Lack of Light Regulation of NADPH: Protochlorophyllide Oxido-Reductase mRNA in Cress Seedlings (Lepidium sativum L.)

Kittsteiner, Ursula; Paulsen, Harald; Schendel, Rudolf; Rüdiger, Wolfhart

doi:10.1515/znc-1990-9-1024

Cited by 19 publications

(9 citation statements)

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“…This result contrasts with the observations made in some dicot and gymnosperm species where little or no effect of light is observed on lpcr message levels [8,23,46,78,79] or where the effects of light are conditioned by the developmental growth stage [35,79]. In barley, the light-induced decline in steady-state pchlide reductase message levels has been shown to be the result of a phytochrome-mediated reduction of transcription rates from the lpcr gene(s) [59].…”

Section: Regulation Ofcrlpcr-i Expression In Wild-type and Mutant Cellsmentioning

confidence: 78%

The pc-1 phenotype of Chlamydomonas reinhardtii results from a deletion mutation in the nuclear gene for NADPH:protochlorophyllide oxidoreductase

Timko

1996

Plant Mol Biol

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The pc-1 mutant of Chlamydomonas reinhardtii has been shown to be incapable of protochlorophyllide photoconversion in vivo and is thought to be defective in light-dependent NADPH:protochlorophyllide oxidoreductase activity. We have isolated and characterized the nuclear genes encoding this enzyme from wild-type and pc-1 mutant Chlamydomonas cells. The wild-type CRlpcr-1 gene encodes a 397 amino acid polypeptide of which the N-terminal 57 residues comprise the chloroplast transit sequence. The Chlamydomonas protochlorophyllide reductase has 66-70% identity (79-82% similarity) to the higher plant enzymes. Transcripts encoding protochlorophyllide reductase are abundant in dark-grown wild-type cells, but absent or at very low levels in cells grown in the light. Similarly, immunoreactive protochlorophyllide reductase protein is also present to a greater extent in dark- versus light-grown wild-type cells. Both pc-1 and pc-1 y-7 cells lack CRlpcr-1 mRNA and the major (36 kDa) immunodetectable form of protochlorophyllide reductase consistent with their inability to photoreduce protochlorophyllide. DNA sequence analysis revealed that the lpcr gene in pc-1 y-7 cells contains a two-nucleotide deletion within the fourth and fifth codons of the protochlorophyllide reductase precursor that causes a shift in the reading frame and results in premature termination of translation. The absence of protochlorophyllide reductase message in pc-1 and pc-1 y-7 cells is likely the consequence of this frameshift mutation in the lpcr gene. Introduction of the CRlpcr-1 gene into pc-1 y-7 cells by nuclear transformation was sufficient to restore the wild-type phenotype. Transformants contained both protochlorophyllide reductase mRNA and immunodetectable enzyme protein. These studies demonstrate that pc-1 was in fact a defect in protochlorophyllide reductase activity and provide the first in vivo molecular evidence that the lpcr gene product is essential for light-dependent protochlorophyllide reduction.

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Section: Regulation Ofcrlpcr-i Expression In Wild-type and Mutant Cellsmentioning

confidence: 78%

The pc-1 phenotype of Chlamydomonas reinhardtii results from a deletion mutation in the nuclear gene for NADPH:protochlorophyllide oxidoreductase

Timko

1996

Plant Mol Biol

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“…7A). White mutant leaves contained about 50% less of the (Schulz et al 1989) subcloned in bluescript vector (Kittsteiner et al 1990) served as the probe. B Same blot as A but hybridized with the 3-kb HindIII-fragrnent of SAc3, representing a genomic clone of the actin gene of soybean (Shah et al 1982).…”

Section: Resultsmentioning

confidence: 99%

Components of chlorophyll biosynthesis in a barley albina mutant unable to synthesize ?-aminolevulinic acid by utilizing the transfer RNA for glutamic acid

Hess

Schendel

Rüdiger

et al. 1992

Planta

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Components of chlorophyll biosynthesis were investigated in the plastid-ribosome-deficient albostrians mutant of barley (Hordeum vulgare L.). Compared with green leaves, white leaves lacked chloroplast tRNA(Glu) and 16S ribosomal RNA, but contained a much higher level of the mRNA for glutamate 1-semialdehyde aminotransferase. Substantial amounts of protochlorophyllide were accumulated when the mutant was incubated in a solution of δ-aminolevulinic acid. The level of protochlorophyllide oxidoreductase mRNA (PCOR, EC 1.6.99.1.) in etiolated albostrians plants reached only about 50% of the level in wild-type plants. In addition the content of PCOR protein and the activity of chlorophyll synthetase were distinctly lower than in the wild-type. Mutant and wild-type barley seedlings which were grown under a daily light/dark regime and were therefore nonetiolated both possessed PCOR mRNA. The data presented may help explain the albino phenotype of this mutant. The results are discussed in relation to biosynthesis of tetrapyrrols in higher plants, regulation of chlorophyll biosynthesis and the action of a plastidderived signal involved in the expression of certain nuclear genes.

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“…The presence of the differentially regulated PorA and PorB genes in both A. thaliana and barley could also offer an explanation for observations that the influence of light on Por mRNA levels ranges from a drastic negative regulation to virtually no effect depending on the plant species (Apel, 1981;Meyer et al, 1983;Batschauer and Apel, 1984;Hauser et al, 1987;Kay et al, 1989;Darrah et al, 1990;Forreiter et al, 1990;Kittsteiner et al, 1990;Benli et al, 1991;Spano et al, 1992a;He et al, 1994). A. thaliana expresses PorA and T o r B at almost equal levels in etiolated seedlings (Figs.…”

Section: Genes In Angiospermsmentioning

confidence: 97%

“…Dicotyledonous species, however, display little negative light regulation at the level of mRNA (Forreiter et al, 1990;Kittsteiner et al, 1990;Benli et al, 1991;Spano et al, 1992a;He et al, 1994). The light-induced disappearance of barley Por mRNA results both from a phytochrome-mediated reduction in transcription initiation (Apel, 1981;Mosinger et al, 1985) and from posttranscriptional effects (Mosinger et al, 1988).…”

mentioning

confidence: 99%

Identification of NADPH:Protochlorophyllide Oxidoreductases A and B: A Branched Pathway for Light-Dependent Chlorophyll Biosynthesis in Arabidopsis thaliana

et al. 1995

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Lack of Light Regulation of NADPH: Protochlorophyllide Oxido-Reductase mRNA in Cress Seedlings (Lepidium sativum L.)

Cited by 19 publications

References 0 publications

The pc-1 phenotype of Chlamydomonas reinhardtii results from a deletion mutation in the nuclear gene for NADPH:protochlorophyllide oxidoreductase

The pc-1 phenotype of Chlamydomonas reinhardtii results from a deletion mutation in the nuclear gene for NADPH:protochlorophyllide oxidoreductase

Components of chlorophyll biosynthesis in a barley albina mutant unable to synthesize ?-aminolevulinic acid by utilizing the transfer RNA for glutamic acid

Identification of NADPH:Protochlorophyllide Oxidoreductases A and B: A Branched Pathway for Light-Dependent Chlorophyll Biosynthesis in Arabidopsis thaliana

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