Diadenosine 5′,5′′′‐P1,P4‐tetraphosphate (Ap4A) controls the timing of cell division in Escherichia coli

Abstract

Background: The timing of the cell division in Escherichia coli is highly regulated, but its mechanism has not been identified. Previously we have found that the cfcA1 mutation uncouples DNA replication and cell division and elevates the frequency of cell division. We further analysed the structure and the role of the cfc genes of cfcA11, a derivative of cfcA1, and another cfc mutant, cfcB1.

Di-Adenosine Tetraphosphate (Ap4A) Metabolism Impacts Biofilm Formation byPseudomonas fluorescensvia Modulation of c-di-GMP-Dependent Pathways

“…In E. coli, mutations in apaH and the associated increases in the level of Ap4A have a broad range of phenotypic consequences. For example, E. coli apaH mutants are nonmotile, are more sensitive to heat or oxidative stress, and are defective for catabolite repression and timing of cell division (10,28). Although the product of the P. fluorescens apaH homologue has enzymatic activities similar to those of the E. coli protein, we wanted to assess the degree to which the apaH mutant phenotypes are also conserved.…”

Isothermal Titration Calorimetry Reveals a Zinc Ion as an Atomic Switch in the Diadenosine Polyphosphates

“…The younger field of extracellular functioning has arguably proved more successful in defining a role for the diadenosine polyphosphates (2), for in spite of their intracellular ubiquity, definitive proof of physiological roles remains elusive, although many such roles have been proposed. The range of roles in which intracellular diadenosine polyphosphates have been implicated includes the control of the proliferative status of mammalian cells (3), prokaryotic stress (4,5), DNA repair (6), the timing of cell division (7), and as substrates of the tumor suppressor fragile histidine triad protein (EC 3.6.1.29) (8). Extracellularly, they have been shown as important signaling molecules (9,10), inducers of nitric oxide release (11), important neurotransmitters (12), and as vasocontrollers (13).…”

The pnhA Gene of Pasteurella multocida Encodes a Dinucleoside Oligophosphate Pyrophosphatase Member of the Nudix Hydrolase Superfamily

“…4A to C). Based on the work of Nishimura and colleagues (38,39), the difference in cell size between wild-type P. multocida and ACP13 may be due to an increase in the concentration of dinucleoside oligophosphates within the cells, resulting from the lack of a functional PnhA protein. Small-cell morphology was observed in an E. coli Nudix hydrolase mutant that contained a 100-fold increase of Ap 4 A, which in turn was thought to trigger the initiation of early cell division and subsequently result in a small cell size (38).…”

“…Based on the work of Nishimura and colleagues (38,39), the difference in cell size between wild-type P. multocida and ACP13 may be due to an increase in the concentration of dinucleoside oligophosphates within the cells, resulting from the lack of a functional PnhA protein. Small-cell morphology was observed in an E. coli Nudix hydrolase mutant that contained a 100-fold increase of Ap 4 A, which in turn was thought to trigger the initiation of early cell division and subsequently result in a small cell size (38). High concentrations of dinucleoside oligophosphates in both prokaryotic and eukaryotic cells have been linked to a number of physiological effects, such as inhibition of ATPsensitive K ϩ channels (31), induction of cell apoptosis and cell differentiation (46), and inhibition of adenylate kinase activity (33).…”

“…The role of the Nudix hydrolase is to remove the excess amounts of these molecules to restore cellular balance. In Escherichia coli, an increased concentration of dinucleoside oligophosphates, such as adenosine (5Ј)-tetraphospho-(5Ј)-adenosine (Ap 4 A), is proposed to be a signal for cell division (38,39) and to be involved in the stress responses by modulating protein refolding by chaperone proteins (21,30).…”