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661 result(s) for "SINTESIS DE PROTEINAS"
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Slow and fast dietary proteins differently modulate postprandial protein accretion
The speed of absorption of dietary amino acids by the gut varies according to the type of ingested dietary protein. This could affect postprandial protein synthesis, breakdown, and deposition. To test this hypothesis, two intrinsically 13C-leucine-labeled milk proteins, casein (CAS) and whey protein (WP), of different physicochemical properties were ingested as one single meal by healthy adults. Postprandial whole body leucine kinetics were assessed by using a dual tracer methodology. WP induced a dramatic but short increase of plasma amino acids. CAS induced a prolonged plateau of moderate hyperaminoacidemia, probably because of a slow gastric emptying. Whole body protein breakdown was inhibited by 34% after CAS ingestion but not after WP ingestion. Postprandial protein synthesis was stimulated by 68% with the WP meal and to a lesser extent (+31%) with the CAS meal. Postprandial whole body leucine oxidation over 7 h was lower with CAS (272 +/- 91 micromoles . kg-1) than with WP (373 +/- 56 micromoles . kg-1). Leucine intake was identical in both meals (380 micromoles . kg-1). Therefore, net leucine balance over the 7 h after the meal was more positive with CAS than with WP (P 0.05, WP vs. CAS). In conclusion, the speed of protein digestion and amino acid absorption from the gut has a major effect on whole body protein anabolism after one single meal. By analogy with carbohydrate metabolism, slow and fast proteins modulate the postprandial metabolic response, a concept to be applied to wasting situations
Accumulation of an acidic dehydrin in the vicinity of the plasma membrane during cold acclimation of wheat
Expression of the acidic dehydrin gene wcor410 was found to be associated with the development of freezing tolerance in several Gramineae species. This gene is part of a family of three homologous members, wcor410, wcor410b, and wcor410c, that have been mapped to the long arms of the homologous group 6 chromosomes of hexaploid wheat. To gain insight into the function of this gene family, antibodies were raised against the WCOR410 protein and affinity purified to eliminate cross-reactivity with the WCS120 dehydrin-like protein of wheat. Protein gel blot analyses showed that the accumulation of WCOR410 proteins correlates well with the capacity of each cultivar to cold acclimate and develop freezing tolerance. Immunoelectron microscope analyses revealed that these proteins accumulate in the vicinity of the plasma membrane of cells in the sensitive vascular transition area where freeze-induced dehydration is likely to be more severe. Biochemical fractionation experiments indicated that WCOR410 is a peripheral protein and not an integral membrane protein. These results provide direct evidence that a subtype of the dehydrin family accumulates near the plasma membrane. The properties, abundance, and localization of these proteins suggest that they are involved in the cryoprotection of the plasma membrane against freezing or dehydration stress. We propose that WCOR410 plays a role in preventing the destabilization of the plasma membrane that occurs during dehydrative conditions
Calmodulin and calmodulin-binding proteins in plants
▪ Abstract  Calmodulin is a small Ca 2+ -binding protein that acts to transduce second messenger signals into a wide array of cellular responses. Plant calmodulins share many structural and functional features with their homologs from animals and yeast, but the expression of multiple protein isoforms appears to be a distinctive feature of higher plants. Calmodulin acts by binding to short peptide sequences within target proteins, thereby inducing structural changes, which alters their activities in response to changes in intracellular Ca 2+ concentration. The spectrum of plant calmodulin-binding proteins shares some overlap with that found in animals, but a growing number of calmodulin-regulated proteins in plants appear to be unique. Ca 2+ -binding and enzymatic activation properties of calmodulin are discussed emphasizing the functional linkages between these processes and the diverse pathways that are dependent on Ca 2+ signaling.
Mechanisms of maize adaptation associated with Glomus spp. in soils with low phosphorus availability
La deficiencia de fósforo es uno de los mayores limitantes para la productividad agrícola en el trópico. Esta investigación está orientada a estudiar los mecanismos de adaptación de maíz asociado a Glomus spp. La investigación se realizó bajo condiciones controladas en los laboratorios del Corpoica. El diseño experimental utilizado fue bloques completos al azar, con seis tratamientos y seis repeticiones: tres tratamientos con 1, 40 y 100 mg·kg-1 de P en el suelo y los anteriores niveles de P más Glomus spp. Los resultados experimentales confirman una disminución en área foliar y materia seca relacionadas con bajo P en suelo, 20 días de la emergencia. Como mecanismos de adaptación a las deficiencias de P, las plántulas trastocan carbohidratos a la raíz en detrimento de las hojas, esto modifica el balance de la materia seca. Este mecanismo fue evidente a 10 días después del estrés. Plantas asociadas a Glomus presentaron mayores tasas de crecimiento, nutrición mineral (N, P, K, Ca, Mg, S) y concentración de azúcares en tejido, debido al papel P en la síntesis de carbohidratos. Plantas micorrizadas aumentaron los niveles de proteínas en tejido, con 1 y 40 mg·kg-1 de P en suelo. Los resultados sugieren que Glomus spp. contribuye con la síntesis de proteínas de estrés en planta, por déficit de P en el suelo. El estrés conduce a la expresión diferencial de la información genética, produciendo cambios en la síntesis de nuevas proteínas, llamadas micorrizinas, las cuales posiblemente dotan a las plantas con la capacidad de adaptación al estrés Phosphorus deficiency is a major limitation to agricultural productivity in tropical regions. This research was addressed to study the mechanisms of maize adaptation in relation to Glomus spp. The research was conducted under controlled conditions in the laboratories of Corpoica, Colombia. The experimental design consisted in completely randomized blocks with six treatments and six replicates: three treatments with different levels of available phosphorus in soil (1, 40 y 100 mg·kg-1) and the other three with the same P levels plus Glomus spp. The experimental results confirmed a reduction in leaf area and dry matter related to low P levels in soil at 20 days after seedling emergence. As an adaptation mechanism for P deficiency, the seedlings transferred the carbohydrates to the roots at the expense of leaves, thus, modifying the balance of dry matter. This mechanism was evident 10 days after the stress application. Plants associated with Glomus spp. had the highest growth rates, mineral nutrition (N, K. P, Ca, Mg, and S), and sugar concentration in tissue, due to the importance of P in the synthesis of carbohydrates. Plants associated with mycorrhizal fungus increased the protein levels in tissue when amended with 1 and 40 mg·kg-1 of P in soil. The results suggest that Glomus spp. contributed to the synthesis of stress proteins because of soil phosphorus deficiency. The stress allows the differential expression of genetic information in the synthesis of new proteins called mycorrhizines, which are probably involved in the adaptation mechanisms of plants to stress
Induction of an outer surface protein on Borrelia burgdorferi during tick feeding
Lyme disease spirochetes, Borrelia burgdorferi sensu lato, are maintained in zoonotic cycles involving ticks and small mammals. In unfed ticks, the spirochetes produce one outer surface protein, OspA, but not OspC. During infection in mammals, immunological data suggest that the spirochetes have changed their surface, now expressing OspC but little or no OspA. We find by in vitro growth experiments that this change is regulated in part by temperature; OspC is produced by spirochetes at 32-37 degrees C but not at 24 degrees C. Furthermore, spirochetes in the midgut of ticks that have fully engorged on mice now have OspC on their surface. Thus two environmental cues, an increase in temperature and tick feeding, trigger a major alteration of the spirochetal outer membrane. This rapid synthesis of OspC by spirochetes during tick feeding may play an essential role in the capacity of these bacteria to successfully infect mammalian hosts, including humans, when transmitted by ticks
Aluminum induces oxidative stress genes in Arabidopsis thaliana
Changes in gene expression induced by toxic levels of Al were characterized to investigate the nature of Al stress. A cDNA library was constructed from Arabidopsis thaliana seedlings treated with Al for 2 h. We identified five cDNA clones that showed a transient induction of their mRNA levels, four cDNA clones that showed a longer induction period, and two down-regulated genes. Expression of the four long-term-induced genes remained at elevated levels for at least 48 h. The genes encoded peroxidase, glutathione-S-transferase, blue copper-binding protein, and a protein homologous to the reticuline:oxygen oxidoreductase enzyme. Three of these genes are known to be induced by oxidative stresses and the fourth is induced by pathogen treatment. Another oxidative stress gene, superoxide dismutase, and a gene for Bowman-Birk protease inhibitor were also induced by Al in A. thaliana. These results suggested that Al treatment of Arabidopsis induces oxidative stress. In confirmation of this hypothesis, three of four genes induced by Al stress in A. thaliana were also shown to be induced by ozone. Our results demonstrate that oxidative stress is an important component of the plant's reaction to toxic levels of Al
Hrp pilus: an hrp-dependent bacterial surface appendage produced by Pseudomonas syringae pv. tomato DC3000
Hypersensitive response and pathogenicity (hrp) genes control the ability of major groups of plant pathogenic bacteria to elicit the hypersensitive response (HR) in resistant plants and to cause disease in susceptible plants. A number of Hrp proteins share significant similarities with components of the type III secretion apparatus and flagellar assembly apparatus in animal pathogenic bacteria. Here we report that Pseudomonas syringae pv. tomato strain DC3000 (race 0) produces a filamentous surface appendage (Hrp pilus) of 6-8 nm in diameter in a solid minimal medium that induces hrp genes. Formation of the Hrp pilus is dependent on at least two hrp genes, hrpS and hrpH (recently renamed hrcC), which are involved in gene regulation and protein secretion, respectively. Our finding of the Hrp pilus, together with recent reports of Salmonella typhimurium surface appendages that are involved in bacterial invasion into the animal cell and of the Agrobacterium tumefaciens virB-dependent pilus that is involved in the transfer of T-DNA into plant cells, suggests that surface appendage formation is a common feature of animal and plant pathogenic bacteria in the infection of eukaryotic cells. Furthermore, we have identified HrpA as a major structural protein of the Hrp pilus. Finally, we show that a nonpolar hrpA mutant of P. syringae pv. tomato DC3000 is unable to form the Hrp pilus or to cause either an HR or disease in plants
The URE3 prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
The [URE3] nonchromosomal genetic element is a prion of Ure2p, a regulator of nitrogen catabolism in Saccharomyces cerevisiae. Ure2p1-65 is the prion domain of Ure2p, sufficient to propagate [URE3] in vivo. We show that full length Ure2p-green fluorescent protein (GFP) or a Ure2p1-65-GFP fusion protein is aggregated in cells carrying [URE3] but is evenly distributed in cells lacking the [URE3] prion. This indicates that [URE3] involves a self-propagating aggregation of Ure2p. Overexpression of Ure2p1-65 induces the de novo appearance of [URE3] by 1,000-fold in a strain initially [ure-o], but cures [URE3] from a strain initially carrying the [URE3] prion. Overexpression of several other fragments of Ure2p or Ure2-GFP fusion proteins also efficiently cures the prion. We suggest that incorporation of fragments or fusion proteins into a putative [URE3] \"crystal\" of Ure2p poisons its propagation