Biosynthesis of C9-aldehydes in the moss Physcomitrella patens☆

Stumpe, Michael; Bode, Julia; Göbel, Cornelia; Wichard, Thomas; Schaaf, Andreas; Frank, Wolfgang; Frank, Markus H.; Reski, Ralf; Pohnert, Georg; Feußner, Ivo

doi:10.1016/j.bbalip.2006.03.008

Cited by 60 publications

(62 citation statements)

References 57 publications

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“…Whereas the PpPAPR-GFP signal was uniformly distributed within the plastids, PpAPR-GFP fluorescence displayed a spotty pattern (Fig. 3) similar to that described previously for Physcomitrella hydroperoxide lyase (30).…”

Section: Subcellular Localization Of Ppapr Andmentioning

confidence: 53%

The Putative Moss 3′-Phosphoadenosine-5′-phosphosulfate Reductase Is a Novel Form of Adenosine-5′-phosphosulfate Reductase without an Iron-Sulfur Cluster

Fritzemeier

Wiedemann

Reski

2007

Journal of Biological Chemistry

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Sulfate assimilation provides reduced sulfur for synthesis of the amino acids cysteine and methionine and for a range of other metabolites. Sulfate has to be activated prior to reduction by adenylation to adenosine 5-phosphosulfate (APS). In plants, algae, and many bacteria, this compound is reduced to sulfite by APS reductase (APR); in fungi and some cyanobacteria and ␥-proteobacteria, a second activation step, phosphorylation to 3-phosphoadenosine 5-phosphosulfate (PAPS), is necessary before reduction to sulfite by PAPS reductase (PAPR). We found previously that the moss Physcomitrella patens is unique among these organisms in possessing orthologs of both APR and PAPR genes (Koprivova, A., Meyer, A. J., Schween, G., Herschbach, C., Reski, R., and Kopriva, S. (2002) J. Biol. Chem. 277, 32195-32201). To assess the function of the two enzymes, we compared their biochemical properties by analysis of purified recombinant proteins. APR from Physcomitrella is very similar to the well characterized APRs from seed plants. On the other hand, we found that the putative PAPR preferentially reduces APS. Sequence analysis, analysis of UV-visible spectra, and determination of iron revealed that this new APR, named PpAPR-B, does not contain the FeS cluster, which was previously believed to determine the substrate specificity of the otherwise relatively similar enzymes. The lack of the FeS cluster in PpAPR-B catalysis is connected with a lower turnover rate but higher stability of the protein. These findings show that APS reduction without the FeS cluster is possible and that plant sulfate assimilation is predominantly dependent on reduction of APS.Sulfur is essential for life. It is present in the amino acids cysteine and methionine as part of proteins and peptides; in many coenzymes and prosthetic groups, such as FeS centers, thiamine, lipoic acid, etc.; and in a variety of secondary metabolites, e.g. glucosinolates and alliins in plants. In these compounds, sulfur is present in the reduced form of organic thiols; however, the major form of sulfur available in nature is sulfate.

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Section: Subcellular Localization Of Ppapr Andmentioning

confidence: 53%

The Putative Moss 3′-Phosphoadenosine-5′-phosphosulfate Reductase Is a Novel Form of Adenosine-5′-phosphosulfate Reductase without an Iron-Sulfur Cluster

Fritzemeier

Wiedemann

Reski

2007

Journal of Biological Chemistry

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“…Interestingly, previous knowledge about the release into seawater of oxidized fatty acid-derived compounds from brown algae was limited to sexual pheromones. [29] These findings also raise the questions of which enzymes are involved with the generation of fatty acid aldehydes in brown algae: either hydroperoxide lyase CYP74 enzymes as in plants [1] and/or LOXs as in the moss Physcomitrella patens, [40] or otherwise, an enzyme machinery specific to the phylum of Heterokonta as suggested by recent results obtained with diatoms. [41] The recently provided access to whole genomes of brown algae [42] and diatoms [43,44] should afford new opportunities to express the cDNA of the conserved sequences and to characterize the products of the associated recombinant enzymes as conducted in the green lineage.…”

mentioning

confidence: 68%

“…[41] The recently provided access to whole genomes of brown algae [42] and diatoms [43,44] should afford new opportunities to express the cDNA of the conserved sequences and to characterize the products of the associated recombinant enzymes as conducted in the green lineage. [1,40] Material and treatment conditions: The marine brown alga Laminaria digitata V. Lamouroux (Laminariales, Laminariaceae) was collected in the intertidal zone close to the Station Biologique de Roscoff in Brittany, France, during low tide. Young fronds (2 to 15 cm in length) were chosen and transported to the laboratory.…”

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confidence: 99%

Release of Volatile Aldehydes by the Brown Algal Kelp Laminaria digitata in Response to Both Biotic and Abiotic Stress

et al. 2009

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“…patens has been widely used to address various questions of primary metabolism, such as fatty acid synthesis, N-glycosylation, or sulfur metabolism [10,11,[17][18][19][20]. Many such analyses revealed an unexpected variety of enzymes and pathways alternative to those in flowering plants.…”

Section: Introductionmentioning

confidence: 99%

Targeted knock‐out of a gene encoding sulfite reductase in the moss Physcomitrella patens affects gametophytic and sporophytic development

et al. 2010

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Edited by Michael R. Sussman Keywords:Bryophyte Moss development Protonema development Spore maturation Sulfate assimilation a b s t r a c t A key step in sulfate assimilation into cysteine is the reduction of sulfite to sulfide by sulfite reductase (SiR). This enzyme is encoded by three genes in the moss Physcomitrella patens. To obtain a first insight into the roles of the individual isoforms, we deleted the gene encoding the SiR1 isoform in P. patens by homologous recombination and subsequently analysed the DSiR1 mutants. While DSiR1 mutants showed no obvious alteration in sulfur metabolism, their regeneration from protoplasts and their ability to produce mature spores was significantly affected, highlighting an unexpected link between moss sulfate assimilation and development, that is yet to be characterized.

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Biosynthesis of C9-aldehydes in the moss Physcomitrella patens☆

Cited by 60 publications

References 57 publications

The Putative Moss 3′-Phosphoadenosine-5′-phosphosulfate Reductase Is a Novel Form of Adenosine-5′-phosphosulfate Reductase without an Iron-Sulfur Cluster

The Putative Moss 3′-Phosphoadenosine-5′-phosphosulfate Reductase Is a Novel Form of Adenosine-5′-phosphosulfate Reductase without an Iron-Sulfur Cluster

Release of Volatile Aldehydes by the Brown Algal Kelp Laminaria digitata in Response to Both Biotic and Abiotic Stress

Targeted knock‐out of a gene encoding sulfite reductase in the moss Physcomitrella patens affects gametophytic and sporophytic development

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