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Amagai, Y.

Publications and source records attributed to Amagai, Y..

2 recordsLinked to original sources

SecSel, a new software tool for conservation prioritization that is applicable to ordinal-scale data for multiple biodiversity features

SecSel, a protected-area prioritization tool, has been developed to help design areas that efficiently protect multiple features, including conservation of biodiversity and use of ecosystem services. The prioritization by SecSel is based on evaluation of the local units of each feature. The evaluation metrics should be quantitative but need not be ratio scale. The minimum requirement of the input data is that they are ordinal. The conservation target is the number of local units with high values of each feature to be protected in the area. SecSel can handle conflicts among features, including conflicts between conservation and utilization of land or specific ecosystem functions. Before the selection procedure, one of a conflicting pair of features in a site is discarded. That decision is based on the dispensability of the local unit to fulfilling the conservation target of each feature. SecSel also considers the cost of including each site in the protected area and the compactness of the area in terms of total boundary length or the distance to the nearest site. To demonstrate the functionality of Secsel, we used it to design land use in an alpine region of northern Japan where conservation of alpine vegetation and its recreational use are important considerations.

ecology

A unique adhesive motif of protein disulfide isomerase P5 supports its function via dimerization

P5, also known as PDIA6, is a PDI-family member that plays an important role in the ER quality control. Herein, we revealed that P5 dimerizes via a unique adhesive motif contained in the N-terminal thioredoxin-like domain. This motif is apparently similar to, but radically different from conventional leucine-zipper motifs, in that the former includes a periodic repeat of leucine or valine residues at the third or fourth position spanning five helical turns on 15-residue anti-parallel -helices, unlike the latter of which the leucine residues appear every two helical turns on [~]30-residue parallel -helices at dimer interfaces. A monomeric P5 mutant with the impaired adhesive motif showed structural instability and local unfolding, and behaved as an aberrant protein that induces the ER stress response. Disassembly of P5 to monomers compromised its ability to inactivate IRE1 via reduction of intermolecular disulfide bonds and its Ca2+-dependent regulation of chaperone function in vitro. Thus, the leucine-valine adhesive motif supports structure and physiological function of P5.

biochemistry