Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados BABT (1) Electron. J. Biotechnol. (1) Autor Li,Rui (2) Chen,Xiao (1) Li,Fosheng (1) Li,Jian (1) Wang,Qingwei (1) Wang,Shenghua (1) Wang,Wanjun (1) Wang,Wenguo (1) Xu,Ying (1) Yang,Qian (1) Zhao,Qi (1) Mais... Palavra-chave 3-Hydroxy-3-methylglutaryl-CoA reductases (1) Cysteine proteinase inhibitor (1) Expression pattern (1) Fritillaria cirrhosa (1) Jatropha curcas (1) Molecular cloning (1) Prokaryotic expression (1) Salinity stress (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Journal article (1) Ano 2018 (1) 2015 (1) País Brazil (1) Chile (1) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Overexpression of a cysteine proteinase inhibitor gene from Jatropha curcas confers enhanced tolerance to salinity stress Electron. J. Biotechnol. Li,Rui; Wang,Wanjun; Wang,Wenguo; Li,Fosheng; Wang,Qingwei; Xu,Ying; Wang,Shenghua. Background Cysteine proteinase inhibitor (cystatin, CPI) is one of the most important molecules involved in plant development and defense, especially in the regulation of stress responses. However, it is still unclear whether the Jatropha curcas CPI (JcCPI) gene functions in salinity response and tolerance. In this study, the sequence of the JcCPI gene, its expression pattern, and the effects of overexpression in Escherichia coli and Nicotiana benthamiana were examined. The purpose of this study was to evaluate the regulatory role of JcCPI in salinity stress tolerance. Results The CPI gene, designated JcCPI, was cloned from J. curcas; its sequence shared conserved domains with other plant cystatins. Based on a transcription pattern analysis, JcCPI was... Tipo: Journal article Palavras-chave: Cysteine proteinase inhibitor; Jatropha curcas; Salinity stress. Ano: 2015 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000500008 Cloning and Characterization of the Gene Encoding 3-hydroxy-3- Methylglutaryl-coenzyme A (HMG-CoA) Reductase from Fritillaria Cirrhosa D. Don BABT Zhao,Qi; Li,Rui; Chen,Xiao; Yang,Qian; Li,Jian. ABSTRACT The enzyme 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR; EC1.1.1.34) catalyzes the first committed step of isoprenoids biosynthesis in Mevalonate (MVA) pathway. Here we report for the first time the cloning and characterization of a full-length cDNA encoding HMGR from Fritillaria cirrhosa (FcHMGR), a bulbous medicinal plant. The full-length cDNA of FcHMGR was 2072 base pair (bp), containing a 1680-bp open reading frame. Bioinformatical analyses revealed that FcHMGR had HMG CoA-binding domains and two NADPH binding domains, which are required for HMGR activity. Quantitative real-time PCR (qRT-PCR) analysis revealed that FcHMGR expressed high in mature bulbs. A truncated version of FcHMGR protein lacking the N-terminal 249-bp GC rich area was... Tipo: Info:eu-repo/semantics/article Palavras-chave: 3-Hydroxy-3-methylglutaryl-CoA reductases; Fritillaria cirrhosa; Molecular cloning; Expression pattern; Prokaryotic expression. Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132018000100438 Registros recuperados: 2 Primeira ... 1 ... Última

Empresa Brasileira de Pesquisa Agropecuária - Embrapa Todos os direitos reservados, conforme Lei n° 9.610 Política de Privacidade Área restrita		Embrapa Parque Estação Biológica - PqEB s/n° Brasília, DF - Brasil - CEP 70770-901 Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco