Is the acid phosphatase of <i>Escherichia coli</i> with pH optimum of 2.5 a polyphosphate depolymerase?

Dassa, Elie; Boquet, P

doi:10.1016/0014-5793(81)80964-7

Cited by 25 publications

(9 citation statements)

References 17 publications

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“…The detection of pH 2.5 acid phosphatase activity on replica plates was as previously described (4,5), except that the time of incubation with PNPP in 1 M formic acid was reduced to 3 to 5 min for the detection of clones with multiple copies of the appA gene. The determination of the enzymatic specific activity in cells growing in liquid cultures was as described previously (3)(4)(5). Alkaline phosphatase specific activity in liquid cultures was measured by incubation of toluenized washed cells in 150 mM Tris hydrochloride (pH 8.8) containing PNPP (25 mM).…”

Section: Methodsmentioning

confidence: 99%

“…These enzymes can be distinguished from each other by their pH optima for activity and their substrate specificities (8,10,19,22,23,25). The periplasmic acid phosphoanhydride-phosphohydrolase (EC 3.6.1.11) referred to hereafter as acid phosphatase, is a monomeric protein of Mr 45,000 which is soluble in acid solutions (such as 1.5 M formic acid) and optimally active at pH 2.5 against inorganic polyphosphates, guanosine polyphosphates, and p-nitrophenyl phosphate (PNPP) (3,5,6). …”

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confidence: 99%

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Use of TnphoA to detect genes for exported proteins in Escherichia coli: identification of the plasmid-encoded gene for a periplasmic acid phosphatase

Boquet¹,

Manoil²,

Beckwith³

1987

J Bacteriol

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The structural gene (appA) for the periplasmic acid phosphatase (optimum pH 2.5) of Escherichia coli was cloned into a plasmid by using a combination of in vivo and in vitro techniques. The position and orientation of the appA gene within the cloned DNA fragment were identified by using fusions to the alkaline phosphatase gene (phoA) generated by Tn5 IS50L::phoA (TnphoA) insertions. For TnphoA-generated hybrid proteins to have high enzymatic activity, it appears that the phoA gene must be fused to a target gene coding for a signal which promotes protein export. The approach used to identify the appA gene thus appears to provide a simple general means of selectively identifying genes encoding membrane and secreted proteins.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

Use of TnphoA to detect genes for exported proteins in Escherichia coli: identification of the plasmid-encoded gene for a periplasmic acid phosphatase

Boquet¹,

Manoil²,

Beckwith³

1987

J Bacteriol

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“…This would explain why colicin E3 action requires energized cells (Jetten and Jetten, 1975). An acidic pH in this region might be expected since the presence of an acid phosphatase with an optimum pH of 2.5 has been found in the periplasmic space (Dassa and Boquet, 1981;Dassa et al, 1982). An alternative hypothesis would be that the fusion activity, expressed in vitro at acidic pH, could be expressed in vivo upon interaction with the outer membrane receptor.…”

Section: Resultsmentioning

confidence: 99%

pH-dependent membrane fusion is promoted by various colicins.

Pattus¹,

Cavard²,

Crozel³

et al. 1985

The EMBO Journal

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The ability of colicin A, a bacteriocin produced by some Enterobacteriaceae, to fuse phospholipid vesicles at acidic pH, was demonstrated by electron microscopy and resonance energy transfer. The fusion depends on protein concentration and on the nature of the phospholipids. Vesicles, prepared from Escherichia coli phospholipids, fused one or more rounds at pH 4.5 upon addition of stochiometric amounts of colicin A. Fusion was not only induced by pore-forming colicins (E1, K) but also by colicins that contain nuclease activities (E2, E3). By recombinant DNA technology it is shown that the first glycine-rich 70 NH2-terminal amino acids and, most probably, the extreme COOH-terminal end of colicin A are involved in the fusion activity of the protein. The physiological relevance of this property of colicins is discussed.

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“…The properties of condensed phosphates (including polyphosphate glasses) have been well-documented (Corbridge, 1990). The transport of polyphosphates across bacterial membranes has been studied extensively (Dassa and Boquet, 1981;Overbeeke and Lugtenberg, 1982;Bauer et al, 1989;Bauer et al, 1988;Rao and Torriani, 1990). The role of polyphosphates in the biology of organisms has been reviewed (Harold, 1996).…”

Section: Introductionmentioning

confidence: 99%

Phosphate Glass as a Phosphate Source in High Cell Density Escherichia coli Fermentations

Curless¹,

Baclaski²,

Sachdev³

1996

Biotechnol. Prog.

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Is the acid phosphatase of Escherichia coli with pH optimum of 2.5 a polyphosphate depolymerase?

Cited by 25 publications

References 17 publications

Use of TnphoA to detect genes for exported proteins in Escherichia coli: identification of the plasmid-encoded gene for a periplasmic acid phosphatase

Use of TnphoA to detect genes for exported proteins in Escherichia coli: identification of the plasmid-encoded gene for a periplasmic acid phosphatase

pH-dependent membrane fusion is promoted by various colicins.

Phosphate Glass as a Phosphate Source in High Cell Density Escherichia coli Fermentations

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