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Scher

Publications and source records attributed to Scher.

2 recordsLinked to original sources

Forest biodiversity benefits from warmer microclimate, but only in colder regions

The diversity of many forest-dwelling organisms depends on forest structure, but it remains unknown to which degree this is mediated by microclimatic temperature, and whether microclimatic buffering is universally beneficial for forest biodiversity. In 234 broad-leaved forest plots across nine climatically differing regions in Germany, we measured micro- and macroclimatic temperatures, canopy cover, and deadwood volume after experimental manipulations of forest structure through thinning operations and gap cuts. We surveyed 21 taxonomic groups, representing plants, bacteria, fungi, and animals, to assess how their diversity depended on the predictors. Multi-taxon diversity, and diversity of ten separate taxonomic groups, increased from closed to open canopies. Only necrophagous beetles were more diverse in closed stands. These effects of canopy cover on diversity were partly mediated by microclimatic temperatures. Thereby, diversity responses to microclimatic temperature depended on the macroclimatic context. In regions with colder summers, locally warmer microclimates in canopy gaps had strong positive effects on biodiversity, while these effects were not found in regions with warmer summers. Consequently, management strategies aimed at multi-taxon forest diversity conservation should be chosen based on the regional climate, favoring canopy gaps primarily in colder regions, and taking future climate warming into consideration.

ecology↗

ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR EVENTS OF VISION

Vision is initiated by the rhodopsin family of light-sensitive G protein-coupled receptors (GPCRs). A photon is absorbed by the 11-cis retinal chromophore of rhodopsin which isomerises within 200 femtoseconds to the all-trans conformation, thereby initiating the cellular signal transduction processes that ultimately lead to vision. However, the intramolecular mechanism by which the photoactivated retinal induces the activation events inside rhodopsin remains elusive. In this work, we use ultrafast time-resolved crystallography at room temperature to determine how an isomerised twisted all-trans retinal stores the photon energy required to initiate protein conformational changes associated with the formation of the G protein-binding signalling state. The distorted retinal at 1 ps time-delay of photoactivation has pulled away from half of its numerous interactions with its binding pocket, and the excess of the photon energy is released through an anisotropic protein breathing motion in the direction of the extracellular space. Strikingly, the very early structural motions in the protein side chains of rhodopsin appear in regions involved in later stages of the conserved Class A GPCR activation mechanism. Our work sheds light on the earliest stages of vision in vertebrates and points to fundamental aspects of the molecular mechanisms of agonist-mediated GPCR activation.

biochemistry↗