosynthesizing plant parts and the most abundant protein on earth. Amino acids deriving from its net degradation during senescence are transported to sinks (e.g. developing leaves, fruits). Rubisco catabolism is not controlled only by the overall sink demand. An accumulation of carbohydrates may also accelerate senescence and Rubisco degradation under certain conditions. Amino acids produced by proteolysis are rapidly redistributed in plants with proper source-sink relationships. In leaves of wheat plants with reduced sink capacity (e.g. sink removal, phloem interruption by steam girdling at the leaf base), Rubisco is degraded and free amino acids accumulate. They may be washed out in the rain during late senescence. In leaves of depodded soybeans, Rubisco is degraded and amino acids can be reutilized in these leaves for the synthesis of special vacuolar proteins in the paraveinal mesophyll (vegetative storage proteins). Nitrogen deriving from Rubisco degradation in older (senescing) leaves of annual crops is integrated to some extent again in newly synthesized Rubisco in younger leaves or photosynthesizing tissues of fruits. Finally, a high percentage of this nitrogen is accumulated in protein bodies (storage proteins). At the subcellular level, Rubisco can be degraded in intact chloroplasts. Reactive oxygen species may directly cleave the large subunit or modify it to become more susceptible to proteolysis. A metalloendopeptidase may play an important role in Rubisco degradation within intact chloroplasts. Additionally, the involvement of vacuolar endopeptidase(s) in Rubisco catabolism (at least under certain conditions) was postulated by various laboratories.

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Section: Levels Of Rubisco and Rubisco Fragments Under Environmental mentioning

confidence: 99%

“…Extreme climatic conditions (e.g. heat, drought, and waterlogging) are important stress factors for plants (Herrmann and Feller, 1998;Demirevska-Kepova and Feller, 2004). Elevated temperature can accelerate protein degradation in leaf segments (Demirevska-Kepova et al, 2005).…”

Section: Levels Of Rubisco and Rubisco Fragments Under Environmental mentioning

confidence: 99%

Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated

Feller

Anders

Mae

2007

Journal of Experimental Botany

362

261

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“…The folding of the ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) large subunit was mediated by the cylindrical chloroplast CPN60 and its co-factor CPN20 (Wilson & Hayer-Hartl, 2018). Consistent with the observation by Gammulla et al (2010), an increase in CPN60 allowed the protein to fold correctly, thereby enabling it to perform its role in the preservation and modification of Rubisco subunits (Demirevska- Kepova & Feller, 2004;Gammulla et al, 2010). Hsp70 and CPN60 in chloroplasts may sequentially assist in the maturation of newly imported ferredoxin-NADP reductase in an ATP-dependent manner (Tsugeki & Nishimura, 1993).…”

Section: Discussionmentioning

confidence: 79%

Transcriptomic and proteomic profiles of II YOU 838 (Oryza sativa) provide insights into heat stress tolerance in hybrid rice

Wang

Huang

et al. 2020

PeerJ

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Heat stress is an increasing threat to rice production worldwide. To investigate the mechanisms of heat tolerance in hybrid rice and their contributions to rice heterosis, we compared the transcriptome of the hybrid rice II YOU 838 (II8) with the transcriptomes of its parents Fu Hui 838 (F8) and II-32A (II3) after heat stress at 42 °C for 0 h, 24 h, 72 h and 120 h. We also performed a proteomic analysis in II8 after heat stress at 42 °C for 24 h. The transcriptome data revealed time-dependent gene expression patterns under the heat stress conditions, and the heat stress response of II8 was greatly different from those of its parents. Gene ontology analysis of the differentially expressed genes that were clustered using k-means clustering showed that most of the up-regulated genes were involved in responses to stimuli, cell communication, and metabolic and transcription factor activities, whereas the down-regulated genes were enriched in photosynthesis and signal transduction. Moreover, 35 unique differentially abundant proteins, including a basic helix-loop-helix transcription factor (bHLH96), calmodulin-binding transcription activator, heat shock protein (Hsp70), and chaperonin 60 (CPN60), were detected in the proteomic analysis of II8 under heat stress. The co-regulatory analysis revealed novel genes and pathways involved in heat tolerance, namely, ferredoxin-NADP reductase, peroxidases, mitogen-activated protein kinase kinase kinase, and heat shock factor (HSF)–Hsp network. Members of the Hsp and HSF families had over-dominant expression patterns in the hybrid compared with its parents, to help maintain the higher photosynthesis and antioxidant defense systems in the hybrid. Our study suggests that the complex HSF–Hsp regulatory network contribute to the heat tolerance of the hybrid rice.

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“…Rubisco subunit -binding protein is homologous to Hsp60 was found to have an auxiliary function in the assembly of a wide range of proteins in chloroplasts including Rubisco, and its proposed main function is to prevent aggregation and assist in either proper folding or targeting proteins to one of the proteases (Gatenby and Ellis 1990;Bukau and Horwich 1998). Induced expression of Rubisco subunit-binding protein has been reported in many plant species under various biotic and abiotic stresses (Demirevska-Kepova and Feller 2004;Fujiwara et al 2006;Demirevska et al 2008).…”

Section: Proteins Associated With Protein Biosynthesis and Foldingmentioning

confidence: 99%

Proteomic Analysis of Differentially Expressed Proteins in Resistant Soybean Leaves after Phakopsora pachyrhizi Infection

Wang

Yuan

et al. 2012

Journal of Phytopathology

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Soybean rust caused by Phakopsora pachyrhizi is a destructive foliar disease in nearly all soybean‐producing countries. Understanding the host responses at the molecular level is certainly essential for effective control of the disease. To identify proteins involved in the resistance to soybean rust, differential proteomic analysis was conducted in soybean leaves of a resistant genotype after P. pachyrhizi infection. A total of 41 protein spots exhibiting a fold change >1.5 between the non‐inoculated and P. pachyrhizi‐inoculated soybean leaves at 12 and 24 h postinoculation (hpi) were unambiguously identified and functionally grouped into seven categories. Twenty proteins were up‐regulated and four proteins were down‐regulated at 12 hpi, whereas 18 proteins were up‐regulated and eight proteins were down‐regulated at 24 hpi. Generally, proteins involved in photosynthesis were down‐regulated, whereas proteins associated with disease and defense response, protein folding and assembly, carbohydrate metabolism and energy production were up‐regulated. Results are discussed in terms of the functional implications of the proteins identified, with special emphasis on their putative roles in defense. Abundance changes of these proteins, together with their putative functions reveal a comprehensive picture of the host response in rust‐resistant soybean leaves and provide a useful platform for better understanding of the molecular basis of soybean rust resistance.

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Heat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants

Cited by 17 publications

References 87 publications

Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated

Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated

Transcriptomic and proteomic profiles of II YOU 838 (Oryza sativa) provide insights into heat stress tolerance in hybrid rice

Proteomic Analysis of Differentially Expressed Proteins in Resistant Soybean Leaves after Phakopsora pachyrhizi Infection

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