NYB is chlorophyll-less barley mutant, which is controlled by a recessive nuclear gene. The mutation mechanism is revealed. The activities of enzymes transforming 5-aminolevulinic acid into protochlorophyllide were the same in both NYB and the wild type (WT), but the activity of the protochlorophyllide oxidoreductase (POR) in WT was much higher than that of NYB. Most of the photosystem 2 apoproteins were present in both WT and NYB, suggesting that the capability of protein synthesis was probably fully preserved in the mutant. Thus chlorophyll (Chl) biosynthesis in NYB was hampered at conversion form protochlorophyllide (Pchlide) into chlorophyllide. The open reading frame of porB gene in NYB was inserted with a 95 bp fragment, which included a stop codon. The NYB mutant is a very useful material for studies of Chl biosynthesis, chloroplast signalling, and structure of light-harvesting POR-Pchlide complex (LHPP). and Z.-L. Liu ... [et al.].
This article focuses on narrative sources for the town histories which are part of the Manuscript collection of the National Museum in Prague. It refers to Early Modern Times historiographic works coming from the following towns: České Budějovice, Horní Blatná, Cheb, Jáchymov, Klatovy, Plzeň, Prachatice, Sedlčany, Vysoké Mýto, and Trutnov.
This article focuses on narrative sources for the town histories which are part of the Manuscript collection of the National Museum in Prague. It refers to Early Modern Times historiographic works coming from the following towns: České Budějovice, Horní Blatná, Cheb, Jáchymov, Klatovy, Plzeň, Prachatice, Sedlčany, Vysoké Mýto, and Trutnov.
This article focuses on narrative sources for the town histories which are part of the Manuscript collection of the National Museum in Prague. It refers to Early Modern Times historiographic works coming from the following towns: České Budějovice, Horní Blatná, Cheb, Jáchymov, Klatovy, Plzeň, Prachatice, Sedlčany, Vysoké Mýto, and Trutnov.
The last step for biosynthesis of c type cytochromes, indispensable for photosynthesis in cyanobacteria and plants, involves heme transport across the membrane and its covalent attachment to the apoprotein. In cyanobacteria, heme attachment occurs in the thylakoid lumen and probably also in the periplasm and requires at least four proteins, believed to be organized in intrinsic membrane protein complex. To allow isolation and identification of such complex, CcsB protein was tagged with 6xHis tag on its N terminus and expressed under the strong psbAII promoter in the cyanobacterium Synechocystis sp. PCC 6803. Similarly, CcsA protein was tagged with FLAG tag under the control of the same promoter. Although expression of both proteins under strong cyanobacterial promoter did not increase steady state contents of the CcsB protein, the fusion tags did not influence properties of the CcsB and CcsA proteins and the resulting mutants had the same phenotype as the wild type. Protein fraction containing CcsBHis protein was partially isolated from the solubilised membranes under native conditions.