Plant trait and vegetation data along a 1314 m elevation gradient with fire history in Puna grasslands, Per\ufa

\ua9 2024. The Author(s). Alpine grassland vegetation supports globally important biodiversity and ecosystems that are increasingly threatened by climate warming and other environmental changes. Trait-based approaches can support understanding of vegetation responses to global change drivers and consequences for ecosystem functioning. In six sites along a 1314 m elevational gradient in Puna grasslands in the Peruvian Andes, we collected datasets on vascular plant composition, plant functional traits, biomass, ecosystem fluxes, and climate data over three years. The data were collected in the wet and dry season and from plots with different fire histories. We selected traits associated with plant resource use, growth, and life history strategies (leaf area, leaf dry/wet mass, leaf thickness, specific leaf area, leaf dry matter content, leaf C, N, P content, C and N isotopes). The trait dataset contains 3,665 plant records from 145 taxa, 54,036 trait measurements (increasing the trait data coverage of the regional flora by 420%) covering 14 traits and 121 plant taxa (ca. 40% of which have no previous publicly available trait data) across 33 families

Global shift in a key plant trait indicates a change in biosphere function

In the face of climate change, understanding the dynamic responses of vegetation is crucial for predicting shifts in biosphere functioning. Plant functional traits, particularly leaf mass per area (LMA), are critical links between plant metabolism, vegetation responses to climate change, and the broader exchanges of energy and matter within the biosphere. Despite their importance, a comprehensive, predictive understanding of traits and biosphere changes is hampered by spatial and temporal gaps in trait observations. Here, we introduce a novel remote sensing method for the global, continuous mapping of LMA and its historical shifts. Consistent with ecological theory predicting a widespread decrease in LMA with global warming, our findings reveal a global LMA reduction of 6.5-7.6 % between 1985 and 2019, primarily due to increasing temperatures. This decrease varies among biomes, with evergreen conifer and tropical forests showing the most significant declines. Due to LMA connections with carbon metabolism in ecosystems, a global decrease in LMA points to a quickening of the carbon cycle, including largely unexplored contributions to increased global photosynthesis in recent decades. Collectively, these results signal an ongoing widespread and profound transformation in the functioning of the biosphere resulting from climate-related changes in vegetation and its traits

Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins

The alanine-based peptide Ac-XX(A)(7)OO-NH(2), referred to as XAO (where X, A, and O denote diaminobutyric acid, alanine, and ornithine, respectively), has recently been proposed to possess a well defined polyproline II (P(II)) conformation at low temperatures. Based on the results of extensive NMR and CD investigations combined with theoretical calculations, reported here, we present evidence that, on the contrary, this peptide does not have any significant amount of organized P(II) structure but exists in an ensemble of conformations with a distorted bend in the N- and C-terminal regions. The conformational ensemble was obtained by molecular dynamics/simulated annealing calculations using the amber suite of programs with time-averaged distance and dihedral-angle restraints obtained from rotating-frame nuclear Overhauser effect (ROE) volumes and vicinal coupling constants (3)J(HNΗα), respectively. The computed ensemble-averaged radius of gyration R(g) (7.4 ± 1.0) Å is in excellent agreement with that measured by small-angle x-ray scattering (SAXS) whereas, if the XAO peptide were in the P(II) conformation, R(g) would be 11.6 Å. Depending on the pH, peptide concentration, and temperature, the CD spectra of XAO do or do not possess the maximum with positive ellipticity in the 217-nm region, which is characteristic of the P(II) structure, reflecting a shifting conformational equilibrium rather than an all-or-none transition. The “P(II) conformation” should, therefore, be considered as one of the accessible conformational states of individual amino acid residues in peptides and proteins rather than as a structure of most of the chain in the early stage of folding

Further Evidence for the Absence of Polyproline II Stretch in the XAO Peptide

It has been suggested that the alanine-based peptide with sequence Ac-XX-[A](7)-OO-NH(2), termed XAO where X denotes diaminobutyric acid and O denotes ornithine, exists in a predominantly polyproline-helix (P(II)) conformation in aqueous solution. In our recent work, we demonstrated that this “polyproline conformation” should be regarded as a set of local conformational states rather than as the overall conformation of the molecule. In this work, we present further evidence to support this statement. Differential scanning calorimetry measurements showed only a very small peak in the heat capacity of an aqueous solution of XAO at 57°C, whereas the suggested transition to the P(II) structure should occur at ∼30°C. We also demonstrate that the temperature dependence of the (3)J(HNHα) coupling constants of the alanine residues can be explained qualitatively in terms of Boltzmann averaging over all local conformational states; therefore, this temperature dependence proves that a conformational transition does not occur. Canonical MD simulations with the solvent represented by the generalized Born model, and with time-averaged NMR-derived restraints, demonstrate the presence of an ensemble of structures with a substantial amount of local P(II) conformational states but not with an overall P(II) conformation