Circadian Oscillations of a Transcript Encoding a Germin-Like Protein That Is Associated with Cell Walls in Young Leaves of the Long-Day Plant Sinapis alba L

Heintzen, Christian; Fischer, Roland; Melzer, Slegbert; Kappeler, Stefan; Apel, Klaus; Staiger, Dorothee

doi:10.1104/pp.106.3.905

Cited by 87 publications

(75 citation statements)

References 39 publications

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“…In our data, mRNA undergoes rapid damping after plants were transferred to darkness. A similar feature was shown on mustard (Sinapsis alba) germin-like protein (SaGLP; Heintzen et al, 1994), in which mRNA could no longer be detected after 1 d in DD, even if its expression is endogenously clock controlled. Like SaGLP, PcISPS and PcPSY are under circadian control, but light positively influences their expression.…”

Section: Discussionmentioning

confidence: 67%

Circadian Rhythms of Isoprene Biosynthesis in Grey Poplar Leaves

et al. 2006

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Isoprene (2-methyl-1,3-butadiene) emission varies diurnally in different species. In poplar (Populus spp.), it has recently been shown that the gene encoding the synthesizing enzyme for isoprene, isoprene synthase (ISPS), displays diurnal variation in expression. Working on shoot cultures of Grey poplar (Populus 3 canescens) placed under a different light regime in phytochambers, we showed that these variations in PcISPS gene expression, measured by quantitative real-time polymerase chain reaction, are not only due to day-night changes, but also are linked to an internal circadian clock. Measurement of additional selected isoprenoid genes revealed that phytoene synthase (carotenoid pathway) displays similar fluctuations, whereas 1-deoxy-D-xylulose 5-phosphate reductoisomerase, possibly the first committed enzyme of the 1-deoxy-D-xylulose 5-phosphate pathway, only shows light regulation. On the protein level, it appeared that PcISPS activity and protein content became reduced under constant darkness, whereas under constant light, activity and protein content of this enzyme were kept high. In contrast, isoprene emission rates under continuous irradiation displayed circadian changes as is the case for gene expression of PcISPS. Furthermore, binding assays with Arabidopsis (Arabidopsis thaliana) late elongated hypocotyl, a transcription factor of Arabidopsis involved in circadian regulation, clearly revealed the presence of circadian-determining regulatory elements in the promoter region of PcISPS.

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Section: Discussionmentioning

confidence: 67%

Circadian Rhythms of Isoprene Biosynthesis in Grey Poplar Leaves

et al. 2006

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“…Germin was first detected in germinating cereals, but subsequently, germin-like proteins were also identified in a protist (Lane, 1991), dicotyledonous angiosperms (Delseny et al, 1994;Heintzen et al, 1994), and gymnosperms (Domon et al, 1995). Germins and germin-like proteins constitute a large family of proteins ubiquitously distributed in the plant kingdom.…”

Section: Introductionmentioning

confidence: 99%

Localization of Germin Genes and Their Products in Developing Wheat Coleoptiles

Çalışkan¹,

Özcan²,

Turan³

et al. 2004

BMB Reports

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Germination is a process which characterized with nescient synthesis of genes. Among the genes synthesized during the germination of wheat embryos, germin genes, proteins and their enzymatic activity were defined. Germin is a water soluble homopentameric glycoprotein which is remarkable resistant to degradation by a broad range of proteases including pepsin. Germin proteins found to have strong oxalate oxidase activity which produces hydrogen peroxide by degrading oxalic acid. The current study, aimed to localize the germin genes, proteins and enzymatic activities in developing coleoptiles which is a rapidly growing protective tissue of leaf primordium and shoot apex. Non-radioactively labeled germin riboprobes were employed to localize germin mRNAs in situ. FITC (Fluorescein isothiocyanate) and alkaline phosphatase linked anti-germin antibodies were used to localize germin proteins under the fluorescence and light microscopy and finally germin enzymatic activity was localized by using appropriate enzyme assay. The results revealed that in coleoptiles germin genes, proteins and their enzymatic activity were predominantly associated with the cells of epidermis and vascular bundle sheath cells.

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“…It has been found that some are expressed at critical developmental stages such as embryogenesis (Domon et al 1995;Neutelings, 1998) or floral induction (Heintzen et al 1994;Staiger et al 1999), and many are induced by a rangeof stresses, either biotic, such as infection with powdery mildew (ThordahlChristensen et al 1997;Schweizer et al 1999), or abiotic, such as exposure to salt (Hurkman and Tanaka, 1996), aluminum (Hamel et al 1998),or high temperatures (Vallelian-Bindschedler et al 1998). Present study demonstrates that peanut Gly-1 is specific to embryogenesis and expressed during early embryo development.…”

Section: Discussionmentioning

confidence: 99%

Cloning and structural analysis of a cDNA clone encoding glycinin (Gly-1) seed storage protein of peanut

Jain¹

2004

Electro Journal of Biotech

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A cDNA clone (peanut Gly-1) encoding for glycinin protein was isolated from the immature seeds (from yellow-1 maturity pods) and characterized. The clone spanning a total of 1836 bp, predicted protein of 529 amino acid residues with a calculated mass of 60,447.61 Da. Peanut Gly-1 sequence comparison shows high level of sequence homology with other two peanut glycinin (arachin) genes [Ara h3 (95%) and Ara h4 (94%)] and glycinin (legumin) genes of other legumes such as soybean, broad bean, French bean and pea etc., both at nucleotide (67 to 69%) and amino acid (60 to 63%) levels. The N-and C-terminals of peanut Gly-1 are highly conserved with other glycinin genes; central region of the gene possess three variable regions, which also show conservation with other glycinin genes. peanut glycinin-1 gene deciphers 11S type A seed storage protein. Mapping for conserved domains indicate that peanut Gly-1 consists of bi-cupin domain.RNA gel blot studies demonstrate that the gene expressed during embryo development that is transcriptionally activated early in embryogenesis (white pod maturity) and is repressed late in seed maturation (orange pod maturity stage). Peanut Gly-1 does not express in other tissues like leaf, stem, root, flower, pegs or post germinating seedlings.Seed proteins are an extremely and increasingly important component of nutrition for both humans and animals (Shewry and Casey, 1999). Plant proteins are the cheapest available sources of protein in many countries where few can afford meat or dairy products, hence are an important part of human diet. Supply of proteins from plant is considered an ideal source of protein to humans without the concern of cholesterol and legumes have been well documented for their high seed storage protein contents (Shewry and Casey, 1999).Peanut (Arachis hypogaea L.), a legume with 24% protein (Cherry, 1977), is a major source of plant protein in most tropical and subtropical regions of the world. In the United States, peanuts are mostly grown in the southern states and they have significant economic impact. Peanuts are the third most important source of plant protein and provide approximately 11% of the world's protein supply. The globulin fraction of peanut seed consists of arachin (glycinin or legumin) and con-arachin (vicilin or conglycinin) (Johnson et al. 1950;Cherry et al. 1973). Of the globulins, glycinin (arachin) accounts for more than 50% of the total protein (Jones and Horn, 1930). Glycinin is superior to con-glycinin from the viewpoint of nutritional value (Millerd, 1975) as well as functional properties (Kinsella, 1978). Immunological studies also demonstrate that glycinin type seed storage peanut proteins (such as Ara h3 and Ara h4) are less severe compared to their vicilin (Ara h1) and conglutin (Ara h2) type seed storage proteins (Burks et al. 1995;Shin et al. 1998;Viquez et al. 2003;Koppelman et al. 2004). It is obvious, that it is important to understand the biosynthesis, targeting and biological functions of seed proteins as a prerequisite to their rati...

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Circadian Oscillations of a Transcript Encoding a Germin-Like Protein That Is Associated with Cell Walls in Young Leaves of the Long-Day Plant Sinapis alba L

Cited by 87 publications

References 39 publications

Circadian Rhythms of Isoprene Biosynthesis in Grey Poplar Leaves

Circadian Rhythms of Isoprene Biosynthesis in Grey Poplar Leaves

Localization of Germin Genes and Their Products in Developing Wheat Coleoptiles

Cloning and structural analysis of a cDNA clone encoding glycinin (Gly-1) seed storage protein of peanut

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