Identification and immunogold localization of a novel bromegrass (Bromus inermis Leyss) peroxisome channel protein induced by ABA, cold and drought stresses, and late embryogenesis

Wu, Guohai; Robertson, A.J.; Zheng, Ping; Liu, Xunjia; Gusta, L. V.

doi:10.1016/j.gene.2005.06.046

Cited by 14 publications

(15 citation statements)

References 39 publications

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“…The 18-, 28-, 31-kDa dehydrin-like proteins in crowfoot seeds (Ranunculus sceleratus L.) were accumulated depending on the extent of water stress. Another study in bromegrass (Bromus inermis Leyss) has shown that the expression of polypeptide with molecular mass of 18.08 kDa and isoelectric point at 7.50 was induced by abscisic acid through cold or drought stress (Wu et al, 2005). Regarding our finding, p18 induced under water deficit could play a role similar to those mentioned above.…”

Section: Discussionsupporting

confidence: 86%

A Proteomics Analysis of Drought Stress-Responsive Proteins as Biomarker for Drought-Tolerant Sugarcane Cultivars

Jangpromma¹,

Kitthaisong²,

Lomthaisong³

et al. 2010

American Journal of Biochemistry and Biotechnology

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Problem statement:The prime objective in breeding selection process of drought-tolerant sugarcane is to identify the correlating marker, which could lead to rapid screening for drought-tolerant cultivars. In this study, we have reported an unknown 18-kDa protein (p18) along with other stress-inducible proteins to be highly expressed in sugarcane leaves under drought stress condition. Approach: The 2D-PAGE patterns of proteins were compared between those expressed in drought-tolerance K86-161 and drought-susceptible Khon Kaen 1 cultivars. The interested proteins were identified by mass spectrometry. The correlation between p18 expression and drought tolerance was verified in additional 4 sugarcane cultivars using ELISA and western blotting. Two physiological indexes, Chlorophyll content and SOD activity were also evaluated. Results: Mass spectrometry and comparison with known sequences in the database reveal that the proteins expressed only in stressed K86-161 are serine protease inhibitor and the one similar to replication protein A1. A group of proteins up-regulated in K86-161 are SAdenosylmethionine decarboxylase proenzyme (SAM), ubiquitin and p18. From ELISA and western blotting analysis, we found that p18 expressed in drought-tolerant sugarcane cultivars had higher binding specificity to antibody than that in drought-susceptible sugarcane cultivars. Two physiological indexes showed higher levels in drought-tolerant than those in drought susceptible sugarcanes. Conclusion: These high levels of chlorophyll and SOD are in agreement with a high level of p18 expression in droughttolerant sugarcanes. It is likely that an accumulation of p18 is a response to water deficit. In conclusion, p18 might be a good candidate for development as a marker in drought-tolerant plants.

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Section: Discussionsupporting

confidence: 86%

A Proteomics Analysis of Drought Stress-Responsive Proteins as Biomarker for Drought-Tolerant Sugarcane Cultivars

Jangpromma¹,

Kitthaisong²,

Lomthaisong³

et al. 2010

American Journal of Biochemistry and Biotechnology

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“…There has been a report recently of the molecular identification and cloning of the peroxisomal channel protein in the grass Bromus inermis (Wu et al, 2005). Such a channel has been predicted in a range of species to allow free movement of compounds of less than 300 D across the membrane, but it has not previously been identified in any species (Visser et al, 2007).…”

Section: Transporters and Integral Membrane Proteinsmentioning

confidence: 99%

Novel Proteins, Putative Membrane Transporters, and an Integrated Metabolic Network Are Revealed by Quantitative Proteomic Analysis of Arabidopsis Cell Culture Peroxisomes

et al. 2008

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Peroxisomes play key roles in energy metabolism, cell signaling, and plant development. A better understanding of these important functions will be achieved with a more complete definition of the peroxisome proteome. The isolation of peroxisomes and their separation from mitochondria and other major membrane systems have been significant challenges in the Arabidopsis (Arabidopsis thaliana) model system. In this study, we present new data on the Arabidopsis peroxisome proteome obtained using two new technical advances that have not previously been applied to studies of plant peroxisomes. First, we followed density gradient centrifugation with free-flow electrophoresis to improve the separation of peroxisomes from mitochondria. Second, we used quantitative proteomics to identify proteins enriched in the peroxisome fractions relative to mitochondrial fractions. We provide evidence for peroxisomal localization of 89 proteins, 36 of which have not previously been identified in other analyses of Arabidopsis peroxisomes. Chimeric green fluorescent protein constructs of 35 proteins have been used to confirm their localization in peroxisomes or to identify endoplasmic reticulum contaminants. The distribution of many of these peroxisomal proteins between soluble, membrane-associated, and integral membrane locations has also been determined. This core peroxisomal proteome from nonphotosynthetic cultured cells contains a proportion of proteins that cannot be predicted to be peroxisomal due to the lack of recognizable peroxisomal targeting sequence 1 (PTS1) or PTS2 signals. Proteins identified are likely to be components in peroxisome biogenesis, b-oxidation for fatty acid degradation and hormone biosynthesis, photorespiration, and metabolite transport. A considerable number of the proteins found in peroxisomes have no known function, and potential roles of these proteins in peroxisomal metabolism are discussed. This is aided by a metabolic network analysis that reveals a tight integration of functions and highlights specific metabolite nodes that most probably represent entry and exit metabolites that could require transport across the peroxisomal membrane.Within the plant cell, energy metabolism is mainly distributed among three distinct organelles: plastids, mitochondria, and peroxisomes. Although the proteomes of both plastids and mitochondria have been investigated extensively, comparatively little systematic analysis of the protein content of plant peroxisomes has been undertaken. The main obstacle for proteomics of plant peroxisomes is the availability of purified organelles from model plants that are also amenable to mass spectrometry (MS)-based identification by matching to protein sequence data. Whereas the preparation of peroxisomes in sufficient amounts and purity from spinach (Spinacia oleracea), cucumber (Cucumis sativus), pea (Pisum sativum), and soybean (Glycine max) for proteomic purposes is possible (Schwitzguebel and Siegenthaler, 1984;Corpas et al., 1994;Lopez-Huertas et al., 1999;Arai et al., 2008), the ...

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“…Recent proteomic analysis of peroxisomes from etiolated soybean also identifi ed a specifi c VDAC homolog, which was subsequently shown to be localized to peroxisomes in onion epidermal cells as RFP fusions (Arai et al, 2008a). Finally, a peroxisome channel protein homologous to putative membrane channel proteins in mitochondria (Tim17/22/23) and chloroplasts (OEP16) has been identifi ed in bromegrass cell culture, immunolocalized to the peroxisomal membrane, and found to be inducible by cold, drought and abscisic acid (Wu et al, 2005). Although Arabidopsis peroxisome proteomic studies have not identifi ed any porin channels, it is possible that some candidate proteins might be dual targeted, thus leading to their being categorized as contaminants from other organelles (Millar et al, 2006).…”

Section: Photorespirationmentioning

confidence: 99%

Peroxisome Biogenesis and Function

Kaur¹,

Reumann

2009

The Arabidopsis Book

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Peroxisomes are small and single membrane-delimited organelles that execute numerous metabolic reactions and have pivotal roles in plant growth and development. In recent years, forward and reverse genetic studies along with biochemical and cell biological analyses in Arabidopsis have enabled researchers to identify many peroxisome proteins and elucidate their functions. This review focuses on the advances in our understanding of peroxisome biogenesis and metabolism, and further explores the contribution of large-scale analysis, such as in sillco predictions and proteomics, in augmenting our knowledge of peroxisome function In Arabidopsis.

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Identification and immunogold localization of a novel bromegrass (Bromus inermis Leyss) peroxisome channel protein induced by ABA, cold and drought stresses, and late embryogenesis

Cited by 14 publications

References 39 publications

A Proteomics Analysis of Drought Stress-Responsive Proteins as Biomarker for Drought-Tolerant Sugarcane Cultivars

A Proteomics Analysis of Drought Stress-Responsive Proteins as Biomarker for Drought-Tolerant Sugarcane Cultivars

Novel Proteins, Putative Membrane Transporters, and an Integrated Metabolic Network Are Revealed by Quantitative Proteomic Analysis of Arabidopsis Cell Culture Peroxisomes

Peroxisome Biogenesis and Function

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