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Polo, A.

Publications and source records attributed to Polo, A..

2 recordsLinked to original sources
bioRxiv2021

Soil respiration variation along an altitudinal gradient in Italian Alps: Disentangling forest structure and temperature effects

To understand the main determinants of soil respiration (SR), we investigated the changes of soil respiration and soil physicochemical properties, including soil carbon (C) and nitrogen (N), root C and N, litter C and N, soil bulk densities and soil pH at five forest sites, along an elevation/temperature gradient (404 to 2101 m a.s.l) in Northern Italy, where confounding factors such as aspect and soil parent material are minimized, but an ample variation in forest structure and composition is present. Our result indicated that SR rates increased with temperature in all sites, and about 55% - 76% of SR was explained by temperature. Annual cumulative SR, ranging between 0.65 and 1.40 kg C m-2 yr-1, declined along the elevation gradient, while temperature sensitivity (Q10) of SR increased with elevation. However, a high SR rate (1.27 kg C m-2 yr-1) and low Q10 were recorded in the old conifer forest stand at 1731 m a.s.l., characterized by a complex structure and high productivity, introducing nonlinearity in the relations with elevation and temperature. Reference SR at the temperature of 10{degrees}C (SRref) was not related to elevation. A significant linear negative relationship was found for bulk density with elevation. On the contrary, soil C, soil N, root C, root N, pH and litter mass were better fitted by nonlinear relations with elevation. However, it was not possible to confirm a significant correlation of SR with these parameters once the effect of temperature has been removed (SRref). These results show how the main factor affecting SR in forest ecosystems along this Alpine elevation gradient is temperature, but its regulating role can be strongly influenced by site biological characteristics, particularly vegetation type and structure. This study also confirms that high elevation sites are rich in C stored in the soil and also more sensitive to climate change, being prone to high carbon losses as CO2. Conversely, forest ecosystems with a complex structure, with high SRref and moderate Q10, can be more resilient.

ecology↗
bioRxiv2020

Kinetics characterization of ASXL1/2-mediated allosteric regulation of BAP1 deubiquitinase

BAP1 is a ubiquitin hydrolase whose deubiquitinase activity is mediated by polycomb group-like protein ASXL2. Cancer-related mutations/deletions of BAP1 lead to loss-of-function either by directly targeting the catalytic (UCH) or ULD domains of BAP1, the latter disrupts binding to ASXL2, an obligate partner for BAP1 enzymatic activity. However, the biochemical and biophysical properties of the domains involved in forming the enzymatically active complex are unknown. Here we investigate the molecular dynamics, kinetics and stoichiometry of these interactions. We demonstrate that the BAP1 and ASXL2 domain/proteins or protein complexes produced in either bacteria or baculovirus are structurally and functionally active. The interaction between BAP1 and ASXL2 is direct, specific, and stable to in vitro biochemical and biophysical manipulations as detected by isothermal titration calorimetry, GST association, and optical biosensor assays. Association of the ASXL2-AB box greatly stimulates BAP1 deubiquitinase activity. A stable ternary complex can be formed comprised of the BAP1-UCH, BAP1-ULD, and ASXL2-AB domains. Binding of the BAP1-ULD domain to the ASXL2-AB box is rapid, with fast association and slow dissociation rates. Stoichiometric analysis revealed that one molecule of the ULD domain directly interacts with one molecule of the AB Box. Real-time kinetics analysis of ULD/AB protein complex to the UCH domain of BAP1, based on SPR, indicated that formation of the ULD/AB complex with the UCH domain is a single-step event with fast association and slow dissociation rates. These structural and dynamic parameters implicate the possibility for future small-molecule approaches to reactivate latent wild-type UCH activity in BAP-mutant malignancies.

cancer biology↗