Showing papers in "Plant and Cell Physiology in 1993"
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TL;DR: Changes in carbon fixation rate and the levels of photosynthetic proteins were measured in fourth leaves of Lolium temulentum grown until full expansion at 360μmol quanta m -2 s -1 and subsequently at the same irradiance.
Abstract: Changes in carbon fixation rate and the levels of photosynthetic proteins were measured in fourth leaves of Lolium temulentum grown until full expansion at 360μmol quanta m -2 s -1 and subsequently at the same irradiance or shaded to 90μmol m -2 s -1
TL;DR: A search for homologies in a protein database (NBRF) revealed that the predicted protein product has a functional peptide domain that resembles that of 2-oxoglutarate-dependent dioxygenases.
Abstract: To clone genes required for the synthesis of mugineic acid (MA) or for the transport of Fe(III)-MA, a lambda ZAPII cDNA library was constructed from poly(A)(+)-RNA isolated from Fe-deficient barley roots. The cDNA library was then used for differential screening of barley roots that had been grown in the presence and absence of iron. Seven clones that hybridized specifically to the probe for Fe deficiency were selected. One clone, presumably encoding a full-length mRNA, as deduced from Northern hybridization, was sequenced. The clone consisting of 1685 nucleotides encoded a putative protein of 169 amino acids and an M(r) of 18704. The gene was specifically expressed in the roots of iron-deficient barley. A search for homologies in a protein database (NBRF) revealed that the predicted protein product has a functional peptide domain that resembles that of 2-oxoglutarate-dependent dioxygenases.
TL;DR: The accumulation and distribution of betaine and the distribution of Betaine aldehyde dehydrogenase, which catalyzes the last step in the synthesis ofbetaine, were analysed in leaves of control and salt-stressed cereal plants of the Gramineae.
Abstract: The accumulation of betaine and the distribution of betaine aldehyde dehydrogenase, which catalyzes the last step in the synthesis of betaine, were analysed in leaves of control and salt-stressed cereal plants of the Gramineae
TL;DR: The 200 kDa protein induced specifically by low temperature in wheat is the largest member of a family of immunologically-related cold-induced proteins in wheat, and protein sequence and immunological analyses indicate that this protein shares similar features with the 50 kDaprotein induced during cold acclimation of wheat.
Abstract: We have purified to homogeneity the 200 kDa protein induced specifically by low temperature in wheat (Triticum aestivum L.). The boiling solubility of the protein has been used as a main step in the purification procedure. Amino acid composition indicates that the 200 kDa has a compositional bias for glycine (11.4%), threonine (13.3%), and alanine (22.0%). Using oligonucleotide probes, we have isolated a clone (p Wcs200) from a cold-acclimated winter wheat cDNA library. Northern analysis demonstrated that the expression of the corresponding gene was specifically upregulated by low temperature. Southern analysis showed that the gene organization and the relative copy number were identical in two cultivars differing in their capacity to develop freezing tolerance. Protein sequence and immunological analyses indicate that this protein shares similar features with the 50 kDa protein induced during cold acclimation of wheat. The two proteins are boiling-soluble, and possess similar repeated elements. These elements may be important for the development of freezing tolerance. We have shown that the 200 kDa protein is the largest member of a family of immunologically-related cold-induced proteins in wheat. Expression of pWcs200 in E. coli yielded a product of around 200 kDa, indicating that the clone contains most of the coding region for this protein.
TL;DR: The isotopic fractionation of nitrogen in the reaction in vitro of glutamine synthetase isolated from spinach leaves was calculated from the changes in natural 15 N abundance of ammonia and amide of glutamines during the incubation.
Abstract: The isotopic fractionation of nitrogen in the reaction in vitro of glutamine synthetase isolated from spinach leaves was calculated from the changes in natural 15 N abundance of ammonia and amide of glutamine during the incubation
TL;DR: A targeted mutant YFM6D-3 exhibited a phenotype similar to that of YFC1004, an frxC-disrupted mutant, which did not synthesize chlorophyll and accumulated Pchlide, a precursor to Chl, in the dark, indicating that the light-independent reduction of PChlide requires not only the FrxC protein but also the ORF467 protein.
Abstract: The frxC gene, which is found in chloroplast DNA (ctDNA) and in cyanobacteria, encodes a protein that is required for the light-independent reduction of protochlorophyllide (Pchlide) to chlorophyllide a (Chlide). A DNA fragment downstream of frxC in the filamentous cyanobacterium Plectonema boryanum was cloned and analyzed. Sequencing of the DNA fragment revealed an open reading frame (ORF) that encoded a protein of 467 amino acid residues (designated ORF467), which showed extensive homology to the proteins encoded by genes on ctDNAs (ORF465 in liverwort, gidA in pine and chlN in Chlamydomonas reinhardtii) and to ORF469 protein of the cyanobacterium Synechocystis sp. strain PCC 6803. We isolated a targeted mutant YFM6D-3 in which ORF467 was inactivated by the insertion of a kanamycin-resistance gene into the coding region. YFM6D-3 exhibited a phenotype similar to that of YFC1004, an frxC-disrupted mutant, which did not synthesize chlorophyll (Chl) and accumulated Pchlide, a precursor to Chl, in the dark. These phenotypic characteristics of YFM6D-3 indicate that the light-independent reduction of Pchlide requires not only the FrxC protein but also the ORF467 protein. The amino acid sequences of the homologues of ORF467 exhibit low but significant similarity to those of the alpha and beta subunits of nitrogenase MoFe-protein, suggesting a phylogenetic relationship between the light-independent Pchlide reductase and nitrogenase, as is observed between the FrxC protein and the Fe-protein of nitrogenase.
TL;DR: Eleven cDNA clones were isolated from a pea (Pisum sativum) leaf cDNA library which were similar to small GTP-binding proteins, andPhylogenetic analysis showed that these clones can be classified into two subgroups: proteins encoded by pra1 to pra7 being related to ypt3 and rab11 proteins; and proteins encode by pra9A, pra9B, and pra9Cbeing related to YPT1 and rab1 proteins.
Abstract: Eleven cDNA clones (pra1 to pra9A, pra9B, and pra9C) were isolated from a pea (Pisum sativum) leaf cDNA library which were similar to small GTP-binding proteins. These cDNAs encoded proteins of 22-25 kDa, which exhibited 45-92% identity to one another at the amino acid level. The putative proteins included the characteristic sequences of ras-related small GTP-binding proteins: four conserved domains involved in binding of GTP/GDP; an effector domain; and cysteine residues at the COOH-terminus. Indeed, the pra6 protein, expressed in Escherichia coli, clearly showed GTP-binding activity. Phylogenetic analysis showed that these clones can be classified into two subgroups: proteins encoded by pra1 to pra7 being related to ypt3 and rab11 proteins; and proteins encoded by pra8, pra9A, pra9B, and pra9C being related to YPT1 and rab1 proteins. The effector sequences in these two subgroups were different. RNA gel blot analysis showed that most of the corresponding genes are differentially expressed in pea leaves and roots. Variations in expression were also observed for structurally related genes.
TL;DR: The levels of prolamines and glutelins, the storage proteins of rice, were quantified during seed development by immunoblot analysis.
Abstract: The levels of prolamines and glutelins, the storage proteins of rice, were quantified during seed development by immunoblot analysis
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