{"id":11957,"date":"2017-11-10T14:51:41","date_gmt":"2017-11-10T22:51:41","guid":{"rendered":"https:\/\/www.darkenergybiosphere.org\/?post_type=publication&#038;p=11957"},"modified":"2017-11-10T14:51:41","modified_gmt":"2017-11-10T22:51:41","slug":"structure-function-and-evolution-of-the-hsp60-chaperonins","status":"publish","type":"publication","link":"https:\/\/www.darkenergybiosphere.org\/publication\/structure-function-and-evolution-of-the-hsp60-chaperonins\/","title":{"rendered":"Structure, Function and Evolution of the\u00a0Hsp60 Chaperonins"},"content":{"rendered":"<p id=\"Par1\" class=\"Para\">In 1973, Christian Anfinsen and coworkers noted that accelerated protein folding in intact cells and cell extracts suggested that a \u201cdisulfide interchange enzyme\u201d 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\u00a0<em class=\"EmphasisTypeItalic \">GroE<\/em>\u00a0mutants of\u00a0<em class=\"EmphasisTypeItalic \">E. coli<\/em>\u00a0failed to grow bacteriophage \u03bb 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 \u201cbuilt-in\u201d 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.<\/p>\n<p id=\"Par2\" class=\"Para\">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.<\/p>\n","protected":false},"template":"","tags":[],"publication_type":[16],"_links":{"self":[{"href":"https:\/\/www.darkenergybiosphere.org\/wp-json\/wp\/v2\/publication\/11957"}],"collection":[{"href":"https:\/\/www.darkenergybiosphere.org\/wp-json\/wp\/v2\/publication"}],"about":[{"href":"https:\/\/www.darkenergybiosphere.org\/wp-json\/wp\/v2\/types\/publication"}],"wp:attachment":[{"href":"https:\/\/www.darkenergybiosphere.org\/wp-json\/wp\/v2\/media?parent=11957"}],"wp:term":[{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.darkenergybiosphere.org\/wp-json\/wp\/v2\/tags?post=11957"},{"taxonomy":"publication_type","embeddable":true,"href":"https:\/\/www.darkenergybiosphere.org\/wp-json\/wp\/v2\/publication_type?post=11957"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}