Surface velocity and mass balance of Livingston Island ice cap, Antarctica

The mass budget of the ice caps surrounding the Antarctica Peninsula and, in particular, the partitioning of its main components are poorly known. Here we approximate frontal ablation (i.e. the sum of mass losses by calving and submarine melt) and surface mass balance of the ice cap of Livingston Island, the second largest island in the South Shetland Islands archipelago, and analyse variations in surface velocity for the period 2007–2011. Velocities are obtained from feature tracking using 25 PALSAR-1 images, and used in conjunction with estimates of glacier ice thicknesses inferred from principles of glacier dynamics and ground-penetrating radar observations to estimate frontal ablation rates by a flux-gate approach. Glacier-wide surface mass-balance rates are approximated from in situ observations on two glaciers of the ice cap. Within the limitations of the large uncertainties mostly due to unknown ice thicknesses at the flux gates, we find that frontal ablation (−509 ± 263 Mt yr−1, equivalent to −0.73 ± 0.38 m w.e. yr−1 over the ice cap area of 697 km2) and surface ablation (−0.73 ± 0.10 m w.e. yr−1) contribute similar shares to total ablation (−1.46 ± 0.39 m w.e. yr−1). Total mass change (δM = −0.67 ± 0.40 m w.e. yr−1) is negative despite a slightly positive surface mass balance (0.06 ± 0.14 m w.e. yr−1). We find large interannual and, for some basins, pronounced seasonal variations in surface velocities at the flux gates, with higher velocities in summer than in winter. Associated variations in frontal ablation (of ~237 Mt yr−1; −0.34 m w.e. yr−1) highlight the importance of taking into account the seasonality in ice velocities when computing frontal ablation with a flux-gate approach.

Estimating the effect of nitrogen fertilizer on the greenhouse gas balance of soils in Wales under current and future climate

This work was supported by a Grant from the Welsh Government (Glastir Monitoring and Evaluation Project—GMEP).

Differences in the oxidative balance of dispersing and non-dispersing individuals : an experimental approach in a passerine bird

Funding This work was supported by grants from the French Ministry of Research (PhD fellowship to CR), the University of Aberdeen (stipend to CR), the CNRS (PICS grant to BD), the L’Oréal Foundation-UNESCO “For Women in Science” program (fellowship to CR), the Région Rhône-Alpes (student mobility grant CMIRA Explora’doc to CR), the Rectors’ Conference of the Swiss Universities (mobility grant to CR), the Fédération de Recherche 41 BioEnvironnement et Santé (training grant to CR), and the Journal of Experimental Biology (travel grant to CR).

The Balance of RanBP1 and RCC1 Is Critical for Nuclear Assembly and Nuclear Transport

Ran is a small GTPase that is essential for nuclear transport, mRNA processing, maintenance of structural integrity of nuclei, and cell cycle control. RanBP1 is a highly conserved Ran guanine nucleotide dissociation inhibitor. We sought to use Xenopus egg extracts for the development of an in vitro assay for RanBP1 activity in nuclear assembly, protein import, and DNA replication. Surprisingly, when we used anti-RanBP1 antibodies to immunodeplete RanBP1 from Xenopus egg extracts, we found that the extracts were also depleted of RCC1, Ran’s guanine nucleotide exchange factor, suggesting that these proteins form a stable complex. In contrast to previous observations using extracts that had been depleted of RCC1 only, extracts lacking both RanBP1 and RCC1 (codepleted extracts) did not exhibit defects in assays of nuclear assembly, nuclear transport, or DNA replication. Addition of either recombinant RanBP1 or RCC1 to codepleted extracts to restore only one of the depleted proteins caused abnormal nuclear assembly and inhibited nuclear transport and DNA replication in a manner that could be rescued by further addition of RCC1 or RanBP1, respectively. Exogenous mutant Ran proteins could partially rescue nuclear function in extracts without RanBP1 or without RCC1, in a manner that was correlated with their nucleotide binding state. These results suggest that little RanBP1 or RCC1 is required for nuclear assembly, nuclear import, or DNA replication in the absence of the other protein. The results further suggest that the balance of GTP- and GDP-Ran is critical for proper nuclear assembly and function in vitro.