Involvement of cyclic AMP and its receptor protein in filamentation of an Escherichia coli fic mutant

Abstract

Cyclic AMP (cAMP) inhibited septum formation in Escherichia coli PA3092 and induced cell filamentation at elevated temperatures. This phenomenon was first observed in E. coli PA3092 and is due to a temperature-sensitive mutation. We tentatively named this mutationfic (filamentation induced by cAMP). Thefic gene was located near rpsL (formerly strA) on the E. coli K-12 map. The inhibitory effect of cAMP on cell division and filamentation in afic mutant was not observed in a crp mutant. When cAMP was removed from the culture medium, filaments were divided into rods as the intracellular cAMP level decreased. These results suggest that the cAMP-cAMP receptor protein complex causes filamentation in the fic mutant, E. coli PA3092.Photography. Photographs were taken according to the method described previously (20).Chemicals. cAMP was purchased from Kohjin Co., Japan.[3H]cAMP was supplied by the Radiochemical Centre, Amersham, England. O-Nitrophenyl-p-D-galactopyranoside was obtained from Nakarai Chemicals Co., Japan. Isopropyl-thio-3-D-galactopyranoside was purchased from the Sigma Chemical Co., St. Louis, Mo. RESULTSIsolation and identification of crp mutant of E. coli PA3092. It was shown that cell division of E. coli PA3092 was completely inhibited at 43°C in 807 on July 31, 2020 by guest

Cyclic AMP in prokaryotes.

“…Kumar et al (186,187) have presented evidence that expression of thefts gene, which codes for a protein localized to the inner membrane and involved in the process of cellular division (249), requires cAMP. In cultures growing with synchronized division, a cya lacZ fusion was expressed during cell elongation but not during cell division, suggesting that cya promoter activity and cell division are coupled (315,316,318). Synchronously dividing cells containing a cAMP-independent lacUV5 cya fusion and induced by the addition of isopropyl-,-D-thiogalactopyranoside (IPTG) demonstrated a two-to threefold increase in cAMP levels, ceased division, and grew as filaments during the time when cAMP production was elevated.…”

Purification and crystallization of Phd, the antitoxin of thephd/docoperon

“…Members of this family of TA modules have since been identified in the genomes of both Gram-positive and Gram-negative bacteria. The 126-amino-acid toxin Doc is similar to Fic (Garcia-Pino, Christensen-Dalsgaard et al, 2008), a protein that has been implicated in regulation of cell division in E. coli (Utsumi et al, 1982). Fic domains are found in both prokaryotes and eukaryotes and have recently been shown to catalyze ATP-mediated AMPylation of a conserved tyrosine residue in the switch I region of Rho GTPases (Worby et al, 2009).…”

Stationary phase-specific expression of the fic gene in Escherichia coli K-12 is controlled by the rpoS gene product (σ38)

“…The tic gene is close to pabA, located at 75 rain of the Escherichia coli chromosome and was previously identified as the regulatory factor of cell division [1,2]. The pabA gene is found at 30 bp downstream from tic.…”