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1.
mSystems ; 4(5)2019 Oct 29.
Article in English | MEDLINE | ID: mdl-31662429

ABSTRACT

Bronchopulmonary dysplasia (BPD) is a common chronic lung condition in preterm infants that results in abnormal lung development and leads to considerable morbidity and mortality, making BPD one of the most common complications of preterm birth. We employed RNA sequencing and 16S rRNA gene sequencing to profile gene expression in blood and the composition of the fecal microbiota in infants born at <29 weeks gestational age and diagnosed with BPD in comparison to those of preterm infants that were not diagnosed with BPD. 16S rRNA gene sequencing, performed longitudinally on 255 fecal samples collected from 50 infants in the first months of life, identified significant differences in the relative levels of abundance of Klebsiella, Salmonella, Escherichia/Shigella, and Bifidobacterium in the BPD infants in a manner that was birth mode dependent. Transcriptome sequencing (RNA-Seq) analysis revealed that more than 400 genes were upregulated in infants with BPD. Genes upregulated in BPD infants were significantly enriched for functions related to red blood cell development and oxygen transport, while several immune-related pathways were downregulated. We also identified a gene expression signature consistent with an enrichment of immunosuppressive CD71+ early erythroid cells in infants with BPD. Intriguingly, genes that were correlated in their expression with the relative abundances of specific taxa in the microbiota were significantly enriched for roles in the immune system, suggesting that changes in the microbiota might influence immune gene expression systemically.IMPORTANCE Bronchopulmonary dysplasia (BPD) is a serious inflammatory condition of the lung and is the most common complication associated with preterm birth. A large body of evidence now suggests that the gut microbiota can influence immunity and inflammation systemically; however, the role of the gut microbiota in BPD has not been evaluated to date. Here, we report that there are significant differences in the gut microbiota of infants born at <29 weeks gestation and subsequently diagnosed with BPD, which are particularly pronounced when infants are stratified by birth mode. We also show that erythroid and immune gene expression levels are significantly altered in BPD infants. Interestingly, we identified an association between the composition of the microbiota and immune gene expression in blood in early life. Together, these findings suggest that the composition of the microbiota may influence the risk of developing BPD and, more generally, may shape systemic immune gene expression.

2.
Planta ; 249(1): 59-70, 2019 Jan.
Article in English | MEDLINE | ID: mdl-30136197

ABSTRACT

MAIN CONCLUSION: Five Vitis vinifera sesquiterpene synthases were characterized, two was previously uncharacterized, one being a caryophyllene/cubebene synthase and the other a cadinene synthase. Residue differences with other Vitis sesquiterpene synthases are described. The biochemical composition of grape berries at harvest can have a profound effect on the varietal character of the wine produced. Sesquiterpenes are an important class of volatile compounds produced in grapes that contribute to the flavor and aroma of wine, making the elucidation of their biosynthetic origin an important field of research. Five cDNAs corresponding to sesquiterpene synthase genes (TPSs) were isolated from Shiraz berries and expressed in planta in Nicotiana benthamiana followed by chemical characterization by GC-MS. Three of the TPS cDNAs were isolated from immature berries and two were isolated from ripe Shiraz berries. Two of the investigated enzymes, TPS26 and TPS27, have been previously investigated by expression in E. coli, and the in planta products generally correspond to these previous studies. The enzyme TPS07 differed by eight amino acids (none of which are in the active site) from germacrene B and D synthase isolated from Gewürztraminer grapes and characterized in vitro. Here in planta characterization of VvShirazTPS07 yielded ylangene, germacrene D and several minor products. Two of the enzymes isolated from immature berries were previously uncharacterized enzymes. VvShirazTPS-Y1 produced cadinene as a major product and at least 17 minor sesquiterpenoid skeletons. The second, VvShirazTPS-Y2, was characterized as a caryophyllene/cubebene synthase, a combination of products not previously reported from a single enzyme. Using in silico methods, we identified residues that could play key roles regarding differences in product formation of these enzymes. The first ring closure that is either a 1,10- or 1,11-ring closure is likely controlled by three neighboring amino acids in helices G1, H2, and J. As for many other investigated TPS enzymes, we also observe that only a few residues can account for radical changes in product formation.


Subject(s)
Fruit/enzymology , Fruit/metabolism , Sesquiterpenes/metabolism , Vitis/enzymology , Vitis/metabolism , Alkyl and Aryl Transferases/metabolism , Plant Proteins/metabolism
3.
BMC Genomics ; 14: 882, 2013 Dec 16.
Article in English | MEDLINE | ID: mdl-24341535

ABSTRACT

BACKGROUND: Gene expression datasets in model plants such as Arabidopsis have contributed to our understanding of gene function and how a single underlying biological process can be governed by a diverse network of genes. The accumulation of publicly available microarray data encompassing a wide range of biological and environmental conditions has enabled the development of additional capabilities including gene co-expression analysis (GCA). GCA is based on the understanding that genes encoding proteins involved in similar and/or related biological processes may exhibit comparable expression patterns over a range of experimental conditions, developmental stages and tissues. We present an open access database for the investigation of gene co-expression networks within the cultivated grapevine, Vitis vinifera. DESCRIPTION: The new gene co-expression database, VTCdb (http://vtcdb.adelaide.edu.au/Home.aspx), offers an online platform for transcriptional regulatory inference in the cultivated grapevine. Using condition-independent and condition-dependent approaches, grapevine co-expression networks were constructed using the latest publicly available microarray datasets from diverse experimental series, utilising the Affymetrix Vitis vinifera GeneChip (16 K) and the NimbleGen Grape Whole-genome microarray chip (29 K), thus making it possible to profile approximately 29,000 genes (95% of the predicted grapevine transcriptome). Applications available with the online platform include the use of gene names, probesets, modules or biological processes to query the co-expression networks, with the option to choose between Affymetrix or Nimblegen datasets and between multiple co-expression measures. Alternatively, the user can browse existing network modules using interactive network visualisation and analysis via CytoscapeWeb. To demonstrate the utility of the database, we present examples from three fundamental biological processes (berry development, photosynthesis and flavonoid biosynthesis) whereby the recovered sub-networks reconfirm established plant gene functions and also identify novel associations. CONCLUSIONS: Together, we present valuable insights into grapevine transcriptional regulation by developing network models applicable to researchers in their prioritisation of gene candidates, for on-going study of biological processes related to grapevine development, metabolism and stress responses.


Subject(s)
Databases, Genetic , Gene Expression Regulation, Plant , Vitis/genetics , Computational Biology/methods , Gene Regulatory Networks , Genomics/methods , Internet , Molecular Sequence Annotation , User-Computer Interface
4.
BMC Genomics ; 13: 691, 2012 Dec 11.
Article in English | MEDLINE | ID: mdl-23227855

ABSTRACT

BACKGROUND: Vitis vinifera berry development is characterised by an initial phase where the fruit is small, hard and acidic, followed by a lag phase known as veraison. In the final phase, berries become larger, softer and sweeter and accumulate an array of organoleptic compounds. Since the physiological and biochemical makeup of grape berries at harvest has a profound impact on the characteristics of wine, there is great interest in characterising the molecular and biophysical changes that occur from flowering through veraison and ripening, including the coordination and temporal regulation of metabolic gene pathways. Advances in deep-sequencing technologies, combined with the availability of increasingly accurate V. vinifera genomic and transcriptomic data, have enabled us to carry out RNA-transcript expression analysis on a global scale at key points during berry development. RESULTS: A total of 162 million 100-base pair reads were generated from pooled Vitis vinifera (cv. Shiraz) berries sampled at 3-weeks post-anthesis, 10- and 11-weeks post-anthesis (corresponding to early and late veraison) and at 17-weeks post-anthesis (harvest). Mapping reads from each developmental stage (36-45 million) onto the NCBI RefSeq transcriptome of 23,720 V. vinifera mRNAs revealed that at least 75% of these transcripts were detected in each sample. RNA-Seq analysis uncovered 4,185 transcripts that were significantly upregulated at a single developmental stage, including 161 transcription factors. Clustering transcripts according to distinct patterns of transcription revealed coordination in metabolic pathways such as organic acid, stilbene and terpenoid metabolism. From the phenylpropanoid/stilbene biosynthetic pathway at least 46 transcripts were upregulated in ripe berries when compared to veraison and immature berries, and 12 terpene synthases were predominantly detected only in a single sample. Quantitative real-time PCR was used to validate the expression pattern of 12 differentially expressed genes from primary and secondary metabolic pathways. CONCLUSIONS: In this study we report the global transcriptional profile of Shiraz grapes at key stages of development. We have undertaken a comprehensive analysis of gene families contributing to commercially important berry characteristics and present examples of co-regulation and differential gene expression. The data reported here will provide an invaluable resource for the on-going molecular investigation of wine grapes.


Subject(s)
Gene Expression Regulation, Developmental/genetics , Gene Expression Regulation, Plant/genetics , Transcriptome/genetics , Vitis/growth & development , Vitis/genetics , Base Sequence , Cluster Analysis , DNA Shuffling/methods , Gene Expression Profiling , Gene Expression Regulation, Developmental/physiology , Gene Expression Regulation, Plant/physiology , High-Throughput Nucleotide Sequencing , Microarray Analysis , Molecular Sequence Data , Real-Time Polymerase Chain Reaction , Vitis/metabolism
5.
Biochem J ; 448(2): 261-71, 2012 Dec 01.
Article in English | MEDLINE | ID: mdl-22938155

ABSTRACT

Thapsigargin is a major terpenoid constituent of Thapsia garganica root. Owing to its potent antagonistic effect on the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase, thapsigargin has been widely used to study Ca2+ signalling and is also a potential drug for prostate cancer. Despite its importance, thapsigargin biosynthesis in T. garganica remains unknown. In order to decipher thapsigargin biosynthesis, deep transcript sequencing (454 and Illumina) of the T. garganica root was performed, and two terpene synthases (TgTPS1/2) were identified. Functional characterization of their encoded enzymes in a metabolically engineered yeast revealed that TgTPS1 synthesized δ-cadinene, whereas TgTPS2 produced ten distinct terpenoids. However, cultivation of the TgTPS2-expressing yeast in pH-maintained conditions (pH 6-7) yielded one major oxygenated sesquiterpenoid, suggesting that formation of multiple terpenoids was caused by acidity. The major terpene product from TgTPS2 was identified as 6ß-hydroxygermacra-1(10),4-diene (kunzeaol) by mass-fragmentation pattern, retention index, the nature of its acid-induced degradation and NMR. Also, recombinant TgTPS2 efficiently catalysed the synthesis of kunzeaol in vitro from farnesyl diphosphate with a Km of 2.6 µM and a kcat of 0.03 s-1. The present paper is the first report of a kunzeaol synthase, and a mechanism for the transformation of kunzeaol into the thapsigargin backbone is proposed.


Subject(s)
Alkyl and Aryl Transferases/metabolism , Plant Proteins/metabolism , Sesquiterpenes/metabolism , Thapsia/enzymology , Thapsigargin/metabolism , Alkyl and Aryl Transferases/chemistry , Alkyl and Aryl Transferases/genetics , DNA, Plant/genetics , Gas Chromatography-Mass Spectrometry , Gene Expression , Genes, Plant , Kinetics , Models, Biological , Plant Proteins/chemistry , Plant Proteins/genetics , Plant Roots/metabolism , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Sesquiterpenes/chemistry , Thapsia/genetics , Thapsia/metabolism , Thapsigargin/chemistry
6.
Plant Physiol ; 160(1): 450-63, 2012 Sep.
Article in English | MEDLINE | ID: mdl-22791304

ABSTRACT

Glycosylation is the most abundant and complex posttranslational modification to be considered for recombinant production of therapeutic proteins. Mucin-type (N-acetylgalactosamine [GalNAc]-type) O-glycosylation is found in eumetazoan cells but absent in plants and yeast, making these cell types an obvious choice for de novo engineering of this O-glycosylation pathway. We previously showed that transient implementation of O-glycosylation capacity in plants requires introduction of the synthesis of the donor substrate UDP-GalNAc and one or more polypeptide GalNAc-transferases for incorporating GalNAc residues into proteins. Here, we have stably engineered O-glycosylation capacity in two plant cell systems, soil-grown Arabidopsis (Arabidopsis thaliana) and tobacco (Nicotiana tabacum) Bright Yellow-2 suspension culture cells. Efficient GalNAc O-glycosylation of two stably coexpressed substrate O-glycoproteins was obtained, but a high degree of proline hydroxylation and hydroxyproline-linked arabinosides, on a mucin (MUC1)-derived substrate, was also observed. Addition of the prolyl 4-hydroxylase inhibitor 2,2-dipyridyl, however, effectively suppressed proline hydroxylation and arabinosylation of MUC1 in Bright Yellow-2 cells. In summary, stably engineered mammalian type O-glycosylation was established in transgenic plants, demonstrating that plants may serve as host cells for the production of recombinant O-glycoproteins. However, the present stable implementation further strengthens the notion that elimination of endogenous posttranslational modifications may be needed for the production of protein therapeutics.


Subject(s)
Acetylgalactosamine/metabolism , Arabidopsis/metabolism , Genetic Engineering/methods , Mucin-1/metabolism , Nicotiana/metabolism , Arabidopsis/cytology , Arabidopsis/genetics , Bacterial Proteins/metabolism , Cell Culture Techniques/methods , Culture Media/metabolism , Glycosylation , Humans , Hydroxylation , Luminescent Proteins/metabolism , Plant Cells/metabolism , Plant Proteins/genetics , Plant Proteins/metabolism , Plants, Genetically Modified/genetics , Plants, Genetically Modified/metabolism , Proline/metabolism , Protein Stability , Proteolysis , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Nicotiana/cytology , Nicotiana/genetics
7.
J Biol Chem ; 287(15): 11911-23, 2012 Apr 06.
Article in English | MEDLINE | ID: mdl-22334671

ABSTRACT

Mucin-type O-glycosylation is an important post-translational modification that confers a variety of biological properties and functions to proteins. This post-translational modification has a particularly complex and differentially regulated biosynthesis rendering prediction and control of where O-glycans are attached to proteins, and which structures are formed, difficult. Because plants are devoid of GalNAc-type O-glycosylation, we have assessed requirements for establishing human GalNAc O-glycosylation de novo in plants with the aim of developing cell systems with custom-designed O-glycosylation capacity. Transient expression of a Pseudomonas aeruginosa Glc(NAc) C4-epimerase and a human polypeptide GalNAc-transferase in leaves of Nicotiana benthamiana resulted in GalNAc O-glycosylation of co-expressed human O-glycoprotein substrates. A chimeric YFP construct containing a 3.5 tandem repeat sequence of MUC1 was glycosylated with up to three and five GalNAc residues when co-expressed with GalNAc-T2 and a combination of GalNAc-T2 and GalNAc-T4, respectively, as determined by mass spectrometry. O-Glycosylation was furthermore demonstrated on a tandem repeat of MUC16 and interferon α2b. In plants, prolines in certain classes of proteins are hydroxylated and further substituted with plant-specific O-glycosylation; unsubstituted hydroxyprolines were identified in our MUC1 construct. In summary, this study demonstrates that mammalian type O-glycosylation can be established in plants and that plants may serve as a host cell for production of recombinant O-glycoproteins with custom-designed O-glycosylation. The observed hydroxyproline modifications, however, call for additional future engineering efforts.


Subject(s)
Genetic Engineering , Nicotiana/genetics , Protein Processing, Post-Translational , Acetylgalactosamine/metabolism , Amino Acid Sequence , Bacterial Proteins/biosynthesis , Bacterial Proteins/genetics , CA-125 Antigen/biosynthesis , CA-125 Antigen/genetics , Carbohydrate Epimerases/biosynthesis , Carbohydrate Epimerases/genetics , Cloning, Molecular , Galactosyltransferases , Genes, Reporter , Glycoproteins/biosynthesis , Glycoproteins/genetics , Glycosylation , Humans , Interferons/biosynthesis , Interferons/genetics , Luminescent Proteins/biosynthesis , Luminescent Proteins/genetics , Membrane Proteins/biosynthesis , Membrane Proteins/genetics , Molecular Sequence Data , Mucins/biosynthesis , N-Acetylgalactosaminyltransferases/biosynthesis , N-Acetylgalactosaminyltransferases/genetics , Peptide Fragments/chemistry , Plant Proteins/genetics , Plants, Genetically Modified , Procollagen-Proline Dioxygenase/genetics , Pseudomonas aeruginosa/enzymology , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics , Nicotiana/enzymology , Nicotiana/metabolism , Polypeptide N-acetylgalactosaminyltransferase
8.
Biochim Biophys Acta ; 1808(6): 1483-92, 2011 Jun.
Article in English | MEDLINE | ID: mdl-21081109

ABSTRACT

PpENA1 is a membrane-spanning transporter from the moss Physcomitrella patens, and is the first type IID P-type ATPase to be reported in the plant kingdom. In Physcomitrella, PpENA1 is essential for normal growth under moderate salt stress, while in yeast, type IID ATPases provide a vital efflux mechanism for cells under high salt conditions by selectively transporting Na+ or K+ across the plasma membrane. To investigate the structural basis for cation-binding within the type IID ATPase subfamily, we used homology modeling to identify a highly conserved cation-binding pocket between membrane helix (MH) 4 and MH 6 of the membrane-spanning pore of PpENA1. Mutation of specific charged and polar residues on MHs 4-6 resulted in a decrease or loss of protein activity as measured by complementation assays in yeast. The E298S mutation on MH 4 of PpENA1 had the most significant effect on activity despite the presence of a serine at this position in fungal type IID ATPases. Activity was partially restored in an inactivated PpENA1 mutant by the insertion of two additional serine residues on MH 4 and one on MH 6 based on the presence of these residues in fungal type IID ATPases. Our results suggest that the residues responsible for cation-binding in PpENA1 are distinct from those in fungal type IID ATPases, and that a fungal-type cation binding site can be successfully engineered into the moss protein.


Subject(s)
Bryopsida/enzymology , Cations/metabolism , Plant Proteins/metabolism , Sodium-Potassium-Exchanging ATPase/metabolism , Amino Acid Sequence , Amino Acid Substitution , Binding Sites/genetics , Fungal Proteins/chemistry , Fungal Proteins/genetics , Fungal Proteins/metabolism , Fungi/enzymology , Genetic Complementation Test , Immunoblotting , Ion Transport , Models, Molecular , Molecular Sequence Data , Mutation , Plant Proteins/chemistry , Plant Proteins/genetics , Potassium/metabolism , Protein Binding , Protein Structure, Secondary , Protein Structure, Tertiary , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/growth & development , Sequence Homology, Amino Acid , Sodium/metabolism , Sodium-Potassium-Exchanging ATPase/chemistry , Sodium-Potassium-Exchanging ATPase/genetics
9.
Plant Physiol ; 144(4): 1786-96, 2007 Aug.
Article in English | MEDLINE | ID: mdl-17556514

ABSTRACT

The bryophyte Physcomitrella patens is unlike any other plant identified to date in that it possesses a gene that encodes an ENA-type Na(+)-ATPase. To complement previous work in yeast (Saccharomyces cerevisiae), we determined the importance of having a Na(+)-ATPase in planta by conducting physiological analyses of PpENA1 in Physcomitrella. Expression studies showed that PpENA1 is up-regulated by NaCl and, to a lesser degree, by osmotic stress. Maximal induction is obtained after 8 h at 60 mm NaCl or above. No other abiotic stress tested led to significant increases in PpENA1 expression. In the gametophyte, strong expression was confined to the rhizoids, stem, and the basal part of the leaf. In the protonemata, expression was ubiquitous with a few filaments showing stronger expression. At 100 mm NaCl, wild-type plants were able to maintain a higher K(+)-to-Na(+) ratio than the PpENA1 (ena1) knockout gene, but at higher NaCl concentrations no difference was observed. Although no difference in chlorophyll content was observed between ena1 and wild type at 100 mm NaCl, the impaired Na(+) exclusion in ena1 plants led to an approximately 40% decrease in growth.


Subject(s)
Adenosine Triphosphatases/metabolism , Bryopsida/growth & development , Cation Transport Proteins/metabolism , Sodium Chloride/metabolism , Adaptation, Physiological , Adenosine Triphosphatases/genetics , Base Sequence , Bryopsida/metabolism , Bryopsida/physiology , Cation Transport Proteins/genetics , Gene Expression , Homeostasis/physiology , Molecular Sequence Data , Potassium/metabolism , Recombination, Genetic , Sodium/metabolism
10.
Planta ; 225(4): 945-54, 2007 Mar.
Article in English | MEDLINE | ID: mdl-16983536

ABSTRACT

Monodehydroascorbate reductase (MDHAR; EC 1.6.5.4) catalyses the reduction of the monodehydroascorbate (MDHA) radical to ascorbate, using NADH or NADPH as an electron donor, and is believed to be involved in maintaining the reactive oxygen scavenging capability of plant cells. This key enzyme in the ascorbate-glutathione cycle has been studied here in the moss Physcomitrella patens, which is tolerant to a range of abiotic stresses and is increasingly used as a model plant. In the present study, three cDNAs encoding different MDHAR isoforms of 47 kDa were identified in P. patens, and found to exhibit enzymic characteristics similar to MDHARs in vascular plants despite low-sequence identity and a distant evolutionary relationship between the species. The three cDNAs for the P. patens MDHAR enzymes were expressed in Escherichia coli and the active enzymes were purified and characterized. Each recombinant protein displayed an absorbance spectrum typical of flavoenzymes and contained a single non-covalently bound FAD coenzyme molecule. The Km and kcat values for the heterologously expressed PpMDHAR enzymes ranged from 8 to 18 microM and 120-130 s(-1), respectively, using NADH as the electron donor. The Km values were at least an order of magnitude higher for NADPH. The Km values for the MDHA radical were approximately 0.5-1.0 microM for each of the purified enzymes, and further kinetic analyses indicated that PpMDHARs follow a 'ping-pong' kinetic mechanism. In contrast to previously published data, site-directed mutagenesis indicated that the conserved cysteine residue is not directly involved in the reduction of MDHA.


Subject(s)
Ascorbic Acid/biosynthesis , Bryopsida/enzymology , NADH, NADPH Oxidoreductases/metabolism , Reactive Oxygen Species/metabolism , Amino Acid Sequence , Bryopsida/genetics , Bryopsida/metabolism , Catalysis , Cysteine/metabolism , DNA, Complementary/metabolism , Escherichia coli/genetics , Escherichia coli/metabolism , Flavin-Adenine Dinucleotide/metabolism , Gene Expression , Kinetics , Molecular Sequence Data , NADH, NADPH Oxidoreductases/genetics , Transformation, Bacterial
11.
Plant Mol Biol ; 60(2): 259-75, 2006 Jan.
Article in English | MEDLINE | ID: mdl-16429263

ABSTRACT

The ascorbate-glutathione pathway plays a major role in the detoxification of reactive oxygen species (ROS) in vascular plants. One of the key enzymes in this pathway is monodehydroascorbate reductase (MDHAR), a FAD enzyme that catalyses the reduction of the monodehydroascorbate radical. To elucidate the evolution and functional role of MDHAR we identified and characterised MDHARs from the moss Physcomitrella patens. Expressed sequence tag (EST) databases containing approximately 100.000 ESTs from Physcomitrella were searched and three isoforms of monodehydroascorbate reductase (PpMDHAR1, PpMDHAR2 and PpMDHAR3) were identified. In vascular plants MDHAR is found in the cytosol, chloroplast, mitochondria and peroxisome. Surprisingly, all three PpMDHARs resembled the cytosolic isoforms from vascular plants lacking the NH(2)-terminal or COOH-terminal extension found in organelle targeted MDHARs. The number and position of introns was also conserved between PpMDHARs and cytosolic MDHARs from vascular plants. Phylogenetic analysis revealed that cytosolic MDHARs are monophyletic in origin and the ancestral gene evolved before the divergence of bryophytes more than 400 million years ago. Transcript analyses showed that expression of PpMdhar1 and PpMdhar3 was increased up to 5-fold under salt stress, osmotic stress or upon exposure to abscisic acid. In contrast, PpMdhar transcription levels were unchanged upon chilling, UV-B exposure or oxidative stress. The conservation of cytosolic MDHAR in the land-plant lineage and the transcriptional upregulation under water deficiency suggest that the evolution of cytosolic MDHAR played an essential role in stress protection for land plants when they inhabited the dry terrestrial environment.


Subject(s)
Bryopsida/genetics , Evolution, Molecular , Gene Expression Regulation, Enzymologic , Gene Expression Regulation, Plant , NADH, NADPH Oxidoreductases/genetics , Amino Acid Sequence , Base Sequence , Bryopsida/enzymology , DNA, Plant , Molecular Sequence Data , NADH, NADPH Oxidoreductases/chemistry , Phylogeny , Promoter Regions, Genetic , Sequence Homology, Amino Acid , Sequence Homology, Nucleic Acid
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