A catalytically dead paralog activates its cognate enzyme through an allosteric mechanism that combined structural and phylogenomic analysis indicates arose through acquisition of a dimerization domain, suggesting a general model for how complex allostery evolves.
An integrated biochemical and evolutionary analysis shows how enzyme specificity evolves after gene loss during genome decay, implicating relaxation of purifying selection as a driving force for functional divergence.
Comparative -omic analyses of five knockout mouse strains with disrupted mitochondrial DNA expression at different levels provide a high quality resource of altered gene expression patterns that reveal several common secondary patophysiological changes of mitochondrial dysfunction.
The correct enzymatic activity of a previously misnamed enzyme is defined, placing the enzyme upstream of LARGE in building functional O-mannose structures on α-dystroglycan that are disrupted in multiple forms of congenital muscular dystrophy.
Structural models of the chromatin remodeling enzyme Chd1 in solution and when bound to chromatin indicate that conformational changes to both the enzyme and the nucleosome occur upon nucleotide dependent engagement.