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In Arabidopsis leaves, the catalytic C-terminal region of STARCH SYNTHASE 4 promotes starch granule initiation while its noncatalytic N-terminal region determines starch granules morphology.

Forage legumes have a relatively high biomass yield and crude protein content, but their grazed and harvested biomass lacks the high-energy carbohydrates required to meet the productivity potential of modern livestock breeds. Because of their low carbohydrate content, forage legume diets are typically supplemented with starch rich cereal grains or maize (Zea mays), leading to the disruption of local nutrient cycles. Although plant leaves were first reported to accumulate starch in a diurnal pattern over a century ago, leaf starch content has yet to be exploited as an agronomic trait in forage crops. Forage legumes such as red clover (Trifolium pratense) have the genetic potential to accumulate up to one third of their leaf dry mass as starch, but this starch is typically degraded at night to support nighttime growth and respiration. Even when diurnal accumulation is considered with regard to the time the crop is harvested, only limited gains are realized due to environmental effects and post-harvest losses from respiration. Here we present original data for starch metabolism in red clover and place it in the broader context of other forage legumes such as, white clover (T. repens), and alfalfa (Medicago sativa). We review the application of recent advances in molecular breeding, plant biology, and crop phenotyping, to forage legumes to improve and exploit a potentially valuable trait for sustainable ruminant livestock production., Agronomy, 7 (1), ISSN:2073-4395

Photosynthesis is a unique process that allows independent colonization of the land by plants and of the oceans by phytoplankton. Although the photosynthesis process is well understood in plants, we are still unlocking the mechanisms evolved by phytoplankton to achieve extremely efficient photosynthesis. Here, we combine biochemical, structural and in vivo physiological studies to unravel the structure of the plastid in diatoms, prominent marine eukaryotes. Biochemical and immunolocalization analyses reveal segregation of photosynthetic complexes in the loosely stacked thylakoid membranes typical of diatoms. Separation of photosystems within subdomains minimizes their physical contacts, as required for improved light utilization. Chloroplast 3D reconstruction and in vivo spectroscopy show that these subdomains are interconnected, ensuring fast equilibration of electron carriers for efficient optimum photosynthesis. Thus, diatoms and plants have converged towards a similar functional distribution of the photosystems although via different thylakoid architectures, which likely evolved independently in the land and the ocean., Phytoplankton and plant plastids have distinct evolutionary origins and membrane organization. Here Flori et al. show that diatom photosynthetic complexes spatially segregate into interconnected subdomains within loose thylakoid stacks enabling fast diffusion of electron carriers and efficient photosynthesis

Isoamylase-type debranching enzymes (ISAs) play an important role in determining starch structure. Amylopectin – a branched polymer of glucose – is the major component of starch granules and its architecture underlies the semi-crystalline nature of starch. Mutants of several species lacking the ISA1-subclass of isoamylase are impaired in amylopectin synthesis. Consequently, starch levels are decreased and an aberrant soluble glucan (phytoglycogen) with altered branch lengths and branching pattern accumulates. Here we use TAP (tandem affinity purification) tagging to provide direct evidence in Arabidopsis that ISA1 interacts with its homolog ISA2. No evidence for interaction with other starch biosynthetic enzymes was found. Analysis of the single mutants shows that each protein is destabilised in the absence of the other. Co-expression of both ISA1 and ISA2 Escherichia coli allowed the formation of the active recombinant enzyme and we show using site-directed mutagenesis that ISA1 is the catalytic subunit. The presence of the active isoamylase alters glycogen biosynthesis in E. coli, resulting in colonies that stain more starch-like with iodine. However, analysis of the glucans reveals that rather than producing an amylopectin like substance, cells expressing the active isoamylase still accumulate small amounts of glycogen together with a population of linear oligosaccharides that stain strongly with iodine. We conclude that for isoamylase to promote amylopectin synthesis it needs to act on a specific precursor (pre-amylopectin) generated by the combined actions of plant starch synthase and branching enzyme isoforms and when presented with an unsuitable substrate (i.e. E. coli glycogen) it simply degrades it., PLoS ONE, 8 (9), ISSN:1932-6203