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C Crone J Frokjaer-Jensen JJ Friedman O Christensen 《The Journal of general physiology》1978,71(2):195-220
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Hsin-Ho Wei Martha Rowe Jean-Jack M. Riethoven Ryan Grove Jiri Adamec Yusuke Jikumaru Paul Staswick 《Plant physiology》2015,169(2):1371-1381
Glutathione (GSH) is essential for many aspects of plant biology and is associated with jasmonate signaling in stress responses. We characterized an Arabidopsis (Arabidopsis thaliana) jasmonate-hypersensitive mutant (jah2) with seedling root growth 100-fold more sensitive to inhibition by the hormone jasmonyl-isoleucine than the wild type. Genetic mapping and genome sequencing determined that the mutation is in intron 6 of GLUTATHIONE SYNTHETASE2, encoding the enzyme that converts γ-glutamylcysteine (γ-EC) to GSH. The level of GSH in jah2 was 71% of the wild type, while the phytoalexin-deficient2-1 (pad2-1) mutant, defective in GSH1 and having only 27% of wild-type GSH level, was not jasmonate hypersensitive. Growth defects for jah2, but not pad2, were also seen in plants grown to maturity. Surprisingly, all phenotypes in the jah2 pad2-1 double mutant were weaker than in jah2. Quantification of γ-EC indicated these defects result from hyperaccumulation of this GSH precursor by 294- and 65-fold in jah2 and the double mutant, respectively. γ-EC reportedly partially substitutes for loss of GSH, but growth inhibition seen here was likely not due to an excess of total glutathione plus γ-EC because their sum in jah2 pad2-1 was only 16% greater than in the wild type. Further, the jah2 phenotypes were lost in a jasmonic acid biosynthesis mutant background, indicating the effect of γ-EC is mediated through jasmonate signaling and not as a direct result of perturbed redox status.Glutathione (GSH) is an essential thiol of most higher organisms, including plants. Primarily found in the reduced form, its roles in maintaining a reduced intracellular state are numerous and well characterized (Foyer and Noctor, 2011; Noctor et al., 2011). Additionally, GSH is involved in detoxifying reactive oxygen species, heavy metal detoxification through phytochelatins, elimination of xenobiotics, and signaling of plant development and stress responses (Rouhier et al., 2008).GSH is synthesized in two steps. The first links Cys to the γ-carboxyl group of Glu through an amide bond catalyzed by γ-glutamylcysteine (γ-EC) synthetase, encoded by the single gene GSH1 in Arabidopsis (Arabidopsis thaliana). Gly is then added by GSH synthetase (GSH-S), also encoded by a single gene (GSH2). GSH is typically present at millimolar levels in plants, and although γ-EC is normally present at only a few percent of this amount, there is evidence that γ-EC has redox activities in Arabidopsis (Pasternak et al., 2008).Insertional knockouts of GSH1 are embryo lethal, and rootmeristemless1, with only 5% of wild-type GSH level, lacks a root apical meristem due to cell cycle arrest (Vernoux et al., 2000; Cairns et al., 2006). Other mutants producing 25% to 50% of wild-type GSH levels grow normally but exhibit defects under various stress conditions. For example, phytoalexin-deficient2-1 (pad2-1) and cadmium sensitive2 mutants are susceptible to pathogens and hypersensitive to Cd, respectively, while regulator of axillary meristems1 causes elevated expression of ASCORBATE PEROXIDASE2 under non-photooxidative-stress conditions (Glazebrook and Ausubel, 1994; Cobbett et al., 1998; Ball et al., 2004).GSH2 null alleles (gsh2-1 and gsh2-2) are also lethal, although plants survive to the early seedling stage (Pasternak et al., 2008). Survival past the embryo stage was attributed to partial complementation of GSH activity by γ-EC, which accumulates to excessive levels in gsh2-1, and the mutant is partially rescued by GSH supplementation. Missense and nonsense GSH2 alleles of membrane trafficking mutants (gsh2-3–gsh2-5) disrupt endoplasmic reticulum (ER) organization and also arrest growth in early seedling development, while a weaker allele (gsh2-6) reached maturity but was smaller than the wild type (Au et al., 2012). A screen for reduced response to Cd also yielded a viable missense mutant of GSH2 (nonresponse or reduced response to Cd2) with approximately 75% of the wild-type GSH level (Jobe et al., 2012).Plant oxidative stress responses involve both redox signaling through GSH and jasmonate hormonal signaling, and gene expression studies have clearly linked these two signaling systems. GSH biosynthesis and metabolism genes are induced by jasmonate, while manipulating GSH level or redox status in various mutants alters expression of genes for jasmonate biosynthesis and signaling (Xiang and Oliver, 1998; Mhamdi et al., 2010; Han et al., 2013). GSH and jasmonate are also associated with protective glucosinolate production in response to insect feeding (Noctor et al., 2011). For example, pad2-1 is deficient in glucosinolates and more susceptible to insects, while several studies have shown jasmonate induces glucosinolates (Brader et al., 2001; Mikkelsen et al., 2003; Sasaki-Sekimoto et al., 2005; Schlaeppi et al., 2008). Liu et al. (2010) isolated jasmonic acid hypersensitive1 (jah1), an Arabidopsis mutant with greater inhibition of root growth than the wild type in the presence of jasmonic acid (JA). The affected gene encodes a cytochrome P450 (CYP82C3) involved in indole glucosinolate production, and this mutant was more susceptible to Botrytis cinerea.The basic mechanism of jasmonate signal transduction and some of the downstream responses emanating from it are now well understood (Browse, 2009; Wasternack and Hause, 2013). However, the mechanisms by which jasmonate and GSH coordinate their activities to mediate oxidative stress and other responses are not known. This study characterized, to our knowledge, a new jasmonate-hypersensitive mutant that accumulates excess γ-EC due to a defect in GSH2, but GSH is only modestly reduced. Results show that elevated γ-EC is deleterious to plant growth through a jasmonate-dependent mechanism. 相似文献
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Lipoteichoic acid is an important microbe-associated molecular pattern of Lactobacillus rhamnosus GG
Claes Ingmar JJ Segers Marijke E Verhoeven Tine LA Dusselier Michiel Sels Bert F De Keersmaecker Sigrid CJ Vanderleyden Jos Lebeer Sarah 《Microbial cell factories》2012,11(1):1-8
Background
Receptors with a single transmembrane (TM) domain are essential for the signal transduction across the cell membrane. NMR spectroscopy is a powerful tool to study structure of the single TM domain. The expression and purification of a TM domain in Escherichia coli (E.coli) is challenging due to its small molecular weight. Although ketosteroid isomerase (KSI) is a commonly used affinity tag for expression and purification of short peptides, KSI tag needs to be removed with the toxic reagent cyanogen bromide (CNBr).Result
The purification of the TM domain of p75 neurotrophin receptor using a KSI tag with the introduction of a thrombin cleavage site is described herein. The recombinant fusion protein was refolded into micelles and was cleaved with thrombin. Studies showed that purified protein could be used for structural study using NMR spectroscopy.Conclusions
These results provide another strategy for obtaining a single TM domain for structural studies without using toxic chemical digestion or acid to remove the fusion tag. The purified TM domain of p75 neurotrophin receptor will be useful for structural studies. 相似文献10.