The Effect of Grain Number per Ear (Sink Size) on Source Activity and its Water-Relations in Wheat

Blum, A., Mayer, J. and Golan, G. 1988. The effect of grainnumber per ear (sink size) on source activity and its water-relationsin wheat.–J. exp. Bot. 39: 106–114. Work was done to evaluate the nature of sink-source relationshipsin wheat (Triticum aestivum L.), when the strength of the sinkwas modified by the removal of half of the grain from the earat about anthesis. The main hypothesis was that sink-sourcerelationship would be modified by water stress and that a weakersink would improve the drought resistance of the source. Two experiments were performed. The first experiment evaluatedthe effect of de-graining in two wheat varieties grown in thefield. The second experiment (in the greenhouse) evaluated theeffect of de-graining in plants subjected to water stress afteranthesis by immersing the root system in a solution of polyethyleneglycol (6000), as compared with non-stressed controls. In bothexperiments measurements were performed after de-graining toprovide data on leaf gas exchange, leaf water potential, osmoticadjustment of leaves and ears (greenhouse), the percent of stemweight loss as an index of stem reserve mobilization, finalroot weight (greenhouse) and ear weight components. De-graining caused a decrease in flag leaf stomatal conductance,carbon exchange rate (CER) and transpiration and an increasein flag leaf water potential. These effects were stronger withwater stress. De-graining did not affect osmotic adjustmentin the flag leaf but induced better adjustment in glumes andawns. De-graining decreased the percent of stem weight lossand increased final root weight, especially under drought stress. A weaker sink was, therefore, considered to improve plant droughtresistance in terms of the maintenance of higher leaf waterpotential, a larger root, a better osmotic adjustment in theear and, possibly, increased flag leaf longevity. The ‘cost’of this improved drought resistance was in reduced flag leafCER and reduced stem (and root?) reserve mobilization. Key words: Drought resistance, carbon exchange rate, stomata, transpiration, osmotic adjustment, leaf water potential, root, awns, yield     

Phylogenetic utility of the nuclear gene arginine decarboxylase: an example from Brassicaceae

Arginine decarboxylase (ADC) is an important enzyme in the production of putrescine and polyamines in plants. It is encoded by a single or low-copy nuclear gene that lacks introns in sequences studied to date. The rate of Adc amino acid sequence evolution is similar to that of ndhF for the angiosperm family studied. Highly conserved regions provide several target sites for PCR priming and sequencing and aid in nucleotide and amino acid sequence alignment across a range of taxonomic levels, while a variable region provides an increased number of potentially informative characters relative to ndhF for the taxa surveyed. The utility of the Adc gene in plant molecular systematic studies is demonstrated by analysis of its partial nucleotide sequences obtained from 13 representatives of Brassicaceae and 3 outgroup taxa, 2 from the mustard oil clade (order Capparales) and 1 from the related order Malvales. Two copies of the Adc gene, Adc1 and Adc2, are found in all members of the Brassicaceae studied to data except the basal genus Aethionema. The resulting Adc gene tree provides robust phylogenetic data regarding relationships within the complex mustard family, as well as independent support for proposed tribal realignments based on other molecular data sets such as those from chloroplast DNA.      

Patterns of divergence during evolution of alpha 1-proteinase inhibitors in mammals

alpha 1-Proteinase inhibitor (alpha 1-PI), a member of the serine proteinase inhibitor superfamily, has a primary role in controlling neutrophil elastase activity within the mammalian circulation. Several studies have indicated that the reactive center region of alpha 1-PI, the amino acid sequence of which is critical to recognition of and binding to target proteinases, is highly divergent within and among species. This appears to be a consequence of accelerated rates of evolution that may have been driven by positive Darwinian selection. In order to examine this and other features of alpha 1-PI evolution in more detail, we have isolated and sequenced cDNAs representing alpha 1- PI mRNAs of the mouse species Mus saxicola and Mus minutoides and have compared these with a number of other mammalian alpha 1-PI mRNAs. Relative to other mammalian mRNAs, the extent of nonsynonymous substitution is generally high throughout the alpha 1-PI mRNA molecule, indicating greater overall rates of amino acid substitution. Within and among mouse species, the 5'-half of the mRNA, but not the 3'-half, has been homogenized by concerted evolution. Finally, the reactive center is under diversifying or positive Darwinian selection in murid rodents (rats, mice) and guinea pigs yet is under purifying selection in primates and artiodactyls. The significance of these findings to alpha 1-PI function and the possible selective forces driving evolution of serpins in general are discussed.      

Isocitrate dehydrogenase 1 R132C mutation occurs exclusively in microsatellite stable colorectal cancers with the CpG island methylator phenotype

The CpG Island Methylator Phenotype (CIMP) is fundamental to an important subset of colorectal cancer; however, its cause is unknown. CIMP is associated with microsatellite instability but is also found in BRAF mutant microsatellite stable cancers that are associated with poor prognosis. The isocitrate dehydrogenase 1 (IDH1) gene causes CIMP in glioma due to an activating mutation that produces the 2-hydroxyglutarate oncometabolite. We therefore examined IDH1 alteration as a potential cause of CIMP in colorectal cancer. The IDH1 mutational hotspot was screened in 86 CIMP-positive and 80 CIMP-negative cancers. The entire coding sequence was examined in 81 CIMP-positive colorectal cancers. Forty-seven cancers varying by CIMP-status and IDH1 mutation status were examined using Illumina 450K DNA methylation microarrays. The R132C IDH1 mutation was detected in 4/166 cancers. All IDH1 mutations were in CIMP cancers that were BRAF mutant and microsatellite stable (4/45, 8.9%). Unsupervised hierarchical cluster analysis identified an IDH1 mutation-like methylation signature in approximately half of the CIMP-positive cancers. IDH1 mutation appears to cause CIMP in a small proportion of BRAF mutant, microsatellite stable colorectal cancers. This study provides a precedent that a single gene mutation may cause CIMP in colorectal cancer, and that this will be associated with a specific epigenetic signature and clinicopathological features.     

PROPERTIES AND CHANGES OF GLUCOSE-6-PHOSPHATE DEHYDROGENASE IN GERMINATING LETTUCE SEEDS

Glucose-6-phosphate dehydrogenase is present in lettuce seedsand seedlings in a particulate, 20,000 g fraction and in a solublefraction of the cells. In both fractions the enzyme activityoccurs in the presence of either NAD or NADP. It seems probablethat an enzyme with two active sites is involved. Total activity does not change during 48 hours germination inwater. It is depressed by coumarin or thiourea treatment. Specificactivity rises in the soluble fraction when germination occurs,but not in the mitochondrial one. Coumarin treatment largelydepresses the increase in specific activity. In vitro 100 ppmcoumarin totally inhibit enzyme activity. 1,250 ppm thioureado not affect enzyme activity. The results are analysed and it is concluded that glucose-6-phosphatedehydrogenase is important, if at all, only in the very earlystages of germination. (Received August 13, 1965; )     

Evolution of eutherian cytochrome c oxidase subunit II: heterogeneous rates of protein evolution and altered interaction with cytochrome c

Cytochrome c oxidase subunit II (COII), encoded by the mitochondrial genome, exhibits one of the most heterogeneous rates of amino acid replacement among placental mammals. Moreover, it has been demonstrated that cytochrome c oxidase has undergone a structural change in higher primates which has altered its physical interaction with cytochrome c. We collected a large data set of COII sequences from several orders of mammals with emphasis on primates, rodents, and artiodactyls. Using phylogenetic hypotheses based on data independent of the COII gene, we demonstrated that an increased number of amino acid replacements are concentrated among higher primates. Incorporating approximate divergence dates derived from the fossil record, we find that most of the change occurred independently along the New World monkey lineage and in a rapid burst before apes and Old World monkeys diverged. There is some evidence that Old World monkeys have undergone a faster rate of nonsynonymous substitution than have apes. Rates of substitution at four-fold degenerate sites in primates are relatively homogeneous, indicating that the rate heterogeneity is restricted to nondegenerate sites. Excluding the rate acceleration mentioned above, primates, rodents, and artiodactyls have remarkably similar nonsynonymous replacement rates. A different pattern is observed for transversions at four-fold degenerate sites, for which rodents exhibit a higher rate of replacement than do primates and artiodactyls. Finally, we hypothesize specific amino acid replacements which may account for much of the structural difference in cytochrome c oxidase between higher primates and other mammals.