title: Role of eukaryotic-like serine/threonine kinases in bacterial cell division and morphogenesis.
abstract: Bacteria possess a repertoire of versatile protein kinases modulating diverse aspects of their physiology by phosphorylating proteins on various amino acids including histidine, cysteine, aspartic acid, arginine, serine, threonine and tyrosine. One class of membrane serine/threonine protein kinases possesses a catalytic domain sharing a common fold with eukaryotic protein kinases and an extracellular mosaic domain found in bacteria only, named PASTA for 'Penicillin binding proteins And Serine/Threonine kinase Associated'. Over the last decade, evidence has been accumulating that these protein kinases are involved in cell division, morphogenesis and developmental processes in Firmicutes and Actinobacteria. However, observations differ from one species to another suggesting that a general mechanism of activation of their kinase activity is unlikely and that species-specific regulation of cell division is at play. In this review, we survey the latest research on the structural aspects and the cellular functions of bacterial serine/threonine kinases with PASTA motifs to illustrate the diversity of the regulatory mechanisms controlling bacterial cell division and morphogenesis.
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, 7 passage du Vercors, 69367 Lyon Cedex 07, France.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Manuse
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, 7 passage du Vercors, 69367 Lyon Cedex 07, France.
authors.forename: Aurore
authors.initials: A
authors.lastname: Fleurie
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, 7 passage du Vercors, 69367 Lyon Cedex 07, France.
authors.forename: Laure
authors.initials: L
authors.lastname: Zucchini
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, 7 passage du Vercors, 69367 Lyon Cedex 07, France.
authors.forename: Christian
authors.initials: C
authors.lastname: Lesterlin
authors.affiliation: Bases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Université Lyon 1, CNRS, UMR 5086, 7 passage du Vercors, 69367 Lyon Cedex 07, France c.grangeasse@ibcp.fr.
authors.forename: Christophe
authors.initials: C
authors.lastname: Grangeasse
mesh_terms: D039903:Actinobacteria / Q000166:cytology / Q000201:enzymology; D020816:Amino Acid Motifs; D001419:Bacteria / Q000166:cytology*; D001426:Bacterial Proteins / Q000378:metabolism*; D002455:Cell Division; D000068536:Bacillota / Q000166:cytology / Q000201:enzymology; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D017346:Protein Serine-Threonine Kinases
keywords: PASTA motifs; actinobacteria; bacterial cell division and morphogenesis; firmicutes; protein kinase; protein phosphorylation