title: The gene ygdP, associated with the invasiveness of Escherichia coli K1, designates a Nudix hydrolase, Orf176, active on adenosine (5')-pentaphospho-(5')-adenosine (Ap5A).
abstract: ygdP, a gene associated with the invasion of brain microvascular endothelial cells by Escherichia coli K1 (Badger, J. L., Wass, C. A., and Kim, K. S. (2000) Mol. Microbiol. 36, 174-182), the primary Gram-negative bacterium causing meningitis in newborns, has been cloned and expressed in E. coli. The protein, YgdP, was purified to near homogeneity and identified as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate pyrophosphatases. It catalyzes the hydrolysis of diadenosine tetra-, penta-, and hexa-phosphates with a preference for diadenosine penta-phosphate, from which it forms ATP and ADP. The enzyme has a requirement for a divalent metal cation that can be met with Mg2+, Zn2+, or Mn2+ and, like most of the Nudix hydrolases, has an alkaline pH optimum between 8.5 and 9. This is the second identification of a gene associated with the invasiveness of a human pathogen as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate pyrophosphatases, and an examination of homologous proteins in other invasive bacteria suggests that this may be a common feature of cellular invasion.
authors.affiliation: Department of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218, USA. zoot@jhu.edu
authors.forename: M J
authors.initials: MJ
authors.lastname: Bessman
authors.forename: J D
authors.initials: JD
authors.lastname: Walsh
authors.forename: C A
authors.initials: CA
authors.lastname: Dunn
authors.forename: J
authors.initials: J
authors.lastname: Swaminathan
authors.forename: J E
authors.initials: JE
authors.lastname: Weldon
authors.forename: J
authors.initials: J
authors.lastname: Shen
mesh_terms: D000595:Amino Acid Sequence; D015226:Dinucleoside Phosphates / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics* / Q000472:pathogenicity*; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D011755:Pyrophosphatases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014774:Virulence / Q000235:genetics*; D000096964:Nudix Hydrolases
chemical_list: D015226:Dinucleoside Phosphates; D011755:Pyrophosphatases; D000096964:Nudix Hydrolases; C012275:P(1),P(5)-di(adenosine-5'-)pentaphosphate