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Germán Nic‑Matos,María Narváez,Santy Peraza‑Echeverría,Luis Sáenz,Carlos Oropeza 한국유전학회 2017 Genes & Genomics Vol.39 No.9
Nonexpressor of pathogenesis-related gene 1 (NPR1) codes for a transcription cofactor involved in the activation of systemic acquired resistance, a salicylic acid (SA)-dependent defense response. This work reports the cloning and characterization of two new genes, CnNPR1 and CnNPR3 from coconut, homologous to AtNPR1 of Arabidopsis thaliana. The cDNA deduced amino acid sequence contains the protein–protein interaction domains the BTB/POZ and ANKYRIN repeat domains, and a nuclear localization site (NLS). Phylogenetic analysis grouped CnNPR1 in a clade with AtNPR1 and CnNPR3 in a clade with AtNPR3, both reported genes of A. thaliana. Exogenous application of SA to coconut plantlets induced changes in the expression of CnNPR1 and CnNPR3 in leaf, stem and root tissues, providing evidence of their possible role in the signaling cascade leading to SAR in coconut palm. This is the first report on the cloning of putative key genes in the SAR-type defense mechanism in coconut palm.
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Edwin David Morales-Álvarez,Claudia Marcela Rivera-Hoyos,Angélica María Baena-Moncada,Patricia Landázuri,Raúl A. Poutou-Piñales,Homero Sáenz-Suárez,Luis A. Barrera,Olga Y. Echeverri-Peña 한국미생물학회 2013 The journal of microbiology Vol.51 No.2
The sulfatase family involves a group of enzymes with a large degree of similarity. Until now, sixteen human sulfatases have been identified, most of them found in lysosomes. Human deficiency of sulfatases generates various genetic disorders characterized by abnormal accumulation of sulfated intermediate compounds. Mucopolysaccharidosis type II is characterized by the deficiency of iduronate 2-sulfate sulfatase (IDS), causing the lysosomal accumulation of heparan and dermatan sulfates. Currently, there are several cases of genetic diseases treated with enzyme replacement therapy, which have generated a great interest in the development of systems for recombinant protein expression. In this work we expressed the human recombinant IDS-Like enzyme (hrIDS-Like) in Escherichia coli DH5α. The enzyme concentration revealed by ELISA varied from 78.13 to 94.35 ng/ml and the specific activity varied from 34.20 to 25.97 nmol/h/mg. Western blotting done after affinity chromatography purification showed a single band of approximately 40 kDa, which was recognized by an IgY polyclonal antibody that was developed against the specific peptide of the native protein. Our 100 ml-shake-flask assays allowed us to improve the enzyme activity seven fold,compared to the E. coli JM109/pUC13-hrIDS-Like system. Additionally, the results obtained in the present study were equal to those obtained with the Pichia pastoris GS1115/pPIC-9-hrIDS-Like system (3 L bioreactor scale). The system used in this work (E. coli DH5α/pGEX-3X-hrIDS-Like)emerges as a strategy for improving protein expression and purification, aimed at recombinant protein chemical characterization,future laboratory assays for enzyme replacement therapy, and as new evidence of active putative sulfatase production in E. coli.
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