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  • 1
    ISSN: 1432-0983
    Keywords: Key words MSS51 ; Mitochondrial translation ; Yeast ; Cytochrome c oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Mutants of Saccharomyces cerevisiae that lack a functional MSS51 gene are respiratory deficient due to the absence of cytochrome c oxidase subunit 1 (Cox1p). It has been previously suggested, but not formally proven, that Mss51p is required for translational activation of COX1 mRNA, rather than being involved in a subsequent step in the synthesis of Cox1p or its assembly into cytochrome c oxidase. Pulse-chase labelling experiments now show that the absence of detectable levels of Cox1p in mss51-null strains is indeed due to the lack of synthesis of Cox1p, and is not caused by reduced stability of the protein. To gain more insight into the exact function of Mss51p, we determined the subcellular localization of the protein. We were able to show that an epitope-tagged version of Mss51p (Mss51HA) complements the mutation and can be localized in mitochondria, where it is firmly associated with the mitochondrial inner membrane. In addition, we characterized the previously identified mutant allele mss51-3. Sequence analysis revealed the presence of a short open reading frame upstream of MSS51 resulting from the creation of an extra ATG startcodon.
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  • 2
    ISSN: 1432-0983
    Keywords: Key words Mitochondrial translation ; RNA binding ; Isocitrate dehydrogenase ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Krebs cycle NAD+-isocitrate dehydrogenase (Idh) binds to the 5-UTRs of all mitochondrial mRNAs in Saccharomyces cerevisiae. We hypothesize that this leader-binding activity plays a role in translational regulation, thereby linking mitochondrial biogenesis to the need for respiratory function. Analysis of effects of leader binding on mitochondrial translation is complicated by the involvement of the enzyme in mitochondrial metabolism. We have therefore searched for an Idh altered in RNA binding, but retaining full enzyme activity. Idh from Kluyveromyces lactis and Schizosaccharomyces pombe was partially purified and examined for the ability to bind Cox2 mRNA. Sch. pombe Idh, like the S. cerevisiae enzyme, has high affinity for both its own, K. lactis and S. cerevisiaeCOX2 leaders. In contrast, Idh purified from K. lactis shows only low affinity for all mRNAs tested. To determine what distinguishes K. lactis Idh from S. cerevisiae Idh, genes encoding the two subunits of Idh in K. lactis were cloned and sequenced. Sequence comparison revealed high levels of similarity throughout the proteins, in particular in regions involved in enzyme activity, co-factor and regulator binding. Non-conserved residues between the subunits from the two yeasts are candidates for involvement in the interaction with RNA.
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  • 3
    ISSN: 1434-1948
    Keywords: Copper ; Magnetic properties ; Supramolecular chemistry ; Three-dimensional architecture ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A novel three-dimensional copper(II) compound of the formula [Cu3(btre)5(H2O)2](ClO4)6·H2O (btre = 1,2-bis(1,2,4-triazol-4-yl)ethane) has been synthesized. The structure has been solved at 150 K by single-crystal X-ray analysis. The compound [C30H44Cu3N30O2·6(ClO4)·H2O] crystallizes in the triclinic space group P1bar with a = 12.488(1), b = 13.195(1), c = 19.756(2) Å, α = 78.959(8), β = 84.553(8), γ = 63.869(7)°, V = 2868.4(5) Å3, Z = 2 (trinuclear CuII units), 6484 reflections [I 〉 4σ(Ι)], RF = 0.0581, wR2 = 0.1214. The structure of this coordination polymer consists of a three-dimensional network built up from linear trinuclear CuII cations of formula [Cu3(btre)5(H2O)2]6+. This crystallographically independent unit comprises a linear array of three CuII ions linked by triple N1,N2-1,2,4-triazole bridges, yielding Cu1-Cu2 = 3.893(1) Å and Cu2-Cu3 = 3.889(1) Å. These linear trinuclear CuII units are linked by various pathways involving tridentate and tetradentate bridging btre ligands, which yields an unprecedented three-dimensional network. The CuII ions are weakly antiferromagnetically coupled with J = -1.01(2) cm-1 (based on the Hamiltonian: H = -J[SCu1·SCu2 + SCu2·SCu3] using the expression for the molar magnetic susceptibility S = 1/2 of a linear trinuclear system). The nature and the magnitude of the antiferromagnetic exchange have been discussed on the basis of the structural features.
    Additional Material: 4 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Berichte der deutschen chemischen Gesellschaft 1999 (1999), S. 505-507 
    ISSN: 1434-1948
    Keywords: Macrocycle ; Pyrazole ; N-Heterocycle ; Carbonate ; Copper ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The 22-membered macrocycle, spanning four endocyclic pyrazole groups, viz. 1,4,9,14,17,22,27,28,29,30-decaaza-5,13,18,26-tetramethylpentacyclo[24.2.1.14,7.111,14.117,20]triacontane-5,7(28),11(29),12,18,20(30),24(27),25-octaene (22Pz), rendered the tetranuclear compound [Cu4(22Pz)2(CO3)2(MeOH)2](ClO4)4(MeOH)4. The copper(II) ions are in distorted octahedral N3O3 environments. All four pyrazole groups of each macrocycle participate in the coordination of the copper(II) ions. The cationic part of this compound is in fact a dimer of two macrocyclic ligands, each containing two copper(II) ions bridged by two carbonate ions in the highly unusual pentacoordinating fashion.Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2005/1999/98332_s.pdf or from the author.
    Additional Material: 2 Ill.
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