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Larsen, E. K.

Publications and source records attributed to Larsen, E. K..

3 recordsLinked to original sources

The ideotype for drought tolerance in bioenergy Populus nigra

Fast-growing perennial trees such as Populus nigra L. are important species for wood, plywood, pulp, and bioenergy feedstock production, yet tree vigor in a changing climate is poorly understood. This research aimed to identify breeding targets for yield in water-limited environments, alongside unraveling the relationship between drought, yield, and glucose release in P. nigra. A diversity panel of 20 P. nigra genotypes, selected from a wide natural association population, was grown at three divergent European sites. Through extensive phenotyping of physiological and morphological productivity and water-use traits, under irrigated conditions and when exposed to a progressive drought, we elucidated the adaptive and plastic drivers underlying tree productivity. We have identified the underpinning traits for drought tolerance, whereby high yields can be maintained under water deficit, in this key species. This highlighted the importance of examining the yield stress index (YSI) over the drought resistance index (DRI) to assess genotypes for performance under moderate drought. In this way, we found genotypes with high hydraulic capacity, and large leaves made up of many cells to be best suited to multiple European environments, with contrasting water availability. Moreover, we identified genotypes that combine yield and water use efficiency, with good glucose release potential, which will be important traits for the future of poplar as a bioenergy crop. Vigorous poplar genotypes, which are adapted to wet climates showed high environmental plasticity. However, in European drought scenarios, these trees outperform drought resistant genotypes, and some exhibit good glucose release. These trees are a valuable resource for the future.

plant biology↗

A Kink in DWORF Helical Structure Controls the Activation of the Sarco-plasmic Reticulum Ca2+-ATPase

The sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) is a P-type ATPase embedded in the sarcoplasmic reticulum. For each enzymatic cycle, SERCA transports 2 Ca2+ ions per ATP hydrolyzed in exchange for 2 to 3 H+ ions. SERCA is responsible for approximately 70% of Ca2+ transport and plays a central role in muscle relaxation. SERCAs function is regulated by endogenous regulins, single-pass membrane proteins that bind the ATPase within the membrane. While most of the regulins, such as phospholamban and sarcolipin, inhibit SERCAs activity, a newly discovered protein DWarf Open Reading Frame (DWORF) has a unique activating effect. DWORF is a 3.8 kDa bitopic membrane protein expressed in cardiac muscle. In this work, we determine the structure, topology, and per-residue lipid interactions of DWORF in lipid bilayers using a combination of high-resolution oriented sample solid-state NMR (OS-ssNMR) spectroscopy and refinement by replica-averaged orientationally-restrained molecular dynamics (RAOR-MD). We found that DWORFs structural topology consists of a dynamic N-terminal domain, an amphipathic juxtamembrane helix that crosses the lipid groups at an angle of 64{degrees} and a transmembrane (TM) C-terminal helix with an angle of 32{degrees}. A kink induced by Pro15, unique to DWORF, separated the two helical domains. A single Pro15Ala mutant significantly decreases the kink and eliminates DWORFs activating effect on SERCA. Overall, our findings directly link DWORFs structural topology to its unique activating effect on SERCA.

biophysics↗

A Bitopic Miniprotein Regulates a Membrane-Embedded Enzyme via Topological Allostery

Phospholamban (PLN) is a mini-membrane protein that directly controls the cardiac Ca2+-transport response to {beta}-adrenergic stimulation, thus modulating cardiac output during the fight- or-flight response. In the sarcoplasmic reticulum membrane, PLN binds to the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA), keeping this enzymes function within a narrow physiological window. PLN phosphorylation by cAMP-dependent protein kinase A or increase in Ca2+ concentration reverses the inhibitory effects through an unknown mechanism. Using oriented-sample solid-state NMR spectroscopy and replica-averaged NMR-restrained structural refinement, we reveal that phosphorylation of PLNs cytoplasmic regulatory domain signals the disruption of several inhibitory contacts at the transmembrane binding interface of the SERCA-PLN complex that are propagated to the enzymes active site, augmenting Ca2+ transport. Our findings address long-standing questions about SERCA regulation, epitomizing a signal transduction mechanism operated by posttranslationally-modified bitopic membrane proteins.

biophysics↗