\n\nKey Results Nitrogen content of all photosynthetic organs and in particular nitrogen vertical distribution along the stem and remobilization patterns in response to fertilization were simulated accurately by the model, from Rubisco turnover modulated by light intercepted by the organ and a mobile nitrogen pool. This pool proved to be a reliable indicator of plant nitrogen status, allowing efficient regulation of nitrogen acquisition by roots, remobilization from vegetative organs and accumulation in grains in response to

nitrogen treatments. In our simulations, root capacity to import carbon, rather than carbon availability, limited nitrogen Copanlisib mouse acquisition and ultimately nitrogen accumulation in grains, while Rubisco turnover intensity mostly affected dry matter accumulation in grains.\n\nConclusions NEMA enabled interpretation of several key patterns usually observed in field conditions and the identification of plausible processes limiting for grain yield, protein content and root nitrogen acquisition that could be targets for plant breeding; however, further understanding requires more mechanistic formalization of carbon metabolism. Its strong physiological basis and its realistic behaviour support its use to gain insights into nitrogen economy after flowering.”
“Synopsis image This study, published alongside

one from the Nilsson laboratory, shows that Mad1 mutants that still recruit Mad2 to kinetochores cannot activate the spindle assembly checkpoint in yeast. Thus, Mad1 has an additional, hitherto PARP inhibitor cancer unidentified role in this process. The Mad1 C-terminus and Bub1 conserved motif 1 are required for kinetochore localization of the Schizosaccharomyces pombe Mad1:Mad2 complex. The Mad1 C-terminal “head” is required for checkpoint activity despite being dispensable for Mad1 and Mad2 kinetochore recruitment. Mad1 is not only the scaffold for presenting Mad2 at kinetochores, but its C-terminus

additionally promotes checkpoint signalling. Abstract The spindle assembly checkpoint inhibits anaphase until all chromosomes have become attached to the mitotic spindle. A complex between the checkpoint proteins Mad1 and Mad2 provides a platform for Mad2:Mad2 dimerization at unattached kinetochores, which enables Mad2 to delay anaphase. Here, we show that mutations selleck compound in Bub1 and within the Mad1 C-terminal domain impair the kinetochore localization of Mad1:Mad2 and abrogate checkpoint activity. Artificial kinetochore recruitment of Mad1 in these mutants co-recruits Mad2; however, the checkpoint remains non-functional. We identify specific mutations within the C-terminal head of Mad1 that impair checkpoint activity without affecting the kinetochore localization of Bub1, Mad1 or Mad2. Hence, Mad1 potentially in conjunction with Bub1 has a crucial role in checkpoint signalling in addition to presenting Mad2.