Caracterización de los aspectos evolutivos, bioquímicos y regulatorios del metabolismo del almidón

El almidón es la principal forma de reserva de carbono en plantas superiores y constituye el polisacárido de mayor importancia en la dieta humana. Este polímero está formado por dos componentes mayoritarios: amilosa, que está compuesta predominantemente por cadenas lineales de glucosa con uniones α-1,4; y amilopectina, un α-1,4 glucano con ramificaciones en α-1,6. A través de la formación de los gránulos insolubles semicristalinos de almidón, las células logran mantener al mínimo el efecto osmótico que causaría esta gran cantidad de residuos de glucosa por separado. El complejo ordenamiento a nivel molecular de estas estructuras involucra a una gran cantidad de enzimas asociadas a la síntesis del almidón. Entre ellas encontramos las almidón sintasas (SS, EC 2.4.1.21) tanto solubles como unidas a gránulo, las enzimas ramificantes (BE, EC 2.4.1.18) involucradas en la generación de los enlaces α-1,6, y las enzimas deramificantes (DBE, EC 3.2.1.68) responsable de la escisión de ramificaciones ubicadas en posiciones no compatibles con la estructura altamente ordenada del gránulo. Si bien los mecanismos exactos de inicio de síntesis del gránulo no fueron dilucidados hasta el momento, se ha visto que la gran mayoría de plantas sintetizan más de un gránulo excepto el organismo eucariota fotosintético más pequeño conocido hasta la fecha, Ostreococcus tauri. Este alga unicelular posee un único gránulo de almidón situado en el único cloroplasto presente en la célula que, al momento de la división celular, se particiona de tal manera que dota de un gránulo a cada uno de sus descendientes. En esta tesis intentamos ampliar los conocimientos sobre los mecanismos moleculares que gobiernan el metabolismo del almidón en Ostreococcus tauri basándonos fundamentalmente en los procesos de síntesis y haciendo principal énfasis en sus aspectos bioquímicos, evolutivos y regulatorios.En una primera sección se presenta la completa caracterización de la enzima ramificante OsstaSBE. Los parámetros que caracterizan la cinética enzimática de OsttaSBE se encuentran dentro de lo esperado para ortólogos de plantas superiores. El modelo molecular propuesto a partir del modelado por homología no solo resulta de buena calidad de acuerdo a criterios aceptados por la comunidad científica, sino que también permitieron la exitosa identificación de los residuos más importantes para la catálisis. Posteriormente se logró corroborar esta información mediante la generación de proteínas recombinantes mutantes para cada uno de estos aminoácidos, las cuales, al no presentar actividad enzimática, demostraron la importancia de los mismos a nivel catalítico. Se detalla también el comportamiento de sus dos módulos de unión a carbohidratos presentes en la estructura de la proteína, frente a la presencia de distintos polisacáridos. Se determinó, mediante la generación de proteínas truncadas, la necesidad absoluta de la presencia de uno de estos módulos, siendo a su vez el primer reporte de un módulo de esta familia en una enzima ramificante.En una segunda sección se detalla la generación de líneas transgénicas de Arabidopsis thaliana sobreexpresando OsttaSBE. Estas líneas presentan una clara disminución en el tamaño de sus gránulos de almidón, demostrando la gran importancia de la enzima ramificante en su morfología. El aumento de los niveles de transcriptos de OsttaSBE trae aparejado un concomitante aumento de aquellos transcriptos que codifican para la almidón sintasa III endógena, en sintonía con la formación de complejos macromoleculares previamente reportados. Si bien nuestros ensayos de interacción no pudieron demostrar la interacción con la isoforma B de la almidón sintasa III de Ostreococcus, entendemos que en el alga esta asociación puede estar dándose tanto con la isoforma A como con la C, las cuales no hemos podido expresar en su forma entera hasta la fecha. Sumado al gránulo de menores proporciones se detectó un aumento generalizado de la degradación del almidón, consecuencia de un mecanismo de constante reestructuración de los gránulos que no llegan a desarrollar los tamaños observados en las líneas salvajes.En la última sección se presenta la caracterización de un polipéptido (OsttaAMILASA) cuya estructura modular presenta un dominio de unión a carbohidratos de la familia 20 y un dominio de hélice superenrollada que suele estar ligado a la interacción proteína-proteína. Los CBM20 están asociados a proteínas de degradación como por ejemplo amilasas, glucoamilasas y la proteína Laforina presente en Homo sapiens cuya función es similar a las fosfoglucano fosfatasas de plantas. Si bien no se pudo contar con la información proveniente de ortólogos en otros organismos, ya que los alineamientos de la secuencia completa de OsttaAMILASA no arrojaron resultados satisfactorios, sí se pudo hacer un análisis de los perfiles de expresión en el ritmo circadiano. Esta proteína no presenta perfiles de expresión típicos de enzimas degradativas como pudimos ver gracias al análisis de datos de RNA-Seq que se obtuvieron de mediciones llevadas a cabo a lo largo de día. OsttaAMILASA presenta una elevada afinidad por el almidón a través de su CBM, y también forma complejos macromoleculares con la almidón sintasa III B de Ostreococcus. Estos datos sugieren un mecanismo de asociación de las almidón sintasas al gránulo durante la síntesis, llevado a cabo por OsttaAMILASA.Fil: Hedin, Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentin

Functional and structural characterization of a novel isoamylase from ostreococcus tauri and role of the n-terminal domain

Background: The debranching starch enzymes, isoamylase 1 and 2 are well-conserved enzymes present in almost all the photosynthetic organisms. These enzymes are involved in the crystallization process of starch and are key components which remove misplaced α-1,6 ramifications on the final molecule. Aim: In this work, we performed a functional and structural study of a novel isoamylase from Ostreococcus tauri. Methods: We identified conserved amino acid residues possibly involved in catalysis. We also identified a region at the N-terminal end that resembles a Carbohydrate Binding Domain (CBM), which is more related to the family CBM48, but has no spatial conservation of the residues involved in carbohydrate binding. Results: The cloning, expression and biochemical characterization of this N-terminal region confirmed that it binds to polysaccharides, showing greater capacity for binding to amylopectin rather than total starch or amylose. Conclusion: This module could be a variant of the CBM48 family or it could be classified within a new CBM family.Fil: Hedin, Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Barchiesi, Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentin

Characterization of SdGA, a cold-adapted and salt-tolerant glucoamylase from Saccharophagus degradans

Glucoamylases (GAs) are hydrolytic enzymes also known as amyloglucosidases, glucan 1,4-alphaglucosidases or exo-1,4-1,6 bonds) from the non- -Dglucose. These are typically microbial enzymes present in archaea, bacteria and fungi but absent in animals and plants, and they are classified into the GH15 family of glycoside hydrolases (www.cazy.org).-amylases and pullulanases) occurs in the process of saccharification of partially processed starch or dextrins to obtain glucose. Currently, there is strong interest in finding GAs with a better performance at low temperatures because these enzymes would avoid the heating requirement in some industrial processes such as starch saccharification among others, and, in this way, production costs could be minimized. Saccharophagus degradans is a  gramnegative marine bacterium. It is the most versatile bacterium in terms of the degradation of complex polymers (CP) found to date. It is capable to degrade at least 10 complex polymers such as starch, agar, laminarin, cellulose, pectin, alginate, chitin, fucoidan, pectin, pullulan, and xylan at high rate. The objective of this work is to carry out the structural characterization and functional properties of SdGA, a novel glucoamylase (GA) from S. degradans. The enzyme is composed mainly of a N-terminal GH15_N domainlinked to a C-terminal catalytic domain (CD) found in the GH15 family of glycosylhydrolases with an overall structure similar to other bacterial GAs. The protein was successfully expressed in Escherichia coli cells, purified and its biochemical properties were investigated. SdGA showed maximum activity at 39°C and pH 6.0. The enzyme has high activity in a wide range, from low to mild temperatures, like cold-adapted enzymes. It showed the same maximum activity in the range of 0 1.0 M NaCl like salt-tolerant amylases.By thermal inactivation assays, we determined that SdGA is thermolabile at temperatures above 42°C and we found that glycerol 10% (V/V), acarbose 0.1 mM and NaCl 1 M stabilized the enzyme. Furthermore, we analyze the CD of SdGA, other cold-adapted, psychrophilic and thermostable GAs and we found that SdGA has a larger CD due to various amino acid insertions and a higher content of flexible residues compared to other thermostable GAs. These characteristics of SdGA allow it to be classified as a coldadaptedenzyme but also, a salt-tolerant enzyme. We propose that this novel SdGA, might have potential applications for use in different industrial processes that require an efficient alpha glucosidase activity at low/mild temperatures, such as biofuel production.Fil: Wayllace, Natael Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Hedin, Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaTercer Encuentro de Red Argentina de Tecnología Enzimática; Primer Workshop de la Red Argentina de Tecnología EnzimáticaRosarioArgentinaRed Argentina de Tecnología Enzimátic

Functional demonstrations of starch binding domains present in Ostreococcus tauri starch synthases isoforms

Abstract Background: Starch‑binding domains are key modules present in several enzymes involved in polysaccharide metabolism. These non‑catalytic modules have already been described as essential for starch‑binding and the cata‑ lytic activity of starch synthase III from the higher plant Arabidopsis thaliana. In Ostreococcus tauri, a unicellular green alga of the Prasinophyceae family, there are three SSIII isoforms, known as Ostta SSIII‑A, SSIII‑B and SSIII‑C. Results: In this work, using in silico and in vitro characterization techniques, we have demonstrated that Ostta SSIII‑ A, SSIII‑B and SSIII‑C contain two, three and no starch‑binding domains, respectively. Additionally, our phylogenetic analysis has indicated that OsttaSSIII‑B, presenting three N‑terminal SBDs, is the isoform more closely related to higher plant SSIII. Furthermore, the sequence alignment and homology modeling data gathered showed that both the main 3‑D structures of all the modeled domains obtained and the main amino acid residues implicated in starch binding are well conserved in O. tauri SSIII starch‑binding domains. In addition, adsorption assays showed that OsttaSSIII‑A D2 and SSIII‑B D2 domains are the two that make the greatest contribution to amylose and amylopectin binding, while OsttaSSIII‑B D1 is also important for starch binding. Conclusions: The results presented here suggest that differences between OsttaSSIII‑A and SSIII‑B SBDs in the number of and binding of amino acid residues may produce differential affinities for each isoform to polysaccharides. Increasing the knowledge about SBDs may lead to their employment in biomedical and industrial applications. Keywords: Ostreococcus tauri, Starch‑binding domains, Starch synthase, Homology modeling, Adsorption assayFil: Barchiesi, Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Hedin, Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaFil: Ballicora, Miguel. Loyola University Chicago; Estados UnidosFil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentin

CBM20CP, a novel functional protein of starch metabolism in green algae

Ostreococcus tauri is a marine picoalga, the smallest free-living eukaryotic and the simplest photosynthetic organism described to date, which has a single chloroplast and mitochondrion. The O. tauri genome codes for less than 8000 genes with low genetic redundancy, however, the pathway of starch metabolism would be conserved. This alga has all the enzymes that participate in the synthesis of starch in higher plants encoded in its genome, at least one ADPGlucose pyrophosphorylase (ADPGlc PPase), one GBSS, SSs I-III (SSI, II, and III), SBEI-II and ISA1- found. It is well known that SSIV regulates the number of starch granules in Arabidopsis and would also participate in the initiation of starch synthesis. The fact that O. tauri contains a single starch granule could be related to the lack of this enzyme. Moreover, we previously described the presence of three different isoforms of SSIII with a variable number of Starch binding domains (SBDs), suggesting that the synthesis and regulation of starch metabolism in this organism is highly complex. SBDsare a special subfamily of CBMs that bind to starch and have acquired the evolutionary advantage of being able to disrupt the surface of their substrate due to the presence of two binding sites. These domains have been classified into thirteen families, in special SBDs included in CBM20 family were first found in starch hydrolases, however, they are present in several amylolytic and non-amylolytic enzymes from plants, mammals, archaea, bacteria, and fungi. In general, CBM20 are attached also to a CD and many of them have regulatory functions and a moderate affinity to starch. Only few proteins from algae containing a CBM20 have been characterized, such a laforin homolog from the red algae Chondrus crispus and a the SAGA1 protein from C. reinhardtii, which is involved in shaping starch plates. Although the O.tauri genome is fully sequenced, there are still many genes and proteins to which no function was assigned. Here, we identify the OT_ostta06g01880 gene that encodes CBM20CP, a plastid protein which contains a central carbohydrate binding domain of the CBM20 family, a coiled coil domain at the C-terminus and lacks catalytic activity. We demonstrate that CBM20CP has the ability to bind starch, amylose and amylopectin with different affinities. Furthermore, this protein interacts with OsttaSSIII-B, increasing its binding to starch granules, its catalytic efficiency and promoting granule growth. The results allow us to postulate a regulatory role for CBM20CP in starch metabolism in green algae.Fil: Velázquez, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Hedin, Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Barchiesi, Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaLVII SAIB Meeting; XVI SAMIGE MeetingCiudad Autónoma de Buenos AiresArgentinaSociedad Argentina de Investigación en Bioquímica y Biología MolecularAsociación Civil de Microbiología Genera

Transforming European Water Governance? Participation and River Basin Management under the EU Water Framework Directive in 13 Member States

The European Union (EU) Water Framework Directive (WFD) requires EU member states to produce and implement river basin management plans, which are to be designed and updated via participatory processes that inform, consult with, and actively involve all interested stakeholders. The assumption of the European Commission is that stakeholder participation, and institutional adaptation and procedural innovation to facilitate it, are essential to the effectiveness of river basin planning and, ultimately, the environmental impact of the Directive. We analyzed official documents and the WFD literature to compare implementation of the Directive in EU member states in the initial WFD planning phase (2000–2009). Examining the development of participatory approaches to river basin management planning, we consider the extent of transformation in EU water governance over the period. Employing a mixed quantitative and qualitative approach, we map the implementation “trajectories” of 13 member states, and then provide a detailed examination of shifts in river basin planning and participation in four member states (Germany, Sweden, Poland and France) to illustrate the diversity of institutional approaches observed. We identify a general tendency towards increased, yet circumscribed, stakeholder participation in river basin management in the member states examined, alongside clear continuities in terms of their respective pre-WFD institutional and procedural arrangements. Overall, the WFD has driven a highly uneven shift to river basin-level planning among the member states, and instigated a range of efforts to institutionalize stakeholder involvement—often through the establishment of advisory groups to bring organized stakeholders into the planning process

Dose-Dependent Immunomodulation of Human Dendritic Cells by the Probiotic Lactobacillus rhamnosus Lcr35

The response of the immune system to probiotics remains controversial. Some strains modulate the cytokine production of dendritic cells (DCs) in vitro and induce a regulatory response, while others induce conversely a pro-inflammatory response. These strain-dependent effects are thought to be linked to specific interactions between bacteria and pattern recognition receptors. We investigated the effects of a well characterized probiotic strain, Lactobacillus rhamnosus Lcr35, on human monocyte-derived immature DCs, using a wide range of bacterial concentrations (multiplicity of infection, MOI, from 0.01 to 100). DNA microarray and qRT-PCR analysis showed that the probiotic induced a large-scale change in gene expression (nearly 1,700 modulated genes, with 3-fold changes), but only with high doses (MOI, 100). The upregulated genes were mainly involved in immune response and identified a molecular signature of inflammation according to the model of Torri. Flow cytometry analysis also revealed a dose-dependent maturation of the DC membrane phenotype, until DCs reached a semi-mature state, with an upregulation of the membrane expression of CD86, CD83, HLA-DR and TLR4, associated with a down-regulation of DC-SIGN, MR and CD14. Measurement of the DC-secreted cytokines showed that Lcr35 induced a strong dose-dependent increase of the pro-Th1/Th17 cytokine levels (TNFα, IL-1β, IL-12p70, IL-12p40 and IL-23), but only a low increase in IL-10 concentration. The probiotic L. rhamnosus Lcr35 therefore induce a dose-dependent immunomodulation of human DCs leading, at high doses, to the semi-maturation of the cells and to a strong pro-inflammatory effect. These results contribute to a fuller understanding of the mechanism of action of this probiotic, and thus of its potential clinical indications in the treatment of either infectious or IgE-dependent allergic diseases

Metabolic adaptation of a Chlamydomonas acidophila strain isolated from acid mine drainage ponds with low eukaryotic diversity

© 2018 Elsevier B.V. The diversity and biological characteristics of eukaryotic communities within acid mine drainage (AMD) sites is less well studied than for prokaryotic communities. Furthermore, for many eukaryotic extremophiles the potential mechanisms of adaptation are unclear. This study describes an evaluation of eight highly acidic (pH 1.6–3.1) and one moderately acidic (pH 5.6) metal-rich acid mine drainage ponds at a disused copper mine. The severity of AMD pollution on eukaryote biodiversity was examined, and while the most species-rich site was less acidic, biodiversity did not only correlate with pH but also with the concentration of dissolved and particulate metals. Acid-tolerant microalgae were present in all ponds, including the species Chlamydomonas acidophila, abundance of which was high in one very metal-rich and highly acidic (pH 1.6) pond, which had a particularly high PO4-P concentration. The C. acidophila strain named PM01 had a broad-range pH tolerance and tolerance to high concentrations of Cd, Cu and Zn, with bioaccumulation of these metals within the cell. Comparison of metal tolerance between the isolated strain and other C. acidophila strains previously isolated from different acidic environments found that the new strain exhibited much higher Cu tolerance, suggesting adaptation by C. acidophila PM01 to excess Cu. An analysis of the metabolic profile of the strains in response to increasing concentrations of Cu suggests that this tolerance by PM01 is in part due to metabolic adaptation and changes in protein content and secondary structure

Research and Design of a Routing Protocol in Large-Scale Wireless Sensor Networks

无线传感器网络，作为全球未来十大技术之一，集成了传感器技术、嵌入式计算技术、分布式信息处理和自组织网技术，可实时感知、采集、处理、传输网络分布区域内的各种信息数据，在军事国防、生物医疗、环境监测、抢险救灾、防恐反恐、危险区域远程控制等领域具有十分广阔的应用前景。 本文研究分析了无线传感器网络的已有路由协议，并针对大规模的无线传感器网络设计了一种树状路由协议，它根据节点地址信息来形成路由，从而简化了复杂繁冗的路由表查找和维护，节省了不必要的开销，提高了路由效率，实现了快速有效的数据传输。 为支持此路由协议本文提出了一种自适应动态地址分配算——ADAR（AdaptiveDynamicAddre...As one of the ten high technologies in the future, wireless sensor network, which is the integration of micro-sensors, embedded computing, modern network and Ad Hoc technologies, can apperceive, collect, process and transmit various information data within the region. It can be used in military defense, biomedical, environmental monitoring, disaster relief, counter-terrorism, remote control of haz...学位：工学硕士院系专业：信息科学与技术学院通信工程系_通信与信息系统学号：2332007115216

Applications of Bioinformatics to Plant Biotechnology

Bioinformatics encompasses many tools and techniques that today are essential for all areas of research in the biological sciences. New databases with a wealth of information about genomes, proteins, metabolites, and metabolic pathways appear almost daily. Particularly for scientists who carry out research in plant biology, the amount of information has multiplied exponentially due to the large number of databases available for many individual plant species. In this sense, bioinformatics together with next-generation sequencing and ‘omics’ approaches, can provide tools for plant breeding and the genetic engineering of plants. In addition, these technologies enable a better understanding of the processes and mechanisms that can lead to plants with increased tolerance to different abiotic stress conditions and resistance to pathogen attack, as well as the development of crop varieties with improved nutritional quality of seeds and fruits.Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Barchiesi, Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Peralta, Diego Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Hedin, Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Bhadauria, V.. University of Saskatchewan; Canad