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  • 1
    Electronic Resource
    Electronic Resource
    Isolation and characterization of cytoplasmic and chloroplastic ribosomes and their ribosomal RNAs from the diatom Cylindrotheca fusiformis (1977)
    Springer
    Archives of microbiology 111 (1977), S. 247-253 
    Details
    ISSN: 1432-072X
    Keywords: Diatom ; Cylindrotheca fusiformis ; Ribosomes ; Ribosomal RNA ; Evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cytoplasmic and chloroplast ribosomes from the marine diatom Cylindrotheca fusiformis were isolated and characterized. The cytoplasmic ribosomes sedimented in sucrose at 84S and dissociated into subunits of 64S and 42S in the absence of Mg2+. It contained ribosomal RNAs with molecular weights of 1.31×106 and 0.70×106. The chloroplast ribosomes sedimented at 70S only in the presence of high Mg2+ concentrations (25–100 mM). No stable subunits were routinely observed and at very high levels of Mg2+ (〉100 mM) the 70S species was converted to a form sedimenting at 55S. At 4°C ribosomal RNAs with molecular weights of 1.1×106 and 0.40×106 were detected on polyacrylamide gel electrophoresis. When the RNAs were resolved at room temperature the large molecular weight component disappeared while RNA with molecular weights of 0.65×106 and 0.53×106 were observed. Apparently the large chloroplast RNAs dissociated into two pieces of unequal molecular weight. These properties of the diatom's chloroplast ribosomes are very similar to those of the counter parts in unicellular green algae, which suggests that both types of algae have a common phylogenetic ancestor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00549362
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  • 2
    Electronic Resource
    Electronic Resource
    Messenger RNA targeting of rice seed storage proteins to specific ER subdomains (2000)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 407 (2000), S. 765-767 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Rice seeds, a rich reserve of starch and protein, are a major food source in many countries. Unlike the seeds of other plants, which typically accumulate one major type of storage protein, rice seeds use two major classes, prolamines and globulin-like glutelins. Both storage proteins are ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/35037633
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  • 3
    Electronic Resource
    Electronic Resource
    COMPARTMENTATION OF PROTEINS IN THE ENDOMEMBRANE SYSTEM OF PLANT CELLS (1996)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology and Plant Molecular Biology 47 (1996), S. 327-350 
    Details
    ISSN: 1040-2519
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract This review focuses on four interrelated processes in the plant endomembrane system: compartmentation of proteins in subdomains of the endoplasmic reticulum, mechanisms that determine whether storage proteins are retained within the ER lumen or transported out, the origin and function of biochemically distinct vacuoles or prevacuolar organelles, and the cellular processes by which proteins are sorted to vacuolar compartments. We postulate that ER-localized protein bodies are formed by a series of orderly events of protein synthesis, protein concentration, and protein assembly in subdomains of the ER. Protein concentration, which facilitates protein-to-protein interactions and subsequent protein assembly, may be achieved by the interactions with chaperones and by the localization of storage protein mRNAs. We also describe recent developments on the coexistence of two biochemically distinguishable vacuolar compartments, the possible direct role of the ER in vacuole biogenesis, and proposed mechanisms for transport of proteins from the ER or Golgi apparatus to the vacuole.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.arplant.47.1.327
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  • 4
    Electronic Resource
    Electronic Resource
    Developing prolamine protein bodies are associated with the cortical cytoskeleton in rice endosperm cells (2000)
    Springer
    Planta 211 (2000), S. 227-238 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Cortical cytoskeleton ; Endoplasmic reticulum subdomain ; Endosperm ; mRNA localization ; Oryza sativa ; Protein body
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract.  The mRNAs that encode the prolamine storage proteins in rice (Oryza sativa L.) endosperm cells are enriched on the surface of the prolamine protein bodies (PBs), a subcellular structure consisting of a prolamine intracisternal granule surrounded by rough endoplasmic reticulum membrane. Previous biochemical studies (D.G. Muench et al., 1998, Plant Physiol. 116: 559–569) have shown that prolamine mRNAs may be anchored to the PB surface via the cytoskeleton. To better understand the mechanism and role of mRNA localization in rice endosperm cells, we studied the subcellular development of prolamine PBs and their relationship with the cytoskeleton in rice endosperm cells. Confocal microscopy of endosperm cells showed that, unlike the glutelin PBs, the developing prolamine PBs are not randomly distributed within the cell, but instead are often enriched in the cortical region of the cell only a few micrometers beneath the plasma membrane. In addition, the peripheral prolamine PBs are closely associated with the cortical microtubule and actin filament networks. The cortical enrichment of rice prolamine protein bodies represents a unique example of endoplasmic reticulum subdomain localization in plant cells. The interaction of this endoplasmic reticulum subdomain with the cytoskeleton provides new insights on the possible mechanism and role of mRNA localization in plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008159
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  • 5
    Electronic Resource
    Electronic Resource
    Formation of wheat protein bodies: Involvement of the Golgi apparatus in gliadin transport (1988)
    Springer
    Planta 176 (1988), S. 173-182 
    Details
    ISSN: 1432-2048
    Keywords: Gliadin ; Golgi apparatus ; Protein deposition ; Storage protein ; Triticum (protein bodies)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Developing wheat (Triticum aestivum L.) endosperm was examined using ultrathin sections prepared from tissues harvested at 5, 9, 16 and 25 d after flowering. Protein bodies were evident by 9 d and displayed a variety of membranous structures and inclusions. The Golgi apparatus was a prominent organelle at all stages, and by 9 d was associated with small electron-dense inclusions. By immunocytochemical techniques, gliadin (wheat prolamine) was localized within these vesicles and in homogeneous regions of protein bodies, but not in the lumen of the rough endoplasmic reticulum. The protein bodies appear to enlarge by fusion of smaller protein bodies resulting in larger, irregular-shaped organelles. The affinity of the Golgi-derived vesicles for gliadin-specific probes during the period of maximal storage-protein synthesis and deposition indicates that this organelle includes the bulk, if not all, of the gliadin produced. The involvement of the Golgi apparatus in the packaging of gliadins into protein bodies indicates a pathway which differs from the mode of prolamine deposition in other cereals such as maize, rice and sorghum, and resembles the mechanism employed for the storage of rice glutelin and legume globulins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392442
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  • 6
    Electronic Resource
    Electronic Resource
    Feedback inhibition of photosynthesis in rice measured by O2 dependent transients (1999)
    Springer
    Photosynthesis research 59 (1999), S. 187-200 
    Details
    ISSN: 1573-5079
    Keywords: chlorophyll fluorescence ; CO2 ; oxygen ; photosynthesis ; rice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The kinetic properties of photosynthesis (both transient and steady-state) were monitored using three non-invasive techniques to evaluate limitations on triose-phosphate (triose-P) conversion to carbohydrate in rice. These included analyzing the O2 sensitivity of CO2 fixation and the assimilatory charge (AC) using gas exchange (estimate of the ribulose 1,5- bisphosphate pool) and measuring Photosystem II activity by chlorophyll fluorescence analysis under varying light, temperature and CO2 partial pressures. Photosynthesis was inhibited transiently upon switching from 20 to 2 kPa O2 (reversed O2 sensitivity), the degree of which was correlated with a terminal, steady-state suppression of low O2 enhancement of photosynthesis. Under current ambient levels of CO2 and moderate to high light, the transient pattern was more obvious at 18 °C than at 26 °C while at 34 °C no tra nsient response was observed. The transient inhibition at 18 °C ranged from 15% to 31% depending on the pre-measurement temperature. This pattern, symptomatic of feedback, was observed with increasing light and CO2 partial pressures with the degree of feedback decreasing from moderate (18 °C) up to high temperature (34 °C). Under feedback conditions, the rate of assimilation is shifted from being photorespiration limited to being triose-P utilization limited. Transitory changes in CO2 assimilation rates (A) under low O2 indicative of feedback coincided with a transitory drop in assimilatory charge (AC) and inhibition of electron transport. In contrast to previous studies with many C3 species, our studies indicate that rice shows susceptibility to feedback inhibition under moderate temperatures and current atmospheric levels of CO2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006180102395
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  • 7
    Electronic Resource
    Electronic Resource
    Analysis of nuclear proteins interacting with a wheat α/β-gliadin seed storage protein gene (1993)
    Springer
    Plant molecular biology 22 (1993), S. 25-41 
    Details
    ISSN: 1573-5028
    Keywords: gliadin storage proteins ; wheat ; transcriptional regulation ; nuclear proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The promoter region (−524 to −46) of the wheat α/β-gliadin seed storage protein gene was analyzed for interactions with nuclear proteins from developing wheat seeds. Six complexes were detected within the first 165 bp upstream of the transcriptional start site. One of the proteins was a non-sequence specific AT-binding protein. The remaining five proteins bound in a sequence specific manner. One (CABP) mapped to a conserved CA-rich element at −134 to −112 while another (PalBP) mapped to an adjacent, palindromic sequence at −112 to −106. Three proteins (CTBPs 1–3) formed complexes at two, independent homologous sites. The activities of four of the binding proteins, CTBPs 1–3 and CABP, exhibited similar patterns of expression during seed development: they first appeared at early to mid stages, reached a maximum at mid stage and subsequently decreased, paralleling the pattern of gliadin mRNA accumulation. The non-specific AT-binding protein was detected at relatively high levels only at mid development. PalBP activity, on the other hand, first appeared at mid stage and was present at a constant level throughout later stages of development. The results suggest that the binding proteins may regulate gliadin expression in an antagonistic manner.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00038993
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  • 8
    Electronic Resource
    Electronic Resource
    Analysis of randomly isolated cDNAs from developing endosperm of rice (Oryza sativa L.): evaluation of expressed sequence tags, and expression levels of mRNAs (1995)
    Springer
    Plant molecular biology 29 (1995), S. 685-689 
    Details
    ISSN: 1573-5028
    Keywords: rice ; endosperm ; cDNA ; ESTs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using a cDNA library prepared from poly(A)+ RNA from 10-day-old rice endosperm, partial nucleotide sequences of randomly isolated clones were analyzed. A total of 153 (30.6%) out of 500 cDNA clones showed high amino acid identity to previously identified genes. There was significant redundancy in cDNAs encoding prolamine and glutelin. About 21.0% of the cDNA clones were found to code for seed storage protein genes. Consequently, 37 independent genes were identified. Using cDNA clones encoding glutelin, prolamine, seed allergen, α-1,4-glucan branching enzyme, glycine-rich RNA binding protein, metallothionein, non-specific lipid-transfer protein and ubiquitin conjugating enzyme the accumulation of mRNA during rice seed development was compared. Genes associated with seed storage protein and starch biosynthesis were expressed according to expected developmental stages. Glycinerich RNA binding protein genes as well as metallothionein-like protein genes were highly expressed in developing seeds, but low in leaves of whole plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00041159
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  • 9
    Electronic Resource
    Electronic Resource
    Accurate in vitro transcription of plant promoters with nuclear extracts prepared from cultured plant cells (1991)
    Springer
    Plant molecular biology 16 (1991), S. 771-786 
    Details
    ISSN: 1573-5028
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A simple method is presented for the preparation of nuclear extracts from suspension cultures of rice, wheat and tobacco cells. These extracts are shown to be capable of RNA Polymerase II-dependent transcription from two plant promoters in vitro; a 250 bp fragment of a wheat gliadin promoter containing sequences from −167 bp to +83 relative to the in vivo transcriptional initiation site and two fragments of the CaMV 35S promoter, containing sequences from −419 to +17, and from −90 to +17. Using the rice extract, transcription is shown to be extract-dependent, DNA-dependent, α-amanatin-sensitive, promoter-dependent, and accurate with respect to initiation site selection on the gliadin promoter and the −90 to +17 35S promoter, but not accurate on the −419 to +17 35S promoter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00015070
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  • 10
    Electronic Resource
    Electronic Resource
    Tissue-specific expression and temporal regulation of the rice glutelin Gt3 gene are conferred by at least two spatially separatedcis-regulatory elements (1994)
    Springer
    Plant molecular biology 25 (1994), S. 429-436 
    Details
    ISSN: 1573-5028
    Keywords: glutelin storage protein ; transcriptional regulation ; rice ; promoter analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The rice glutelin Gt3 promoter was fused to a β-glucuronidase (GUS) reporter gene and its expression evaluated in transgenic tobacco plants. Histochemical analysis revealed that the expression of the introduced Gt3 promoter/GUS (β-glucuronidase) chimeric gene was confined to endosperm tissue of developing seeds. 5′-promoter deletion analysis revealed that two domains of the Gt3 promoter, -346 to -263 bp (domain I) and -945 to -726 bp (domain II) from the transcriptional start site, were essential for optimum expression of the GUS reporter gene. Removal of 5′ sequences upstream of -726 resulted in a reduction in overall promoter activity and a shift in temporal expression from a maximum of 16–20 days after flowering to 24 days. Removal of DNA sequences from the 5′ end to -346 yielded a promoter fragment that was still able to confer endosperm-specific expression, although a further deletion to -263 abolished promoter activity. These data suggest that at least twocis-regulatory elements are required for endosperm specificity and temporal regulation of glutelin Gt3 gene expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00043871
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