The development of a classification system for inland aquatic ecosystems in South Africa

A classification system is described that was developed for inland aquatic ecosystems in South Africa, including wetlands. The six-tiered classification system is based on a top-down, hierarchical  classification of aquatic ecosystems, following the functionally-oriented hydrogeomorphic (HGM)  approach to classification but incorporating structural attributes at the lower levels of the hierarchy. At Level 1, a distinction is made between inland, estuarine and shallow marine systems using the degree of connectivity to the open ocean as the key discriminator. Inland systems are characterised by the  complete absence of marine exchange and/or tidal influence. At Level 2, inland systems are grouped according to the most appropriate spatial framework for the particular application. At Level 3, four  primary Landscape Units are distinguished (Valley floor, Slope, Plain, Bench) on the basis of the  topographic position within which a particular inland aquatic ecosystem is situated, in recognition of the influence that the landscape setting has over hydrological and hydrodynamic processes acting within an aquatic ecosystem. Level 4 identifies HGM Units, defined primarily according to landform, hydrological characteristics and hydrodynamics. The following primary HGM Units (or HGM Types), which represent the main units of analysis for the classification system, are distinguished at Level 4A: (1) River; (2) Floodplain Wetland; (3) Channelled Valley-Bottom Wetland; (4) Unchannelled Valley-Bottom Wetland; (5) Depression; (6) Seep; (7) Wetland Flat. Secondary discriminators are applied at Level 5 to classify the hydrological regime of an HGM Unit, and Descriptors at Level 6 to categorise a range of biophysical attributes. The HGM Unit at Level 4 and the Hydrological Regime at Level 5 together constitute a Functional Unit, which represents the focal point of the classification system. The utility of the  classification system is ultimately dependent on the level to which ecosystem units are classified, which is in turn constrained by the type and extent of information available.Keywords: freshwater ecosystems, hydrogeomorphic (HGM) units, inland water ecosystems,  wetlands, wetland classification syste

How Protein Stability and New Functions Trade Off

Numerous studies have noted that the evolution of new enzymatic specificities is accompanied by loss of the protein's thermodynamic stability (ΔΔG), thus suggesting a tradeoff between the acquisition of new enzymatic functions and stability. However, since most mutations are destabilizing (ΔΔG>0), one should ask how destabilizing mutations that confer new or altered enzymatic functions relative to all other mutations are. We applied ΔΔG computations by FoldX to analyze the effects of 548 mutations that arose from the directed evolution of 22 different enzymes. The stability effects, location, and type of function-altering mutations were compared to ΔΔG changes arising from all possible point mutations in the same enzymes. We found that mutations that modulate enzymatic functions are mostly destabilizing (average ΔΔG = +0.9 kcal/mol), and are almost as destabilizing as the “average” mutation in these enzymes (+1.3 kcal/mol). Although their stability effects are not as dramatic as in key catalytic residues, mutations that modify the substrate binding pockets, and thus mediate new enzymatic specificities, place a larger stability burden than surface mutations that underline neutral, non-adaptive evolutionary changes. How are the destabilizing effects of functional mutations balanced to enable adaptation? Our analysis also indicated that many mutations that appear in directed evolution variants with no obvious role in the new function exert stabilizing effects that may compensate for the destabilizing effects of the crucial function-altering mutations. Thus, the evolution of new enzymatic activities, both in nature and in the laboratory, is dependent on the compensatory, stabilizing effect of apparently “silent” mutations in regions of the protein that are irrelevant to its function