4.3 Article

Mutation mechanism of chlorophyll-less barley mutant NYB

Journal

PHOTOSYNTHETICA
Volume 46, Issue 1, Pages 73-78

Publisher

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)

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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).

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