MODULAR MULTIDOMAIN PHOSPHORYL TRANSFER PROTEINS OF BACTERIA

Recent phylogenetic and structural analyses of multidomain phosphoryl transfer proteins of bacteria have revealed that interdomain (but not intradomain) splicing and fusion, as well as domain duplication and de letion, have occurred frequently during evolution. These events have b een found to be exceedingly rare in certain other protein families. Do main-shuffling events are illustrated by examples from the superfamili es of phosphoenolpyruvate-dependent sugar phosphotransferase systems, their transcriptional regulatory protein targets of phosphorylation, s ensor autokinase/response regulator signal transduction systems, and p ermeases of the ATP-binding-cassette type. (C) Current Biology Ltd.