Publicaciones 2011-2020

@article{RN347,
title = {Elucidation of Gibberellin Biosynthesis in Bacteria Reveals Convergent Evolution},
author = { R.S. Nett and M. Montanares and A. Marcassa and X. Lul and R. Nagel and T.C. Charles and P. Hedden and M.C. Rojas and R.J. Peters},
url = {/brokenurl#<Go to ISI>://WOS:000393267200015},
doi = {10.1038/Nchembio.2232},
issn = {1552-4450},
year = {2017},
date = {2017-01-01},
journal = {Nature Chemical Biology},
volume = {13},
number = {1},
pages = {69-74},
abstract = {Gibberellins (GAs) are crucial phytohormones involved in many aspects of plant growth and development, including plant-microbe interactions, which has led to GA production by plant-associated fungi and bacteria as well. While the GA biosynthetic pathways in plants and fungi have been elucidated and found to have arisen independently through convergent evolution, little has been uncovered about GA biosynthesis in bacteria. Some nitrogen-fixing, symbiotic, legume-associated rhizobia, including Bradyrhizobium japonicum-the symbiont of soybean and Sinorhizobium fredii-a broad-host-nodulating species-contain a putative GA biosynthetic operon, or gene cluster. Through functional characterization of five unknown genes, we demonstrate that this operon encodes the enzymes necessary to produce GA(9), thereby elucidating bacterial GA biosynthesis. The distinct nature of these enzymes indicates that bacteria have independently evolved a third biosynthetic pathway for GA production. Furthermore, our results also reveal a central biochemical logic that is followed in all three convergently evolved GA biosynthetic pathways.},
keywords = {artemisinin biosynthesis, bradyrhizobium-japonicum, cloning, cytochrome-p450 ent-kaurene, fungi, gene-cluster, green-revolution, identification, plants, rearrangement},
pubstate = {published},
tppubtype = {article}
}

@article{RN37c,
title = {Production of a Heterologous Recombinant Protein Using Fragments of the Glyceraldehyde-3-Phosphate Dehydrogenase Promoter from Penicillium Camemberti},
author = { Y. Espinosa and J. Trebotich and F. Sepulveda and J. Cadena and M.J. Vargas-Straube and I. Vaca and P. Bull and G. Levican and R. Chavez},
url = {/brokenurl#<Go to ISI>://WOS:000297594400033},
doi = {10.1007/s11274-011-0782-7},
issn = {0959-3993},
year = {2011},
date = {2011-01-01},
journal = {World Journal of Microbiology & Biotechnology},
volume = {27},
number = {12},
pages = {3019-3023},
abstract = {The biotechnological applications of cheese-ripening fungi have been limited by a lack of genetics tools, in particular the identification and characterization of suitable promoters for protein expression. In this study, the suitability of the glyceraldehyde-3-phosphate dehydrogenase (gpdP) promoter from Penicillium camemberti to drive the production of a recombinant protein was evaluated. The gpdP gene and its promoter were isolated using PCR and Genome Walker. The promoter of gpdP has two regions with high identity to the regulatory elements gpd-box and ct-box previously described in Aspergillus nidulans. Two fragments of the promoter containing the gpd- and ct-box or the ct-box alone were used to drive the in vivo production of recombinant beta-galactosidase using A. nidulans as host. Our results indicate that larger fragment containing gpd-box enhances the production of beta-galactosidase activity levels respect to ct-box alone, and that both boxes are necessary to obtain maximal enzymatic activity production. The smaller fragment (187 nt) containing the ct-box alone was able to trigger up to 27% of beta-galactosidase activity, and to our knowledge this is the smallest fragment from a gpd gene used to produce a recombinant protein. Differences were not observed when glycerol, galactose or glucose were used as carbon sources, suggesting that the promoter activity is carbohydrate-independent. This is the first report in which a Penicillium gpd promoter is used for recombinant protein production. Our results open the way for the future development of a system for recombinant proteins expression in the biotechnologically important cheese-ripening fungus P. camemberti.},
keywords = {aspergillus-nidulans, beta-galactosidase, camemberti, cloning, dehydrogenase elements, expression, functional gene, glyceraldehyde-3-phosphate gpda heterologous nidulans penicillium promoter, protein region sequence-analysis, transformation, yeast},
pubstate = {published},
tppubtype = {article}
}