Function of the universally conserved bacterial GTPases.
The GTPase superfamily of cellular regulators is well represented in bacteria. A small number are universally conserved over the entire range of bacterial species. Such a pervasive taxonomic distribution suggests that these enzymes play important roles in bacterial cellular systems. Recent advances have demonstrated that bacterial GTPases are important regulators of ribosome function, and important for the distribution of DNA to daughter cells following cell division. In addition, the atomic structure of a unique GTPase, EngA, has recently been established. Unlike any other GTPase, EngA contains tandem GTP-binding domains. This structural study suggests that the GTPase cycles of the domains are regulated differentially in a manner that remains to be elucidated.
Caldon
Catherine E
CE
School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia.
March
Paul E
PE
D001419:Bacteria / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics; D029968:Escherichia coli Proteins; D019143:Evolution, Molecular; D020558:GTP Phosphohydrolases / Q000235:genetics / Q000502:physiology*; D019204:GTP-Binding Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D008957:Models, Genetic; D020559:Monomeric GTP-Binding Proteins / Q000235:genetics / Q000502:physiology; D016601:RNA-Binding Proteins; D012270:Ribosomes / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C090542:Obg GTP-binding protein, Bacteria; D016601:RNA-Binding Proteins; C068027:era protein, E coli; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins; D020559:Monomeric GTP-Binding Proteins