The universally conserved prokaryotic GTPases.

TitleThe universally conserved prokaryotic GTPases.
Publication TypeJournal Article
Year of Publication2011
AuthorsVerstraeten, N., M. Fauvart, W. Versées, and J. Michiels
JournalMicrobiol Mol Biol Rev
Volume75
Issue3
Pagination507-42, second and third pages of table of contents
Date Published2011 Sep
ISSN1098-5557
KeywordsAmino Acid Sequence, Archaea, Bacteria, Conserved Sequence, GTP Phosphohydrolases, Intracellular Space, Molecular Sequence Data
Abstract

Members of the large superclass of P-loop GTPases share a core domain with a conserved three-dimensional structure. In eukaryotes, these proteins are implicated in various crucial cellular processes, including translation, membrane trafficking, cell cycle progression, and membrane signaling. As targets of mutation and toxins, GTPases are involved in the pathogenesis of cancer and infectious diseases. In prokaryotes also, it is hard to overestimate the importance of GTPases in cell physiology. Numerous papers have shed new light on the role of bacterial GTPases in cell cycle regulation, ribosome assembly, the stress response, and other cellular processes. Moreover, bacterial GTPases have been identified as high-potential drug targets. A key paper published over 2 decades ago stated that, "It may never again be possible to capture [GTPases] in a family portrait" (H. R. Bourne, D. A. Sanders, and F. McCormick, Nature 348:125-132, 1990) and indeed, the last 20 years have seen a tremendous increase in publications on the subject. Sequence analysis identified 13 bacterial GTPases that are conserved in at least 75% of all bacterial species. We here provide an overview of these 13 protein subfamilies, covering their cellular functions as well as cellular localization and expression levels, three-dimensional structures, biochemical properties, and gene organization. Conserved roles in eukaryotic homologs will be discussed as well. A comprehensive overview summarizing current knowledge on prokaryotic GTPases will aid in further elucidating the function of these important proteins.

DOI10.1128/MMBR.00009-11
Alternate JournalMicrobiol. Mol. Biol. Rev.
PubMed ID21885683
PubMed Central IDPMC3165542