Journal
PHOTOSYNTHETICA
Volume 46, Issue 1, Pages 73-78Publisher
ACAD SCIENCES CZECH REPUBLIC, INST EXPERIMENTAL BOTANY
DOI: 10.1007/s11099-008-0013-0
Keywords
chlorophyll; fluorescence emission spectra; light-harvesting complex 2; Nanchong yellow barley (NYB); nucleotide sequences; photosystem 2; proteins; protochlorophyllide oxidoreductase (POR)
Categories
Ask authors/readers for more resources
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).
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available