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1.
Rev Epidemiol Sante Publique ; 56(1): 54-62, 2008 Feb.
Artigo em Francês | MEDLINE | ID: mdl-18294793

RESUMO

BACKGROUND: The French health and services system to maintain at home is characterized by its fragmentation, whereas the need of the people for intervention is generally total. This fragmentation have consequences: delay in services delivery, inadequate transmission of information, redundant evaluation, service conditioned by the entrance point solicited rather than by the need of the person and inappropriate use of expensive resources by ignorance or difficulty of access to the less expensive resources. PRESENTATION OF THE INNOVATION: The purpose of integration is to improve continuity of interventions for people in loss of autonomy. It consists in setting up a whole of organisational, managerial and clinical common tools. Organisational model "Projet et Recherches sur l'Intégration des Services pour le Maintien de l'Autonomie" (Prisma) tested in Quebec showed a strong impact on the prevention of the loss of autonomy in term of public health on a population level. This model rests on six principal elements: partnership, single entry point, case-management, a multidimensional standardized tool for evaluation, an individualized services plan and a system for information transmission. CONTEXTUAL ANALYSIS: Thus, it was decided to try to implement in France this organisational model. The project is entitled Prisma France and is presented here. The analysis of the context of implementation of the innovation which represents integration in the field of health and services for frail older reveals obstacles (in particular because of diversity of professional concerned and a presentiment of complexity of the implementation of the model) and favourable conditions (in particular the great tension towards change in this field). CONCLUSION: The current conditions in France appear mainly favourable to the implementation of integration. The establishment of Prisma model in France requires a partnership work of definition of a common language as well on the diagnoses as on the solutions. The strategic and operational dialogue is thus a key element of the construction of integration. This stage currently occurs in parallel in three areas contrasted in France. The results of associated qualitative research should make it possible to define the factors fostering or hindering the realization of integration according to each site (analyzes contrasted) and in all the sites (related to the particular context of care and French services as a whole).


Assuntos
Administração de Caso , Pessoas com Deficiência , Acessibilidade aos Serviços de Saúde , França , Necessidades e Demandas de Serviços de Saúde , Humanos , Desenvolvimento de Programas
2.
Plant Physiol ; 105(4): 1223-1229, 1994 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-12232278

RESUMO

To study the regulation of gene expression for enzymes in the C4 photosynthetic pathway of maize (Zea mays L.) in response to changing N status in developing photosynthetic cells, we have studied in vitro transcription of the phosphoenolpyruvate carboxylase (PEPC) gene in leaf nuclei isolated from plants during recovery from N starvation. The induction was specific for the C4-type PEPC gene (C4Ppc1), and its transcription was N dependent and increased markedly by supply of an N source, but there was a discrepancy between the steady-state levels of mRNA and the stimulation of in vitro transcription. The results suggest that the N-inducible expression of C4Ppc1 is regulated both transcriptionally and posttranscriptionally by N availability. The in vitro transcription rate of C4Ppc1 was greatly stimulated by incubating detached leaves with zeatin alone, whereas the rate remained essentially unchanged by incubating with an exogenous N source alone. The results, taken together, imply that cytokinins up-regulate the transcription of C4Ppc1 in response to N status, whereas glutamine and/or its metabolite(s) up-regulate the level of the transcript. The transcription was totally inhibited by cycloheximide, indicating that the cytokinin-dependent transcription of C4Ppc1 requires the synthesis of protein.

3.
Gene ; 89(2): 171-7, 1990 May 14.
Artigo em Inglês | MEDLINE | ID: mdl-2373367

RESUMO

A genomic clone encoding the NADP-malate dehydrogenase precursor has been isolated from a Sorghum vulgare lambda EMBL4 library using a cDNA probe. The entire structure of this nuclear gene (4.6 kb) encoding the 429-amino acid precursor is reported, as well as 602 bp of the 5'-flanking and 695 bp of the 3'-flanking regions. The gene is interrupted by 13 introns from 79 to 495 bp in length. S1 nuclease mapping showed the S. vulgare gene transcript to contain an untranslated leader sequence of 44 nucleotides. In the 5'-flanking region, several short sequences similar to the consensus motifs involved in the light-regulation process of other plant genes were found.


Assuntos
Genes de Plantas , Malato Desidrogenase/genética , Plantas/genética , Sequência de Aminoácidos , Sequência de Bases , Clonagem Molecular , Éxons , Genes de Plantas/efeitos da radiação , Íntrons , Luz , Dados de Sequência Molecular , Mapeamento de Nucleotídeos , Plantas/enzimologia , RNA Mensageiro/genética , Mapeamento por Restrição , Homologia de Sequência do Ácido Nucleico , Transcrição Gênica
4.
Gene ; 99(1): 87-94, 1991 Mar 01.
Artigo em Inglês | MEDLINE | ID: mdl-2022326

RESUMO

Two different members of the phosphoenolpyruvate carboxylase(PEPC)-encoding multigene family (clones lambda CP21 and lambda CP46) have been isolated from a Sorghum vulgare lambda EMBL4 genomic library. The use of the 3'-noncoding regions to probe Northern blots of RNA from roots, etiolated leaves and green leaves indicated that lambda CP21 and lambda CP46 encode the C3- and C4-type leaf PEPC isoforms, respectively. The lambda CP21 clone is expressed in the three tissues and is not light-regulated, whereas lambda CP46 is only expressed in greening leaves. The nucleotide sequence of the 5'-flanking DNA (520 bp) has been determined for both genes. For lambda CP46, several direct repeats were located in this region with similarities to sequences found in other light-regulated genes, but not in lambda CP21. The deduced amino acid sequences of the two S. vulgare PEPC proteins are 75% identical.


Assuntos
Genes de Plantas , Isoenzimas/genética , Família Multigênica , Fosfoenolpiruvato Carboxilase/genética , Plantas/genética , Regiões Promotoras Genéticas , Sequência de Aminoácidos , Sequência de Bases , Clonagem Molecular , Éxons , Expressão Gênica , Biblioteca Genômica , Dados de Sequência Molecular , Plantas/enzimologia , Sequências Repetitivas de Ácido Nucleico , Mapeamento por Restrição , Homologia de Sequência do Ácido Nucleico
5.
New Phytol ; 125(2): 339-343, 1993 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-33874502

RESUMO

As part of a project to identify symbiosis-related genes, we report here a simple differential screening procedure for isolating up- and down-regulated fungal transcripts from a cDNA library of the developing Eucalyptus globulus-Pisolithus tinctorius mycorrhiza. cDNA inserts of randomly selected λZAP plaques were amplified by PCR and separated by agarose gel electrophoresis. The PCR-amplified cDNA samples were then screened by Southern blotting, using radiolabelled-cDNA probes of high specific activity. We have applied this method to fungal transcripts that are differentially expressed in ectomycorrhizas during the early stages of development. We estimate that about 50 % of the fungal mRNA population is regulated by development of the symbiosis; several up- and down-regulated cDNAs have been isolated for further analysis.

8.
Mol Gen Genet ; 228(3): 473-81, 1991 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-1896015

RESUMO

We previously described the isolation and the nucleotide sequence of a nuclear gene from sorghum (NMDHI; 4.6 kb) encoding the NADP-malate dehydrogenase. Further analysis led us to identify a second homologous gene (NMDH II; 4.8 kb) located within the same 12.3 kb genomic clone (lambda LM17); these two genes are tandemly organized, in direct orientation. This second gene was entirely sequenced and comparison with the first gene showed that the positions on the 14 exons and 13 introns are conserved in both genes. The analysis of the genomic organization and copy number in the Sorghum vulgare genome revealed that there are no additional homologues and there is only one copy each of NMDH I and NMDH II. The isolation of two different cDNA clones in a previous work suggested that both genes were probably expressed. Analysis of specific mRNA accumulation during the greening process using synthetic oligonucleotide probes showed that the NMDH I gene is induced in the presence of light while the NMDH II gene seems to be constitutively expressed at low level.


Assuntos
Expressão Gênica , Malato Desidrogenase/genética , Plantas/enzimologia , Sequência de Aminoácidos , Sequência de Bases , Northern Blotting , Malato Desidrogenase (NADP+) , Dados de Sequência Molecular , RNA Mensageiro/genética , Mapeamento por Restrição , Homologia de Sequência do Ácido Nucleico , Transcrição Gênica
9.
Plant Mol Biol ; 21(3): 487-502, 1993 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-8443342

RESUMO

Although housekeeping functions have been shown for the phosphoenolpyruvate carboxylase (EC 4.1.1.31, PEPC) in plants and in prokaryotes, PEPC is mainly known for its specific role in the primary photosynthetic CO2 fixation in C4 and CAM plants. We have shown that in Sorghum, a monocotyledonous C4 plant, the enzyme is encoded in the nucleus by a small multigene family. Here we report the entire nucleotide sequence (7.5 kb) of the third member (CP21) that completes the structure of the Sorghum PEPC gene family. Nucleotide composition, CpG islands and GC content of the three Sorghum PEPC genes are analysed with respect to their possible implications in the regulation of expression. A study of structure/function and phylogenetic relationships based on the compilation of all PEPC sequences known so far is presented. Data demonstrated that: (1) the different forms of plant PEPC have very similar primary structures, functional and regulatory properties, (2) neither apparent amino acid sequences nor phylogenetic relationships are specific for the C4 and CAM PEPCs and (3) expression of the different genes coding for the Sorghum PEPC isoenzymes is differently regulated (i.e. by light, nitrogen source) in a spatial and temporal manner. These results suggest that the main distinguishing feature between plant PEPCs is to be found at the level of genes expression rather than in their primary structure.


Assuntos
Fosfoenolpiruvato Carboxilase/genética , Poaceae/enzimologia , Sequência de Aminoácidos , Sequência de Bases , Evolução Biológica , Regulação Enzimológica da Expressão Gênica , Isoenzimas/genética , Dados de Sequência Molecular , Família Multigênica , Oligodesoxirribonucleotídeos , Filogenia , Poaceae/genética , Homologia de Sequência de Aminoácidos , Relação Estrutura-Atividade
10.
Photosynth Res ; 43(3): 283-8, 1995 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-24306851

RESUMO

A peptide containing the N-terminal phosphorylation site (Ser-8) of Sorghum C4-phospho enolpyruvate carboxylase (PEPC) was synthesized, purified and used to raise an antiserum in rabbits. Affinity-purified IgGs prevented PEPC phosphorylation in a reconstituted in vitro assay and reacted with both the phosphorylated and dephosphorylated forms of either native or denatured PEPC in immunoblotting experiments. Saturation of dephospho-PEPC with these specific IgGs resulted in a marked alteration of its functional and regulatory properties that mimicked phosphorylation of Ser-8. A series of recombinant C4 PEPCs mutated in the N-terminal phosphorylation domain and a C3-like PEPC isozyme from Sorghum behaved similarly to their C4 counterpart with respect to these phosphorylation-site antibodies.

11.
Plant Mol Biol ; 17(1): 83-8, 1991 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-1868224

RESUMO

Phosphoeolpyruvate carboxylase (PEPC)-deficient mutants of Escherichia coli have been complemented with a plasmid bearing a full-length cDNA encoding the C4-type form of Sorghum leaf PEPC. Transformed cells grew on minimal medium. Two clones were selected which produce a functional and full-sized enzyme protein as determined by activity assays, immunochemical behavior and SDS-PAGE. In addition, regulatory phosphorylation of immunopurified recombinant PEPC was observed when the enzyme was incubated with a partially purified plant PEPC kinase. These results establish that E. coli cells produce a genuine, phosphate-free, higher-plant PEPC. Application of immunoadsorbtion chromatography to bacterial extracts makes it possible to prepare highly pure protein available for biochemical studies.


Assuntos
Fosfoenolpiruvato Carboxilase/genética , Poaceae/enzimologia , Clonagem Molecular , Escherichia coli/genética , Fosfoenolpiruvato Carboxilase/isolamento & purificação , Fosfoenolpiruvato Carboxilase/metabolismo , Fosforilação , Plasmídeos , Poaceae/genética , Transformação Genética
12.
Plant Cell Rep ; 9(12): 688-90, 1991 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-24213694

RESUMO

The expression of a Sorghum vulgäre gene encoding the phosphoenol-pyruvate carboxylase involved in C4 photosynthesis has been studied after introduction into tobacco. Northern blot analysis of poly(A) mRNA from green leaves demonstrated i) the efficiency of this monocot promoter, ii) the transcription of the sorghum phosphoenol-pyruvate carboxylase mRNA with the expected size (3.4kb). These results strongly suggested that introns of this monocot gene have been excised efficiently by the dicot cells. Moreover, the presence of the sorghum phosphoenol-pyruvate carboxylase mRNA was not detected in the roots of the transformed plants, suggesting that the 2.4kb 5'-region of the gene could be sufficient to confer the tissue specific expression.

13.
Plant Physiol ; 85(1): 243-6, 1987 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-16665664

RESUMO

The mechanism underlying the light effect on phosphoenolpyruvate carboxylase (PEPC) from the C(4) plant sorghum (Sorghum vulgare Pers., var Tamaran) leaves was investigated. Following exposure to light a new isozyme of PEPC, specific for the green leaf and responsible for primary CO(2) fixation in photosynthesis, was established. Northern blot experiments revealed the presence of PEPC mRNA showing a molecular weight of 3.4 kilobases. During the greening process, concomitant to enzyme activity, PEPC protein and PEPC messenger RNA amounts increased considerably. This photoresponse was shown to be under phytochrome control.

14.
Biochem Biophys Res Commun ; 197(3): 1415-23, 1993 Dec 30.
Artigo em Inglês | MEDLINE | ID: mdl-8280159

RESUMO

In this work, the C3-type form of Sorghum phosphoenolpyruvate carboxylase (PyrPC) was produced in PyrPC-deficient strains of Escherichia coli transformed by a plasmid bearing the corresponding full-length cDNA (CPR1). The full-sized protein was purified to homogeneity by immunoaffinity chromatography. Some functional and regulatory properties were described; notably, the immunopurified PyrPC could be phosphorylated in reconstituted assay by 1) both a mammalian PKA and the PyrPC protein serine kinase purified from Sorghum leaves and 2) a novel protein kinase affinity-purified from Sorghum roots. In all cases phosphorylation was accompanied by a marked reduction in its malate sensitivity.


Assuntos
Isoenzimas/biossíntese , Fosfoenolpiruvato Carboxilase/biossíntese , Poaceae/enzimologia , Proteínas Serina-Treonina Quinases/metabolismo , Proteínas Recombinantes/biossíntese , Sequência de Aminoácidos , Animais , Cromatografia de Afinidade , Clonagem Molecular , Proteínas Quinases Dependentes de AMP Cíclico/metabolismo , Eletroforese em Gel de Poliacrilamida , Escherichia coli , Isoenzimas/isolamento & purificação , Isoenzimas/metabolismo , Cinética , Mamíferos , Dados de Sequência Molecular , Peso Molecular , Fosfoenolpiruvato Carboxilase/isolamento & purificação , Fosfoenolpiruvato Carboxilase/metabolismo , Fosforilação , Proteínas Recombinantes/isolamento & purificação , Proteínas Recombinantes/metabolismo , Especificidade por Substrato
15.
J Biol Chem ; 267(30): 21577-83, 1992 Oct 25.
Artigo em Inglês | MEDLINE | ID: mdl-1400468

RESUMO

The chloroplastic enzyme NADP-malate dehydrogenase is activated by a reversible thiol/disulfide interchange with reduced thioredoxin. Its target disulfide bridge is considered to be located at the amino terminus. To further substantiate the regulatory role of this disulfide, site-directed mutagenesis has been used to replace each or both of the amino-terminal cysteines of the sorghum leaf NADP-malate dehydrogenase, expressed in Escherichia coli, by serines. A truncation mutant lacking the amino terminus has also been produced. Surprisingly, the mutant proteins still required activation by reduced thioredoxin. However, their activation was almost instantaneous, whereas the native enzyme reached full activity after a 10-20 min preincubation. The 8 1/2 for reduced thioredoxin was decreased 2-fold in the mutants, but their Km values for NADPH and oxaloacetate did not change significantly. The inhibition of activation by NADP and inhibition of activity by thiol-derivatizing agents were also retained. These results are interpreted as an indication that two thioredoxin-dependent reduction steps are involved in NADP-dependent malate dehydrogenase light activation, hence that two disulfides per monomer participate in the process. The overall activation rate would depend on a conformational change following the reduction of the amino-terminal disulfide bridge. The amino terminus also plays a role in the dimerization of the protein.


Assuntos
Grão Comestível/enzimologia , Malato Desidrogenase/metabolismo , Tiorredoxinas/metabolismo , Sequência de Bases , DNA , Dissulfetos/metabolismo , Eletroforese em Gel de Poliacrilamida , Ativação Enzimática/efeitos da radiação , Luz , Malato Desidrogenase/antagonistas & inibidores , Malato Desidrogenase/genética , Malato Desidrogenase (NADP+) , Dados de Sequência Molecular , Mutagênese Sítio-Dirigida , Plasmídeos , Proteínas Recombinantes/antagonistas & inibidores , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo
16.
Plant Physiol ; 74(2): 448-50, 1984 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-16663441

RESUMO

Chloroplastic glutamine synthetase from tobacco leaves (Nicotiana tabacum L. var Xanthi) was purified to homogeneity. By using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and high performance liquid chromatography, a single subunit was identified with a molecular weight of 45,000 daltons. However the native protein seems to be composed of four different subunits which can be separated by isoelectrofocusing. It is suggested that different genes with eventual posttranslational and/or posttranscriptional modifications may control the synthesis of the chloroplastic glutamine synthetase.

17.
J Biol Chem ; 269(5): 3511-7, 1994 Feb 04.
Artigo em Inglês | MEDLINE | ID: mdl-8106392

RESUMO

Unique among malate dehydrogenases, the NADP-dependent chloroplastic form undergoes a reductive activation in the light. This process is thioredoxin-mediated and involves at least two disulfides. Only one of them, situated near the N terminus, has been localized. The enzyme also bears 2 cysteines at the C terminus. The possible role of these cysteines was investigated by replacing them separately, or together, by alanines, by site-directed mutagenesis. The proteins altered at the C terminus were still dithiol-dependent for full activation, with activation kinetics similar to those of the wild type enzyme. However, they exhibited a weak activity in the oxidized form with a dramatically increased Km for oxalacetate. Their activation was not inhibited by NADP. When C-terminal Cys mutations were combined with N-terminal Cys mutations, permanently active, thioredoxin-independent enzymes were obtained. They exhibited the biochemical properties of the activated wild type protein. Clearly, the 2 C-terminal cysteines constitute the second thioredoxin-dependent regulatory disulfide of NADP-malate dehydrogenase. Integrating our data about the characteristics of each of the regulatory disulfides and information from three-dimensional structure modeling, we propose a model for the redox control of NADP-malate dehydrogenase.


Assuntos
Cisteína , Dissulfetos/análise , Malato Desidrogenase/química , Malato Desidrogenase/metabolismo , NADP/metabolismo , Poaceae/enzimologia , Estrutura Secundária de Proteína , Sequência de Aminoácidos , Sequência de Bases , Cloroplastos/enzimologia , Gráficos por Computador , Ativação Enzimática , Cinética , Malato Desidrogenase (NADP+) , Modelos Moleculares , Dados de Sequência Molecular , Mutagênese Sítio-Dirigida , NADP/farmacologia , Oligodesoxirribonucleotídeos , Proteínas Recombinantes/química , Proteínas Recombinantes/isolamento & purificação , Proteínas Recombinantes/metabolismo
18.
Plant Mol Biol ; 26(1): 225-34, 1994 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-7948872

RESUMO

The recently cloned cDNA for pea chloroplast thioredoxin f was used to produce, by PCR, a fragment coding for a protein lacking the transit peptide. This cDNA fragment was subcloned into a pET expression vector and used to transform E. coli cells. After induction with IPTG the transformed cells produce the protein, mainly in the soluble fraction of the broken cells. The recombinant thioredoxin f has been purified and used to raise antibodies and analysed for activity. The antibodies appear to be specific towards thioredoxin f and do not recognize other types of thioredoxin. The recombinant protein could activate two chloroplastic enzymes, namely NADP-dependent malate dehydrogenase (NADP-MDH) and fructose 1,6-bisphosphatase (FBPase), both using dithiothreitol as a chemical reductant and in a light-reconstituted/thylakoid assay. Recombinant pea thioredoxin f turned out to be an excellent catalyst for NADP-MDH activation, being the more efficient than a recombinant m-type thioredoxin of Chlamydomonas reinhardtii and the thioredoxin of E. coli. At the concentrations of thioredoxin used in the target enzyme activation assays only the recombinant thioredoxin f activated the FBPase.


Assuntos
Escherichia coli/genética , Pisum sativum/química , Proteínas de Plantas/isolamento & purificação , Proteínas Recombinantes/isolamento & purificação , Tiorredoxinas , Sequência de Aminoácidos , Sequência de Bases , Tiorredoxinas de Cloroplastos , Indução Enzimática , Frutose-Bifosfatase/metabolismo , Expressão Gênica , Isopropiltiogalactosídeo , Malato Desidrogenase/metabolismo , Malato Desidrogenase (NADP+) , Dados de Sequência Molecular , Folhas de Planta/enzimologia , Proteínas de Plantas/genética , Proteínas de Plantas/imunologia , Proteínas de Plantas/metabolismo , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/imunologia , Proteínas Recombinantes/metabolismo , Alinhamento de Sequência , Análise de Sequência , Spinacia oleracea/enzimologia
19.
Eur J Biochem ; 199(1): 47-51, 1991 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-2065679

RESUMO

In this study, a cDNA clone coding for sorghum leaf NADP-malate dehydrogenase [Crétin, C., Luchetta, P., Joly, C., Decottignies, P., Lepiniec, L., Gadal, P., Sallantin, M., Huet, J. C. & Pernollet, J. C. (1990) Eur. J. Biochem. 192, 299-303] was used either in the full-length form or in a shorter form deprived of the 5' end coding for the transit peptide. Both cDNA fragments were cloned into the expression vector pKK233-2 and the resulting constructions were used to transform E. coli cells. The bacterial cells which do not contain any NADP-dependent malate dehydrogenase before transformation were able to express the protein after transformation and induction, as detected both by activity measurements and by immunoblot. The recombinant proteins could be purified to homogeneity and their biochemical characteristics studied. They were identical to those of the enzyme isolated from corn or sorghum leaves, including the well known redox regulatory properties. The NADP-malate dehydrogenases derived from both constructions had a similar subunit size and the analysis of their N-terminal sequences revealed that E. coli cells were able to recognize the processing signal of the precursor polypeptide and to mature and assemble the protein in a manner similar to higher plants.


Assuntos
Escherichia coli/genética , Regulação Bacteriana da Expressão Gênica , Malato Desidrogenase/genética , Plantas/enzimologia , Sequência de Aminoácidos , DNA/genética , Eletroforese em Gel de Poliacrilamida , Genes Bacterianos , Malato Desidrogenase (NADP+) , Dados de Sequência Molecular , Plasmídeos , Proteínas Recombinantes/genética
20.
Eur J Biochem ; 174(3): 497-501, 1988 Jun 15.
Artigo em Inglês | MEDLINE | ID: mdl-3391167

RESUMO

The mechanisms underlying the photoregulation of the synthesis of sorghum leaf malate dehydrogenase (NADP) (EC 1.1.1.82) (NADP-MDH), a key enzyme in C4 photosynthesis, have been investigated. During the greening process a light-dependent increase in enzyme activity took place, accompanied by de novo synthesis of the protein. In vitro translation experiments showed that this chloroplastic protein is synthesized as a precursor (46 kDa) with a 'transit peptide' of about 2.5 kDa. A large increase in NADP-MDH-translatable RNAs was also observed during greening. We describe also the construction and characterization of a cDNA clone for NADP-MDH (pCM18A) in the expression vector lambda gt11. The use of this homologous probe demonstrated a light-dependent mRNA accumulation.


Assuntos
Clonagem Molecular , DNA/análise , Malato Desidrogenase/genética , Plantas/enzimologia , RNA Mensageiro/biossíntese , Eletroforese em Gel de Poliacrilamida , Ativação Enzimática , Luz , Malato Desidrogenase/biossíntese , Biossíntese de Proteínas/efeitos da radiação , RNA Mensageiro/efeitos da radiação
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