Seld
Mostrando 1-12 de 20 artigos, teses e dissertações.
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1. Validação da via de biossíntese de selenocisteína e selenoproteínas em Trypanosoma por RNA de interferência
Selênio (Se) é um elemento essencial encontrado em selenoproteínas na forma do 21 aminoácido selenocisteína (Sec U). A incorporação co-traducional de Sec depende de uma complexa via de síntese, de um códon de terminação UGA em fase de leitura e uma estrutura terciária do RNA mensageiro conhecida como elemento SECIS. A maioria das selenoproteínas
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 24/04/2012
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2. Biophysical studies of Escherichia coli Selenophosphate Synthetase and investigation of its role in the Selenocysteine biosynthesis pathway / Estudos biofísicos da Selenofosfato Sintetase de Escherichia coli e investigação de seu papel na via de biossíntese de Selenocisteínas
A principal forma biológica do selênio em vários organismos é o aminoácido Selenocisteína (Sec, U), que é incorporado em um polipeptídio emergente em códons UGA específicos. Em Escherichia coli, esta incorporação requer os genes que codificam para Seril-tRNA Sintetase (SerRS), Selenocisteína Sintase (SELA), um tRNASec específico (SELC), Selenof
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 30/01/2012
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3. Identificação de elementos estruturais no tRNAsecuca determinantes da ligação com proteínas / Identification of structural elements of the tRNAsecuca determining its protein binding
Em Escherichia coli a formação e incorporação do aminoácido selenocisteína é um evento cotraducional dirigido pelo códon de terminação UGA e deve se a uma complexa via de biosíntese cujas principais proteínas envolvidas são: Selenocisteína sintase (SELA), Fator de elongação de selenocisteína (SELB), Selenofosfato sintetase (SELD), Seril-tRNA
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 25/01/2012
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4. Structural determination of Selenocysteine Synthase from Escherichia coli / Determinação estrutural da proteína Selenocisteína Sintase de Escherichia coli
A biossíntese do 21o. aminoácido, Selenocisteína (Sec - U), envolve uma complexa maquinaria enzimática composta, em eubactérias, pela Selenocisteína Sintase (SELA), Fator de Elongação de Selenocisteína (SELB), Selenofosfato Sintetase (SELD) e tRNA de Inserção Selenocisteína (tRNAsec). Em arqueobactérias e eucariotos existem ainda O fosforil tRNA
Publicado em: 2010
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5. Estudos moleculares das enzimas envolvidas na biossíntese de selenocisteína em Trypanosoma brucei e Leishmania major / Molecular studies of the enzymes involved in selenocysteine synthesis in Trypanosoma brucei and Leishmania major
One of the main biological forms of the selenium incorporation is the amino acid form named selenocysteine (Sec, U), which is incorporated co-translationally at the emerging new polypeptide in the specific positions at the UGA codon, that is usually recognized as stop codon. The incorporation of the selenocysteine in E.coli is already solved with the involve
Publicado em: 2008
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6. Estudos moleculares da Selenocisteína Sintase (SELA) de Escherichia coli.
The study of translation processes attracts the interest of a wide range of research groups due to its main role in general cellular metabolism. In particular, the investigation of new amino acid residues, such as selenocysteine and pyrrolysin, which result in an expansion of the genetic code from the traditional 20 residues to a total of 22 residues up to t
Publicado em: 2005
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7. In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product.
The selD gene from Escherichia coli, whose product is involved in selenium metabolism, has been cloned and sequenced. selD codes for a protein of 347 amino acids with a calculated molecular weight of 36,687. Analysis of the selD gene product through expression of the gene in the phage T7 promoter/polymerase system confirmed the predicted molecular weight of
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8. Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus.
An enzyme preparation from Salmonella typhimurium catalyzes the conversion of 5-methylaminomethyl-2-thiouridine in tRNAs to 5-methylaminomethyl-2-selenouridine when supplemented with selenide and ATP. Similar preparations from a Salmonella mutant strain carrying a defective selD gene fail to catalyze this selenium substitution reaction. However, supplementat
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9. Identification of a novel selD homolog from Eukaryotes, Bacteria, and Archaea: Is there an autoregulatory mechanism in selenocysteine metabolism?
Escherichia coli selenophosphate synthetase (SPS, the selD gene product) catalyzes the production of monoselenophosphate, the selenium donor compound required for synthesis of selenocysteine (Sec) and seleno-tRNAs. We report the molecular cloning of human and mouse homologs of the selD gene, designated Sps2, which contains an in-frame TGA codon at a si
The National Academy of Sciences of the USA.
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10. Expression of the putA gene encoding proline dehydrogenase from Rhodobacter capsulatus is independent of NtrC regulation but requires an Lrp-like activator protein.
Four Rhodobacter capsulatus mutants unable to grow with proline as the sole nitrogen source were isolated by random Tn5 mutagenesis. The Tn5 insertions were mapped within two adjacent chromosomal EcoRI fragments. DNA sequence analysis of this region revealed three open reading frames designated selD, putR, and putA. The putA gene codes for a protein of 1,127
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11. Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling l-selenocysteine and Sps2 for selenite assimilation
A labile selenium donor compound monoselenophosphate is synthesized from selenide and ATP by selenophosphate synthetase (SPS). In the present study, Sps1 and Sps2 were cloned from a cDNA library prepared from human lung adenocarcinoma cells (NCIH441). The human lung Sps1 has been cloned as an ORF of 1,179 bp, identical in sequence to that of the recently rev
National Academy of Sciences.
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12. Elevation of Glutamine Level by Selenophosphate Synthetase 1 Knockdown Induces Megamitochondrial Formation in Drosophila Cells*
Although selenophosphate synthetase 1 (SPS1/SelD) is an essential gene in Drosophila, its function has not been determined. To elucidate its intracellular role, we targeted the removal of SPS1/SelD mRNA in Drosophila SL2 cells using RNA interference technology that led to the formation of vacuole-like globular structures. Surprisingly, these structures were
American Society for Biochemistry and Molecular Biology.