Search PubMedSearch

PubMed · 6202676

Amplification of the Streptococcus faecalis proton-translocating ATPase by a decrease in cytoplasmic pH.

Abstract

When Streptococcus faecalis was grown in the presence of protonophores , an ATPase activity of the membrane was increased at a pH below 8.0 but not at a pH above 8.0. Characteristics of this increased ATPase were identical to those of a proton-translocating ATPase (H+-ATPase) located on the membrane of normal cells. The cytoplasmic pH was regulated at 7.6 to 7.8 but was not regulated in the presence of protonophores . The increase in the H+-ATPase was observed when the cytoplasmic pH was lowered to less than 7.6 by the addition of protonophores and was not related to the dissipation of the proton motive force. Thus, we suggest that the H+-ATPase of the membrane is amplified when the cytoplasmic pH is lowered below the pH at which it is regulated under normal conditions.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

H Kobayashi, T Suzuki, N Kinoshita, T Unemoto. 1984. Amplification of the Streptococcus faecalis proton-translocating ATPase by a decrease in cytoplasmic pH.. https://doi.org/10.1128/jb.158.3.1157-1160.1984

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Mitochondrial defects in cis-diamminedichloroplatinum(II)-resistant human ovarian carcinoma cells.

We have been studying the membranes of cisplatin (DDP)-resistant 2008 human ovarian carcinoma cells (C13* cells) for alterations that may account for their decreased DDP accumulation. We now report that C13* cells have significant changes in their mitochondrial and plasma membrane potentials and in their mitochondrial morphology. C13* cells accumulated 2.0 +/- 0.1-fold more of the membrane potential marker [3H]tetraphenylphosphonium cation (TPP+) than sensitive cells. In high K+ medium, which depolarizes the plasma membrane but not the mitochondrial membrane, [3H]TPP+ accumulation was still 2.3 +/- 0.1- fold greater in resistant cells, indicating that the mitochondrial membrane potential was higher. In the presence of carbonyl cyanide p-trifluoromethoxyphenyl hydrazone, which depolarizes the mitochondrial membrane but not the plasma membrane, [3H]TPP+ accumulation demonstrated that the plasma membrane potential in C13* cells was elevated as well. These elevations were also present in C8 cells with low-level DDP resistance. After ouabain treatment, exposure to nigericin stimulated [3H]TPP+ accumulation 3-fold in sensitive cells but had no effect in C13* cells, indicating either that: (a) the mitochondrial pH gradient was minimal; or (b) the mitochondrial electric potential was already at a maximal level in C13* cells. Fluorescence microscopy of living cells stained with the mitochondria-specific dye rhodamine 123 revealed that resistant cells had significant changes in their mitochondrial morphology. Electron microscopy also revealed major alterations in the cristae structure. The C13* cells, which were approximately 15-fold resistant to DDP, were 5-fold hypersensitive to the mitochondrial poison rhodamine 123. We conclude that these DDP-resistant 2008 cells have an elevated plasma membrane potential and alterations in their mitochondria as indicated by their membrane potential, morphology, and sensitivity to mitochondrial poisons. These results imply that mitochondria play an important role in the cellular pharmacology of DDP.

Carbonyl Cyanide m-Chlorophenyl Hydrazone

Differential permeability for lipophilic compounds in uncoupler-resistant cells of Escherichia coli.

The acrA strain AS-1 of Escherichia coli is more sensitive than its parent W3110 to growth inhibition by Methylene blue, sodium dodecyl sulfate and novobiocin. UR-3 is an uncoupler-resistant strain isolated from AS-1 which is resistant to growth inhibition by carbonylcyanide m-chlorophenylhydrazone (CCCP), 3,3',4',5-tetrachlorsalicylanilide (TCS) and tributyltin chloride, while remaining sensitive to the first group of compounds. A revertant of AS-1 acquired resistance to Methylene blue and sodium dodecyl sulfate but remained sensitive to uncouplers. In contrast to AS-1, proline uptake in UR-3 was resistant to uncouplers. Strain UR-3 grown in the presence of uncoupler incorporated elongation factor Tu to high levels in the outer membrane of the cell. A role for the outer membrane in the acquisition of uncoupler-resistance by UR-3 is suggested by the behaviour of the mutant to the fluorescence probe N-phenyl-1-naphthylamine. The fluorescence intensity of this probe was quenched by membrane energization in the wild-type strain W3110 but not in AS-1. UR-3 behaved like W3110, suggesting that an outer membrane barrier to neutral lipophilic compounds like N-phenyl-1-naphthylamine (NPN) and uncouplers had been restored in UR-3. By contrast, AS-1 and UR-3 both allowed energized uptake of the fluorescent lipophilic cation 2-(dimethylaminostyryl)-1-ethylpyridinium (DMP+). It is concluded that lipophilic materials must permeate the outer membrane of E. coli by at least two different routes. However, uncoupler-resistance in UR-3 appears to be more complex than the provision of an outer membrane barrier to uncouplers. Thus, uncouplers readily discharged a pH gradient established in both AS-1 and UR-3 by addition of HCl to cell suspensions.

Carbonyl Cyanide m-Chlorophenyl Hydrazone

Polar and lateral flagellar motors of marine Vibrio are driven by different ion-motive forces.

Various species of marine Vibrio produce two distinct types of flagella, each adapted for a different type of motility. A single, sheathed polar flagellum is suited for swimming in liquid medium, and numerous unsheathed lateral flagella, which are produced only under viscous conditions, are suited for swarming over viscous surfaces. Both types of flagella are driven by reversible motors embedded in the cytoplasmic membrane. Here we report that the energy source for the polar flagellar motor of Vibrio parahaemolyticus is the sodium-motive force, whereas the lateral flagellar motors are driven by the proton-motive force. This is evidence that two distinct types of flagella powered by different energy sources are functionally active in one cell.

Carbonyl Cyanide m-Chlorophenyl Hydrazone