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B Guerin

Publications and source records attributed to B Guerin.

At least 19 recordsLinked to original sources
PubMed1992

The C-terminal region of subunit 4 (subunit b) is essential for assembly of the F0 portion of yeast mitochondrial ATP synthase.

The role of the C-terminal part of yeast ATP synthase subunit 4 (subunit b) in the assembly of the whole enzyme was studied by using nonsense mutants generated by site-directed mutagenesis. The removal of at least the last 10 amino-acid residues promoted mutants which were unable to grow with glycerol or lactate as carbon source. These mutants were devoid of subunit 4 and of another F0 subunit, the mitochondrially encoded subunit 6. The removal of the last eight amino-acid residues promoted a temperature-sensitive mutant (PVY161). At 37 degrees C this strain showed the same phenotype as above. When grown at permissive temperature (30 degrees C) with lactate as carbon source, PVY161 and the wild-type strain both displayed the same generation time and growth yield. Furthermore, the two strains showed identical cellular respiration rates at 30 degrees C and 37 degrees C. However, in vitro the ATP hydrolysis of PVY161 mitochondria exhibited a low sensitivity to F0 inhibitors, while ATP synthesis displayed the same oligomycin sensitivity as wild-type mitochondria. It is concluded that, in this mutant, the assembly of the truncated subunit 4 in PVY161 ATP synthase is thermosensitive and that, once a functional F0 is formed, it is stable. On the other hand, the removal of the last eight amino-acid residues promoted in vitro a proton leak between the site of action of oligomycin and F1.

Adenosine Triphosphatases↗
PubMed1992

The house dust mite Dermatophagoides pteronyssinus is the most important allergen on the island of Mauritius.

To determine the relative importance of mites as a cause of allergic sensitivity and asthma on the western Indian Ocean island of Mauritius, we measured specific IgE antibodies to common inhalant allergens in sera from Mauritians claiming to have allergic symptoms and we examined house dust samples for evidence of mites and their allergens. Seventy-two of the 110 sera tested (65%) contained detectable IgE antibody to at least one mite, mould or pollen allergenic extract. By far the most prevalent was antibody to one or both of the common house dust mites, Dermatophagoides pteronyssinus and Dermatophagoides farinae, being present in 67 (61%) of the 110 sera. Allergy to pollens, including the locally prevalent Bermuda grass and sugar cane, was infrequent. Antibody to a limited number of moulds was detected in 22% of the sera tested. Of 81 subjects whose clinical history was known, 60 were asthmatic, and 75% of these asthmatic individuals had IgE antibody to mites. In contrast, only 35% of the subjects with rhinitis without asthma were sensitive to mites. Different mite species, including D. pteronyssinus but not D. farinae, were identified microscopically in samples of local house dust. Mite antigen Der p I but not antigen Der f I was detected with specific monoclonal antibodies in extracts of these dust samples. On the bases of this serological and environmental survey, we conclude that our data support the hypothesis that the house dust mite D. pteronyssinus is the principal cause of allergic sensitivity and asthma in that tropical environment.

Adolescent↗
PubMed1990

Capillary leakage complicated by compartment syndrome necessitating surgery.

A single episode of systemic capillary leak syndrome is reported in a HIV-positive patient. The shock had necessitated the infusion of large amounts of fluid with concomitant diffuse swelling and weight gain leading to compartment syndrome of both legs. This required surgical relief. The initial high hematocrit (62%) and low serum protein concentration (48 g/l) with normal factor V (molecular weight above 300,000) concentrations are the hallmark of capillary leak when they are associated with hypovolemic shock. It must be emphasized that fluid resuscitation may worsen the muscle damage with ultimate compartment syndrome. Therefore, it appears reasonable to monitor muscular pressure during volume expansion in patients with capillary leak syndrome, severe shock and muscular swelling.

Adult↗
PubMed1989

The role of subunit 4, a nuclear-encoded protein of the F0 sector of yeast mitochondrial ATP synthase, in the assembly of the whole complex.

The yeast nuclear gene ATP4, encoding the ATP synthase subunit 4, was disrupted by insertion into the middle of it the selective marker URA3. Transformation of the Saccharomyces cerevisiae strain D273-10B/A/U produced a mutant unable to grow on glycerol medium. The ATP4 gene is unique since subunit 4 was not present in mutant mitochondria; the hypothetical truncated subunit 4 was never detected. ATPase was rendered oligomycin-insensitive and the F1 sector of this mutant appeared loosely bound to the membrane. Analysis of mitochondrially translated hydrophobic subunits of F0 revealed that subunits 8 and 9 were present, unlike subunit 6. This indicated a structural relationship between subunits 4 and 6 during biogenesis of F0. It therefore appears that subunit 4 (also called subunit b in beef heart and Escherichia coli ATP synthases) plays at least a structural role in the assembly of the whole complex. Disruption of the ATP4 gene also had a dramatic effect on the assembly of other mitochondrial complexes. Thus, the cytochrome oxidase activity of the mutant strain was about five times lower than that of the wild type. In addition, a high percentage of spontaneous rho- mutants was detected.

Adenosine Triphosphatases↗
PubMed1989

Thermodynamic and kinetic control of ATP synthesis in yeast mitochondria: role of delta pH.

ATP synthesis rate, measured as the variation in external Pi concentration, varied as a linear function of either delta mu H+ or delta Gpin, in such a manner that the delta Gpin/delta mu H+ ratio increased while VATP increased. We also observed a linear dependence of the flux control coefficient of the Pi carrier on delta pH. All the results presented can be explained by a relatively large delta pH drop when VATP increases.

Adenosine Diphosphate↗
PubMed1989

The yeast ATP synthase subunit 4: structure and function.

The structure of ATP synthase subunit 4 was determined by using the oligonucleotide probe procedure. This subunit is the fourth polypeptide of the complex when classifying subunits in order of decreasing molecular mass. Its relative molecular mass is 25 kDa. The ATP4 gene was isolated and sequenced. The nucleotide sequence predicts that subunit 4 is probably derived from a precursor protein 244 amino acids long. Mature subunit 4 contains 209 amino acid residues and the predicted molecular mass is 23250 kDa. Subunit 4 shows homology with the b-subunit of Escherichia coli ATP synthase and the b-subunit of beef heart mitochondrial ATP synthase. By using homologous transformation, a mutant lacking wild subunit 4 was constructed. This mutant is devoid of oxidative phosphorylation and F1 is loosely bound to the membrane. Our data are in favor of a structural relationship between subunit 4 and the mitochondrially-translated subunit 6 during biogenesis of F0.

Amino Acid Sequence↗
PubMed1988

Localization of the synthesis of very-long-chain fatty acid in mitochondria from Saccharomyces cerevisiae.

The localization of the mitochondrial elongation activities ('elongases') from Saccharomyces cerevisiae has been investigated. It was shown, using carboxyatractyloside in the incubation mixture, that synthesis of very-long-chain fatty acids probably occurred outside the matrix and, by fractionation experiments, that elongases are membrane-bound enzymes. The solubilization of the outer membrane by digitonin showed that three elongating activities are correlated with a marker of the outer membrane and not with an inner membrane marker. A further partial purification of the outer membrane showed that elongases are present in the outer membrane of mitochondria.

Acyl-Carrier Protein S-Malonyltransferase↗
PubMed1988

Redistribution of the flux-control coefficients in mitochondrial oxidative phosphorylations in the course of brain edema.

This work describes the control exerted by dicarboxylate carrier and succinate dehydrogenase activities on the oxidative phosphorylations in rabbit brain mitochondria as an edema develops. Vasogenic edema leads to an uncompetitive inhibition of succinate dehydrogenase activity and to a large decrease of oxidative phosphorylations linked to succinate utilisation. Naftidrofuryl treatment in vivo restores both a high succinate dehydrogenase activity and a normal respiratory rate. In order to quantify the control of oxidative phosphorylations by the succinate dehydrogenase step, we applied the control analysis (Kacser, H. and Burns, J.A. (1973) in Rate Control of Biological Processes (Davies, D.D., ed.), pp. 65-104, Cambridge University Press, London; Heinrich, R. and Rapoport, T.A. (1974) Eur. J. Biochem. 42, 89-95). By using two inhibitors, one (phenylsuccinate) acting only on the dicarboxylate carrier and another (malonate) acting on both the dicarboxylate carrier and the succinate dehydrogenase, a method was developed to calculate the control coefficients of these two steps. The main result is that in mitochondria isolated from normal tissue succinate dehydrogenase exerted no control, but in the course of edema this enzymatic step became a controlling one: a transition from zero to a high control coefficient (0.5) was observed from the onset of intracellular edema for the threshold value of water/dry-weight tissue of 4.6.

Animals↗
PubMed1988

Comparative studies on the glycolytic and hexose monophosphate pathways in Candida parapsilosis and Saccharomyces cerevisiae.

Some enzymatic activities of the glycolytic and hexose monophosphate pathways of Candida parapsilosis, a yeast lacking alcohol dehydrogenase but able to grow on high glucose concentrations, were compared to those of Saccharomyces cerevisiae. Cells were grown either on 8% glucose or on 2% glycerol and activities measured under optimal conditions. Results were as follows: glycolytic enzymes of C. parapsilosis, except glyceraldehyde 3-phosphate dehydrogenase, exhibited an activity weaker than that of S. cerevisiae, especially when yeasts were grown on glycerol. Fructose-1,6 bisphosphatase, an enzyme implicated in gluconeogenesis and in the hexose monophosphate pathway, and known to be very sensitive to catabolite repression in S. cerevisiae, was always active in C. parapsilosis even when cells were grown on 8% glucose. However, the allosteric properties towards AMP and fructose-2,6-bisphosphate were the same in both strains. Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, two other enzymes of the hexose monophosphate pathway, exhibited a higher activity in C. parapsilosis than in S. cerevisiae. Regulation of two important control points of the glycolytic flux, phosphofructokinase and pyruvate kinase, was investigated. In C. parapsilosis phosphofructokinase was poorly sensitive to ATP but fructose-2,6-bisphosphate completely relieved the light ATP inhibition. Pyruvate kinase did not require fructose-1,6-bisphosphate for its activity, and by this way, did not regulate the glycolytic flux.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine Triphosphate↗
PubMed1988

Skin tests.

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Allergens↗
PubMed1987

Modification of flow-force relationships by external ATP in yeast mitochondria.

The purpose of this work is to measure protonmotive force and cytochrome reduction level under different respiratory steady states in isolated yeast mitochondria. The rate of respiration was varied by using three sets of conditions: (a) different external phosphate concentrations with a fixed concentration of ADP (ATP synthesis) and (b) different concentrations of carbonylcyanide m-chlorophenylhydrazone in the presence of oligomycin and carboxyatractylate (uncoupling) either in the absence or (c) in the presence of external ATP. ADP plus phosphate stimulates respiration more than uncoupler at the same protonmotive force value. However, the relationships between respiratory rate and protonmotive force were similar when stimulation was induced either by ADP + Pi or by carbonylcyanide m-chlorophenylhydrazone in the presence of ATP. At the same respiratory rate, cytochrome a + a3 is more reduced by uncoupler than by ADP + Pi additions. However, the relationships between respiratory rate and reduction level of cytochrome-c oxidase are similar both under ATP synthesis and with uncoupling conditions in the presence of external ATP. Control of respiration exerted by cytochrome-c oxidase, and support the view the condition mentioned above. This control was low when the respiratory rate was varied by the ATP synthesis rate; it increased as a function of the respiratory rate with uncoupler in the absence of ATP. ATP decreased this control under uncoupling conditions. These results suggest a regulatory effect of external ATP on cytochrome-c oxidase, and support the view that the relationships between respiratory rate and protonmotive force, on the one hand, and respiratory rate and the reduction level of cytochrome-c oxidase, on the other, depend respectively on the kinetic regulations of the system.

Adenosine Triphosphate↗
PubMed1987

Fatty acid synthesis in mitochondria from Saccharomyces cerevisiae.

The ability of purified mitochondria isolated from S. cerevisiae to synthesize fatty acids and especially very long chain fatty acids (VLCFA) has been investigated. The VLCFA synthesis requires malonyl-CoA as the C2 unit donor and NADPH as the reducing agent. Moreover the yeast mitochondrial elongase is able to accept either exogenous long chain fatty acyl-CoAs as substrates or elongate endogenous substrates. In the latter case, ATP is required for full activity. Besides this important VLCFA formation, the mitochondria from S. cerevisiae were also able to synthesize C16 and C18.

Acetyltransferases↗
PubMed1986

Localisation of the hydrophilic C terminal part of the ATP synthase subunit 8 of Saccharomyces cerevisiae.

The hydrophobic subunit 8 of the yeast ATP synthase was modified using the non-penetrating amino reactive specific reagent: isethionylacetimidate. The polypeptide was modified when using the isolated ATP synthase and sodium bromide-treated submitochondrial particles. It is shown that the only lysine of the protein was modified by the reagent. It is concluded that the hydrophilic C terminal part of the protein containing lysine 47 is located on the inner side of the inner mitochondrial membrane.

Amino Acid Sequence↗