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Burroughs, N. J.

Publications and source records attributed to Burroughs, N. J..

2 recordsLinked to original sources

Spatial photosynthesis modelling sets guidelines to constructing a viable single-cell cytoplasm-to-stroma C4 cycle

It has been proposed that introducing C4 photosynthesis into C3 crops would increase yield. The simplest scheme in- volves concentrating carbon originating from the cytosol in the chloroplast stroma of mesophyll cells without altering leaf or cell anatomy. Photosynthetic efficiency would then strongly depend on the chloroplast envelope permeability to CO2. We examine the performance of this C4 cycle with a spatial model of carbon assimilation in C3 mesophyll cell geometry, conducting a thorough exploration of parameter space relevant to C4 photosynthesis. For envelope perme- abilities below 300 {micro}m/s C4 photosynthesis has a higher quantum efficiency than C3. However, even when envelope permeability is above this threshold, the C4 pathway can provide a substantial boost to carbon assimilation with only a moderate decrease in efficiency. Depending on the available light-harvesting capacity of plastids, C4 photosynthesis could boost carbon assimilation anywhere from 20% to 100%. Gains are even more prominent under CO2 deprivation, and can be achieved in conjunction with lower investment in plastids if chloroplast surface coverage is also altered. A C4 pathway operating within individual mesophyll cells of C3 plants could hence lead to higher growth rates and better drought resistance in dry, high-sunlight climates.

plant biology

Structural-mechanical remodelling of GDP-microtubules by kinesin

Kinesin-1 is a nanoscale molecular motor that walks towards the fast growing (plus) ends of microtubules (MTs), hauling molecular cargo to specific reaction sites in cells. Kinesin-driven transport is central to the self-organisation of eukaryotic cells and shows great promise as a tool for nano-engineering1,2. Recent work hints that kinesin may also play a role in modulating the stability of its MT track, both in vitro3-5 and in vivo6, but results are conflicting7-9 and mechanisms are unclear. Here we report a new dimension to the kinesin-MT interaction, whereby strong-state (ATP-bound and apo) kinesin-1 motor domains inhibit the shrinkage of GDP-MTs by up to 2 orders of magnitude and expand their lattice spacing by ~1.6%. Our data reveal an unexpected new mechanism by which the mechanochemical cycles of kinesin and tubulin interlock, allowing motile kinesins to influence the structure, stability and mechanics of their MT track.

biophysics