title: GTPases in bacterial cell polarity and signalling.
abstract: In bacteria, large G domain GTPases have well-established functions in translation, protein translocation, tRNA modification and ribosome assembly. In addition, bacteria also contain small Ras-like GTPases consisting of stand-alone G domains. Recent data have revealed that small Ras-like GTPases as well as large G domain GTPases in bacteria function in the regulation of cell polarity, signal transduction and possibly also in cell division. The small Ras-like GTPase MglA together with its cognate GAP MglB regulates cell polarity in Myxococcus xanthus, and the small Ras-like GTPase CvnD9 in Streptomyces coelicolor is involved in signal transduction. Similarly, the large GTPase FlhF together with the ATPase FlhG regulates the localization and number of flagella in polarly flagellated bacteria. Moreover, large dynamin-like GTPases in bacteria may function in cell division. Thus, the function of GTPases in bacteria may be as pervasive as in eukaryotes.
authors.affiliation: Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str. 10, 35043 Marburg, Germany.
authors.forename: Iryna
authors.initials: I
authors.lastname: Bulyha
authors.forename: Edina
authors.initials: E
authors.lastname: Hot
authors.forename: Stuart
authors.initials: S
authors.lastname: Huntley
authors.forename: Lotte
authors.initials: L
authors.lastname: Søgaard-Andersen
mesh_terms: D016764:Cell Polarity; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D008954:Models, Biological; D016941:Myxococcus xanthus / Q000201:enzymology* / Q000502:physiology*; D015398:Signal Transduction; D048372:Streptomyces coelicolor / Q000201:enzymology* / Q000502:physiology*
chemical_list: D020558:GTP Phosphohydrolases