anti-OxPhos Complex IV subunit IV (yeast), -"DISCONTINUED" - Citations

anti-OxPhos Complex IV subunit IV (yeast), -"DISCONTINUED" - Citations

View additional product information for anti-OxPhos Complex IV subunit IV (yeast), -"DISCONTINUED" - Citations (A6432)

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Abstract
Subunit VIa of yeast cytochrome c oxidase is not necessary for assembly of the enzyme complex but modulates the enzyme activity. Isolation and characterization of the nuclear-coded gene.
AuthorsTaanman JW, Capaldi RA
JournalJ Biol Chem
PubMed ID8395517
'COX13, the nuclear gene for cytochrome c oxidase subunit VIa of Saccharomyces cerevisiae, has been isolated in two steps. First, the partial amino acid sequence information of the subunit was used to design two degenerate oligodeoxynucleotide primers to amplify part of the gene in a polymerase chain reaction. Next, the ... More
A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast.
AuthorsPavlov EV, Priault M, Pietkiewicz D, Cheng EH, Antonsson B, Manon S, Korsmeyer SJ, Mannella CA, Kinnally KW
JournalJ Cell Biol
PubMed ID11724814
'During apoptosis, proapoptotic factors are released from mitochondria by as yet undefined mechanisms. Patch-clamping of mitochondria and proteoliposomes formed from mitochondrial outer membranes of mammalian (FL5.12) cells has uncovered a novel ion channel whose activity correlates with onset of apoptosis. The pore diameter inferred from the largest conductance state of ... More
Absence of the mitochondrial AAA protease Yme1p restores F0-ATPase subunit accumulation in an oxa1 deletion mutant of Saccharomyces cerevisiae.
AuthorsLemaire C, Hamel P, Velours J, Dujardin G
JournalJ Biol Chem
PubMed ID10816574
'The nuclear gene OXA1 encodes a protein located within the mitochondrial inner membrane that is required for the biogenesis of both cytochrome c oxidase (Cox) and ATPase. In the absence of Oxa1p, the translocation of the mitochondrially encoded subunit Cox2p to the intermembrane space (also referred to as export) is ... More
Complexity and tissue specificity of the mitochondrial respiratory chain.
AuthorsCapaldi RA, Halphen DG, Zhang YZ, Yanamura W
JournalJ Bioenerg Biomembr
PubMed ID2841307
There is a renewed interest in the structure and functioning of the mitochondrial respiratory chain with the realization that a number of genetic disorders result from defects in mitochondrial electron transfer. These socalled mitochondrial myopathies include diseases of muscle, heart, and brain. The respiratory chain can be fractionated into four ... More
Subunit function in eukaryote cytochrome c oxidase. A mutation in the nuclear-coded subunit IV allows assembly but alters the function and stability of yeast cytochrome c oxidase.
AuthorsLightowlers R, Chrzanowska-Lightowlers Z, Marusich M, Capaldi RA
JournalJ Biol Chem
PubMed ID1850417
Strains of the yeast Saccharomyces cerevisiae disrupted in YCOX4, the nuclear gene encoding cytochrome c oxidase subunit IV, do not assemble a functional or spectrally visible oxidase. We report the characterization of a yeast strain, RM1, expressing a mutated YCOX4 gene which is temperature sensitive for respiration at 37 degrees ... More
Activation of membrane-associated procaspase-3 is regulated by Bcl-2.
AuthorsKrebs JF, Armstrong RC, Srinivasan A, Aja T, Wong AM, Aboy A, Sayers R, Pham B, Vu T, Hoang K, Karanewsky DS, Leist C, Schmitz A, Wu JC, Tomaselli KJ, Fritz LC
JournalJ Cell Biol
PubMed ID10085291
The mechanism by which membrane-bound Bcl-2 inhibits the activation of cytoplasmic procaspases is unknown. Here we characterize an intracellular, membrane-associated form of procaspase-3 whose activation is controlled by Bcl-2. Heavy membranes isolated from control cells contained a spontaneously activatable caspase-3 zymogen. In contrast, in Bcl-2 overexpressing cells, although the caspase-3 ... More
The characterization and role of zinc binding in yeast Cox4.
AuthorsCoyne HJ, Ciofi-Baffoni S, Banci L, Bertini I, Zhang L, George GN, Winge DR
JournalJ Biol Chem
PubMed ID17215247
Yeast Cox4 is a zinc binding subunit of cytochrome c oxidase. Cox4 is the only cofactor-containing subunit that is not directly part of the catalytic core of the enzyme located in the mitochondrial inner membrane. The Zn(II) site is shown to be distinct from the bovine ortholog, as it results ... More
MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria.
AuthorsBurgess SM, Delannoy M, Jensen RE
JournalJ Cell Biol
PubMed ID8089172
In the yeast Saccharomyces cerevisiae, mitochondria are elongated organelles which form a reticulum around the cell periphery. To determine the mechanism by which mitochondrial shape is established and maintained, we screened yeast mutants for those defective in mitochondrial morphology. One of these mutants, mmm1, is temperature-sensitive for the external shape ... More
Cardiolipin is not required to maintain mitochondrial DNA stability or cell viability for Saccharomyces cerevisiae grown at elevated temperatures.
AuthorsZhang M, Su X, Mileykovskaya E, Amoscato AA, Dowhan W
JournalJ Biol Chem
PubMed ID12840009
In eukaryotic cells, the phospholipid cardiolipin (CL) is primarily found in the inner mitochondrial membrane. Saccharomyces cerevisiae mutants, unable to synthesize CL because of a null allele of the CRD1 gene (encodes CL synthase), have been reported with different phenotypes. Some mutants, when grown on a nonfermentable carbon source at ... More
The phosphatidylglycerol/cardiolipin biosynthetic pathway is required for the activation of inositol phosphosphingolipid phospholipase C, Isc1p, during growth of Saccharomyces cerevisiae.
AuthorsVaena de Avalos S, Su X, Zhang M, Okamoto Y, Dowhan W, Hannun YA
JournalJ Biol Chem
PubMed ID15611094
Inositolsphingolipid phospholipase C (Isc1p) is the Saccharomyces cerevisiae member of the extended family of neutral sphingomyelinases that regulates the generation of bioactive ceramides. Recently, we reported that Isc1p is post-translationally activated in the post-diauxic phase of growth and that it localizes to mitochondria (Vaena de Avalos, S., Okamoto, Y., and ... More