Chaperonin 20 might be an iron chaperone for superoxide dismutase in activating iron superoxide dismutase (FeSOD)

Kuo, Wen-Yu; Huang, Chien-Hua; Jinn, Tsung-Luo

doi:10.4161/psb.23074

Cited by 12 publications

(11 citation statements)

References 23 publications

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“…This finding suggests a differential response strategy or simply a response caused by different degrees of freezing damage. AT1G12520 (homolog of GRMZM2G175728) encodes a copper chaperone for SOD1 and is up-regulated in response to copper and senescence (Huang et al, 2012 ; Kuo et al, 2013 ). GRMZM2G044194 encodes phytosulfokine, which is an important small peptide signal (Yang et al, 2001 ).…”

Section: Resultsmentioning

confidence: 99%

Transcriptome Sequencing Identified Genes and Gene Ontologies Associated with Early Freezing Tolerance in Maize

Zhao

Liu

et al. 2016

Front. Plant Sci.

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Originating in a tropical climate, maize has faced great challenges as cultivation has expanded to the majority of the world's temperate zones. In these zones, frost and cold temperatures are major factors that prevent maize from reaching its full yield potential. Among 30 elite maize inbred lines adapted to northern China, we identified two lines of extreme, but opposite, freezing tolerance levels—highly tolerant and highly sensitive. During the seedling stage of these two lines, we used RNA-seq to measure changes in maize whole genome transcriptome before and after freezing treatment. In total, 19,794 genes were expressed, of which 4550 exhibited differential expression due to either treatment (before or after freezing) or line type (tolerant or sensitive). Of the 4550 differently expressed genes, 948 exhibited differential expression due to treatment within line or lines under freezing condition. Analysis of gene ontology found that these 948 genes were significantly enriched for binding functions (DNA binding, ATP binding, and metal ion binding), protein kinase activity, and peptidase activity. Based on their enrichment, literature support, and significant levels of differential expression, 30 of these 948 genes were selected for quantitative real-time PCR (qRT-PCR) validation. The validation confirmed our RNA-Seq-based findings, with squared correlation coefficients of 80% and 50% in the tolerance and sensitive lines, respectively. This study provided valuable resources for further studies to enhance understanding of the molecular mechanisms underlying maize early freezing response and enable targeted breeding strategies for developing varieties with superior frost resistance to achieve yield potential.

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Section: Resultsmentioning

confidence: 99%

Transcriptome Sequencing Identified Genes and Gene Ontologies Associated with Early Freezing Tolerance in Maize

Zhao

Liu

et al. 2016

Front. Plant Sci.

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“…Chloroplast proteomic studies in Arabidopsis showed that Cpn20 is much more abundant than other subunits in the chloroplast chaperonin system, which suggested Cpn20 has additional moonlighting function (Peltier et al, 2006 ). Cpn20 overexpressing mutants and mutants with defective co-chaperonin activity were reported to increase FeSOD activity by functioning as probable Fe chaperones (Kuo et al, 2013a , b ). Analysis of Cpn20 knock down mutants showed that Cpn20 functions negatively in the ABAR-WRKY40 coupled ABA signaling pathway by antagonizing Mg-chelatase H subunit to derepress the ABA-responsive WRKY40 transcription repressor (Zhang et al, 2013 , 2014 ).…”

Section: Functional Divergence Of Chloroplast Chaperonin and Co-chapementioning

confidence: 99%

Chloroplast Chaperonin: An Intricate Protein Folding Machine for Photosynthesis

Zhao

Liu

2018

Front. Mol. Biosci.

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Group I chaperonins are large cylindrical-shaped nano-machines that function as a central hub in the protein quality control system in the bacterial cytosol, mitochondria and chloroplasts. In chloroplasts, proteins newly synthesized by chloroplast ribosomes, unfolded by diverse stresses, or translocated from the cytosol run the risk of aberrant folding and aggregation. The chloroplast chaperonin system assists these proteins in folding into their native states. A widely known protein folded by chloroplast chaperonin is the large subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), an enzyme responsible for the fixation of inorganic CO2 into organic carbohydrates during photosynthesis. Chloroplast chaperonin was initially identified as a Rubisco-binding protein. All photosynthetic eucaryotes genomes encode multiple chaperonin genes which can be divided into α and β subtypes. Unlike the homo-oligomeric chaperonins from bacteria and mitochondria, chloroplast chaperonins are more complex and exists as intricate hetero-oligomers containing both subtypes. The Group I chaperonin requires proper interaction with a detachable lid-like co-chaperonin in the presence of ATP and Mg2+ for substrate encapsulation and conformational transition. Besides the typical Cpn10-like co-chaperonin, a unique co-chaperonin consisting of two tandem Cpn10-like domains joined head-to-tail exists in chloroplasts. Since chloroplasts were proposed as sensors to various environmental stresses, this diversified chloroplast chaperonin system has the potential to adapt to complex conditions by accommodating specific substrates or through regulation at both the transcriptional and post-translational levels. In this review, we discuss recent progress on the unique structure and function of the chloroplast chaperonin system based on model organisms Chlamydomonas reinhardtii and Arabidopsis thaliana. Knowledge of the chloroplast chaperonin system may ultimately lead to successful reconstitution of eukaryotic Rubisco in vitro.

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“…The existing data suggest that Cpn60a2 together with Cpn60b3 and Cpn60b2 are the main housekeeping proteins involved in chloroplast biogenesis [40], whereas the less-abundant Cpn60b4 and Cpn60b1 seem to have more unique roles [38,43]. Cpn60b2 has an additional, specific task in heat shock [44,46] together with its housekeeping role, and Cpn20 is essential, functioning in additional processes that are unrelated to protein folding [47][48][49][50].…”

Section: Trends In Plant Sciencementioning

confidence: 95%

“…Indeed, characterization of mutant plants expressing lower levels of Cpn20 linked this protein to abscisic acid (ABA) signaling regulation [47]. Cpn20 was also demonstrated to activate iron superoxide dismutase (FeSOD), possibly by serving as an iron chaperone [48,49]. Both of these roles were demonstrated to be independent of co-chaperonin function.…”

Section: Trends In Plant Sciencementioning

confidence: 95%

“…However, some species (e.g., E. coli) and some organelles (e.g., mammalian mitochondria) survive and even thrive with only one copy of type I chaperonin. Several possibilities have been proposed to explain multiple copies ABA signaling [47] Biogenesis of chlorop hyll a/b bindin g p rotein [42] FeSO D acƟvaƟon [48,49] Root-specific processes [43] α2 β2 β3 β4 β1 Cpn20…”

Section: Multiplicity Of Chloroplast Chaperoninsmentioning

confidence: 99%

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