AbstractOrganic matter degradation and preservation play a key role in global biogeochemical cycles and climate. The degradation of OM generally proceeds via multiple enzymatic reactions involving millions of different organisms, billions of organic compounds, and a number of different oxidants, as well as intermediate compounds. As a result, OM degradation and preservation is controlled by a dynamic and complex interplay of different environmental factors. Attempts to isolate the impact of a single variable on the rate of OM degradation have often led to contradictory results. It is therefore becoming increasingly clear that OM degradability is not an intrinsic property of the organic matter itself but an ecosystem property. Correspondingly, the likelihood that a given organic compound will be degraded by a microbial community or be preserved will depend on the chemical formula and structure of that compound, in addition to the metabolic capabilities of the resident microorganisms in response to environmental factors such as electron acceptor and intermediate metabolite concentrations, temperature, and physical associations with minerals or other organic compounds.
In 1973, Christian Anfinsen and coworkers noted that accelerated protein folding in intact cells and cell extracts suggested that a “disulfide interchange enzyme” might be present in vivo. This concept of catalyzed folding foreshadowed the discovery of ubiquitous protein chaperones. The chaperonin GroEL/GroES was identified serendipitously when GroE mutants of E. coli failed to grow bacteriophage λ and were also temperature sensitive. The GroEL/GroES proved to be a ubiquitous chaperone and heat shock protein in bacteria and eukaryotic organelles, with two back-to-back rings of seven subunits each, forming a cavity that enclosed nonnative proteins, capped by the separate GroES lid complex. Group II chaperonins were subsequently discovered in all of the Archaea and in the Eukaryote cytoplasm with a similar cage-like shape, only with a “built-in” lid instead of the GroES module of Group I chaperonins. These chaperones have been intensely studied for three decades and have provided deep insights into protein-folding mechanisms. Despite this, some aspects of chaperonin-induced protein folding remain controversial.
The shared architecture and sequence similarity of two classes of chaperonins implies that they share a common ancestor. A recently identified, deeply branching clade of archaeal-like chaperonins encoded in bacteria may shed light on the early history of chaperonins. This clade shares many molecular properties with Group II chaperones; however, their phylogeny suggests that they arose early in prokaryotic evolution and may represent a vestige of the common ancestor of Group I and Group II chaperonins.