2 resultados para Plants - Nitrogen metabolism
em QSpace: Queen's University - Canada
Resumo:
Climate change is occurring most rapidly in the Arctic where warming has been twice as fast as the rest of the globe over the last few decades. Arctic soils contain a vast store of carbon and warmer arctic soils may mediate current atmospheric CO2 concentrations and global warming trends. Warmer soils could increase nutrient availability to plants, leading to increased primary production and sequestration of CO2. Presumably because of these effects of warming on shrub ecosystems, shrubs have been expanding across the arctic over the last 50 years, Arctic shrub expansion may track or cause changes in nutrient cycling and availability that favour growth of larger, denser shrubs. This study aimed at measuring gross and net nitrogen cycling rates, major soil nitrogen and carbon pool sizes, and elucidating controls on nutrient cycling and availability between a mesic birch (Betula nana) hummock tundra ecosystem and an ecosystem of dense, tall, birch (B. nana) shrubs. Nitrogen cycling and availability was enhanced at the tall shrub ecosystem compared to the birch hummock ecosystem. Net nitrogen immobilization by microbes was approximately threefold greater at the tall shrub ecosystem. This was in part because of larger microbial biomass nitrogen and carbon (interpreted as a larger microbial community) at the tall shrub ecosystem. Nitrogen inputs via litter were significantly larger at the tall shrub ecosystem and were hypothesized to be the major contributor to the higher dissolved organic and inorganic nitrogen pools in the soil at the tall shrub ecosystem. The results from this study suggest a positive feedback mechanism between litter nitrogen inputs and the enhancement of nitrogen cycling and availability as a driver of shrub expansion across the Arctic.
Resumo:
Two distinct phosphoenolpyruvate carboxylase (PEPC) isozymes occur in vascular plants and green algae: plant-type PEPC (PTPC) and bacterial-type PEPC (BTPC). PTPC polypeptides typically form a tightly regulated cytosolic Class-1 PEPC homotetramer. BTPCs, however, appear to be less widely expressed and to exist only as catalytic and regulatory subunits that physically interact with co-expressed PTPC subunits to form hetero-octameric Class-2 PEPC complexes that are highly desensitized to Class-1 PEPC allosteric effectors. Yeast two-hybrid studies indicated that castor plant BTPC (RcPPC4) interacts with all three Arabidopsis thaliana PTPC isozymes, and that it forms stronger interactions with AtPPC2 and AtPPC3, suggesting that specific PTPCs are preferred for Class-2 PEPC formation. In contrast, Arabidopsis BTPC (AtPPC4) appeared to interact very weakly with AtPPC2 and AtPPC3, suggesting that BTPCs from different species may have different physical properties, hypothesized to be due to sequence dissimilarities within their ~10 kDa intrinsically disordered region. Recent RNA-seq and microarray data were analyzed to obtain a better understanding of BTPC expression patterns in different tissues of various monocot and dicot species. High levels of BTPC transcripts, polypeptides and Class-2 PEPC complexes were originally discovered in developing castor seeds, but the analysis revealed a broad range of diverse tissues where abundant BTPC transcripts are also expressed, such as the developing fruits of cucumber, grape, and tomato. Marked BTPC expression correlated well with the presence of ~116 kDa immunoreactive BTPC polypeptides, as well as Class-2 PEPC complexes in the immature fruit of cucumbers and tomatoes. It is therefore hypothesized that in vascular plants BTPC and thus Class-2 PEPC complexes maintain anaplerotic PEP flux in tissues with elevated malate levels that would potently inhibit ‘housekeeping’ Class-1 PEPCs. Elevated levels of malate can be used by biosynthetically active sink tissues such as immature tomatoes and cucumbers for rapid cell expansion, drought or salt stressed roots for osmoregulation, and developing seeds and pollen as a precursor for storage lipid and protein biosynthesis.