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  • Key wordsKluyveromyces lactis  (2)
  • enthalpy change  (2)
  • Springer  (4)
  • American Heart Association (AHA)
  • 1
    Electronic Resource
    Electronic Resource
    Cloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis : synergistic respiratory deficiency due to mutations in LIPB and mitochondrial F1-ATPase subunits (1997)
    Springer
    Molecular genetics and genomics 255 (1997), S. 341-349 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsKluyveromyces lactis ; Lipoic acid ; Mitochondria ; LIPB gene ; F1-ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The mgi1-4 and mgi2-1 mutants of the petite-negative yeast Kluyveromyces lactis have mutations in the β- and α-subunits of the mitochondrial F1-ATPase, respectively. The mutants are respiratory competent but can form petites with deletions in mitochondrial DNA. In this study a cryptic nuclear mutation (lipB-1) was identified which, in combination with the mgi alleles, displays a synergistic respiratory-deficient phenotype on glycerol medium. The gene defined by the mutation was cloned and shown to encode a polypeptide of 332 amino acids with an N-terminal sequence characteristic of a mitochondrial targeting signal. The deduced protein shares 27% sequence identity with the product of the Escherichia coli lipB gene, which encodes a lipoyl-protein ligase involved in the attachment of lipoyl groups to lipoate-dependent apoproteins. A K. lactis strain carrying a disrupted lipB allele is severely compromised for growth on glycerol medium. The growth defect cannot be rescued by addition of lipoic acid, but cell growth can be restored on medium containing ethanol plus succinate. In addition, it was observed that lipB mutants of K. lactis, unlike the wild-type, are unable to utilize glycine as sole nitrogen source, indicating that activity of the glycine decarboxylase complex (GDC) is also affected. Taken together, these findings suggest that LIPB is the main determinant of the lipoyl-protein ligase activity required for lipoylation of enzymes such as α-ketoacid dehydrogenases and GDC.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050505
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  • 2
    Electronic Resource
    Electronic Resource
    Suppression of ρ 0 lethality by mitochondrial ATP synthase F1 mutations in Kluyveromyces lactis occurs in the absence of F0 (1998)
    Springer
    Molecular genetics and genomics 259 (1998), S. 457-467 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsKluyveromyces lactis ; MGI genes ; F1F0-ATP synthase ; F1 assembly ; F0 subunits
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Specific mgi mutations in the α, β or γ subunits of the mitochondrial F1-ATPase have previously been found to suppress ρ0 lethality in the petite-negative yeast Kluyveromyces lactis. To determine whether the suppressive activity of the altered F1 is dependent on the F0 sector of ATP synthase, we isolated and disrupted the genes KlATP4, 5 and 7, the three nuclear genes encoding subunits b, OSCP and d. Strains disrupted for any one, or all three of these genes are respiration deficient and have reduced viability. However a strain devoid of the three nuclear genes is still unable to lose mitochondrial DNA, whereas a mgi mutant with the three genes inactivated remains petite-positive. In the latter case, ρ0 mutants can be isolated, upon treatment with ethidium bromide, that lack six major F0 subunits, namely the nucleus-encoded subunits b, OSCP and d, and the mitochondrially encoded Atp6, 8 and 9p. Production of ρ0 mutants indicates that an F1-complex carrying a mgi mutation can assemble in the absence of F0 subunits and that suppression of ρ0 lethality is an intrinsic property of the altered F1 particle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050836
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  • 3
    Electronic Resource
    Electronic Resource
    Thermodynamic quantities for the interaction of Cl− with Mg2+, Ca2+ and H+ in aqueous solution from 250 to 325°C (1992)
    Springer
    Journal of solution chemistry 21 (1992), S. 761-788 
    Details
    ISSN: 1572-8927
    Keywords: Equilibrium constant ; enthalpy change ; entropy change ; heat capacity change ; flow calorimetry ; high temperature ; magnesium chloride ; calcium chloride ; hydrochloric acid ; ion association ; isocoulombic reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The aqueous reactions, Mg2++Cl−=MgCl+, Ca2++Cl−=CaCl+, and H+ +Cl−=HCl(aq), were studied as a function of ionic strength at 250, 275, 300, and 325°C using a flow calorimetric technique. The logK, ΔH, ΔS and ΔCp values were determined from the fits of the calculated and experimental heast. The data were reduced assuming a known functionality of the activity coefficient. Hence, the logK, ΔH, ΔS and ΔCp values determined in this study are dependent on the activity coefficient model used. These thermodynamic values were compared with literature results. The logK values for the formation of MgCl+ agree reasonably well with those reported in the literature. The logK values for CaCl+ formation agree reasonably well with those reported in the literature at 300 and 325°C. At lower temperatures, the agreement is poorer. The logK values for the formation of HCl(aq) are generally lower than those reported in the literature. The logK, ΔH, ΔS and ΔCp values for all three ion association reactions are positive and increase with temperature over the temperature range studied. These values are the first determined calorimetrically for the formation of MgCl+ and CaCl+ in the temperature range 275–325°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00651508
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  • 4
    Electronic Resource
    Electronic Resource
    Thermodynamic quantities for the ionization of nitric acid in aqueous solution from 250 to 319°C (1992)
    Springer
    Journal of solution chemistry 21 (1992), S. 789-801 
    Details
    ISSN: 1572-8927
    Keywords: Equilibrium constant ; enthalpy change ; entropy change ; heat capacity change ; flow calorimetry ; high temperature ; nitric acid ; ion association ; isocoulombic reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The aqueous reaction, HNO3(aq)=H++NO 3 − was studied as a function of ionic strength I at 250, 275, 300 and 319°C using a flow calorimeter and the equilibrium constant K and enthalpy change (ΔH) at I=0 were determined. Using these experimental values, equations describing logK, ΔH, the entropy change ΔS and the heat capacity change ΔC p of reaction at I=0 and temperatures from 250 to 319°C were derived. The increasing importance of ion association as temperature rises was discussed. The use of an equation containing identical numbers of positive and identical numbers of negative charges on both sides of the equal sign (isocoulombic reaction principle) was applied to the logK values reported here and to those determined by others. The resulting plot of logK for the isocoulombic reaction vs. 1/T was fairly linear which supports the postulate that the principle is a useful technique for the extrapolation of logK values from low to high temperatures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00651509
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