title: Elevated guanosine 5'-diphosphate 3'-diphosphate level inhibits bacterial growth and interferes with FtsZ assembly.
abstract: FtsZ, a protein essential for prokaryotic cell division, forms a ring structure known as the Z-ring at the division site. FtsZ has a GTP binding site and is assembled into linear structures in a GTP-dependent manner in vitro. We assessed whether guanosine 5'-diphosphate 3'-diphosphate (ppGpp), a global regulator of gene expression in starved bacteria, affects cell division in Salmonella Paratyphi A. Elevation of intracellular ppGpp levels by using the relA expression vector induced repression of bacterial growth and incorrect FtsZ assembly. We found that FtsZ forms helical structures in the presence of ppGpp by using the GTP binding site; however, ppGpp levels required to form helical structures were at least 20-fold higher than the required GTP levels in vitro. Furthermore, once formed, helical structures did not change to the straight form even after GTP addition. Our data indicate that elevation of the ppGpp level leads to inhibition of bacterial growth and interferes with FtsZ assembly.
authors.affiliation: Department of Bacteriology, Faculty of Medical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan yama_guts@yahoo.co.jp.
authors.forename: Takayoshi
authors.initials: T
authors.lastname: Yamaguchi
authors.affiliation: Department of Bacteriology, Faculty of Medical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan.
authors.forename: Ken-Ichiro
authors.initials: K
authors.lastname: Iida
authors.affiliation: Department of Oral Health, Growth and Development, Division of Oral Infectious Diseases and Immunology, Faculty of Dental Science, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan.
authors.forename: Susumu
authors.initials: S
authors.lastname: Shiota
authors.affiliation: Department of Bacteriology, Faculty of Medical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan.
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Nakayama
authors.affiliation: Department of Bacteriology, Faculty of Medical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan.
authors.forename: Shin-Ichi
authors.initials: S
authors.lastname: Yoshida
mesh_terms: D001089:Arabinose / Q000494:pharmacology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001665:Binding Sites; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D005822:Genetic Vectors; D006159:Guanosine Tetraphosphate / Q000235:genetics / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D011485:Protein Binding; D012482:Salmonella paratyphi A / Q000187:drug effects / Q000235:genetics / Q000254:growth & development* / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D006159:Guanosine Tetraphosphate; D006160:Guanosine Triphosphate; D001089:Arabinose
keywords: FtsZ assembly; guanosine 5′-diphosphate 3′-diphosphate; starved condition