title: Bacterial cell division regulation by Ser/Thr kinases: a structural perspective.
abstract: Recent genetic, biochemical and structural studies have established that eukaryotic-like Ser/Thr protein-kinases are critical mediators of developmental changes and host pathogen interactions in bacteria. Although with lower abundance compared to their homologues from eukaryotes, Ser/Thr protein-kinases are widespread in gram-positive bacteria. These data underline a key role of reversible Ser/Thr phosphorylation in bacterial physiology and virulence. Numerous studies have revealed how phosphorylation/dephosphorylation of Ser/Thr protein-kinases governs cell division and cell wall biosynthesis and that Ser/Thr protein kinases are responsible for distinct phenotypes, dependent on different environmental signals. In this review we discuss the current understandings of Ser/Thr protein-kinases functional processes based on structural data.
authors.affiliation: Institute of Biostructure and Bioimaging, CNR, Via Mezzocannone, 16. I-80134, Napoli, Italy. alessia.ruggiero@unina.it
authors.forename: Alessia
authors.initials: A
authors.lastname: Ruggiero
authors.forename: Paola
authors.initials: P
authors.lastname: De Simone
authors.forename: Giovanni
authors.initials: G
authors.lastname: Smaldone
authors.forename: Flavia
authors.initials: F
authors.lastname: Squeglia
authors.forename: Rita
authors.initials: R
authors.lastname: Berisio
mesh_terms: D001419:Bacteria / Q000166:cytology* / Q000201:enzymology*; D002455:Cell Division; D004789:Enzyme Activation; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary
chemical_list: D010455:Peptides; D017346:Protein Serine-Threonine Kinases