Chromosomal mapping of the KlCYC1 gene from Kluyveromyces lactis

Genome ◽  
1994 ◽  
Vol 37 (3) ◽  
pp. 515-517 ◽  
Author(s):  
M. Isabel González-Siso ◽  
M. Angeles Freire-Picos ◽  
M. Esperanza Cerdán ◽  
M. Wésolowski-Louvel ◽  
H. Fukuhara
Keyword(s):  
Cytochrome C ◽  
Kluyveromyces Lactis ◽  
Chromosomal Mapping ◽  
Hybridization Signal ◽  
Chromosomal Assignment

Chromosomal assignment of the KlCYC1 gene from Kluyveromyces lactis has been performed by hybridization of the labelled probe to a DNA blot of isolated chromosomes. A clear hybridization signal to chromosome VI is reported.Key words: Kluyveromyces lactis, cytochrome c gene, chromosomal mapping.

Codon usage in Kluyveromyces lactis and in yeast cytochrome c-encoding genes

Gene ◽  
1994 ◽  
Vol 139 (1) ◽  
pp. 43-49 ◽  
Author(s):  
M.Angeles Freire-Picos ◽  
M.Isabel Gonzalez-Siso ◽  
Esther Rodríguez-Belmonte ◽  
Ana María Rodríguez-Torres ◽  
Elvira Ramil ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Codon Usage ◽  
Kluyveromyces Lactis ◽  
Encoding Genes

Regulation of cytochrome c expression in the aerobic respiratory yeast Kluyveromyces lactis

FEBS Letters ◽  
1995 ◽  
Vol 360 (1) ◽  
pp. 39-42 ◽  
Author(s):  
M.Angeles Freire-Picos ◽  
Cornelis P. Hollenberg ◽  
Karin D. Breunig ◽  
M.Esperanza Cerdan
Keyword(s):  
Cytochrome C ◽  
Kluyveromyces Lactis

Isolation and molecular analysis of the gene for cytochrome c 1 from Kluyveromyces lactis

1996 ◽  
Vol 30 (2) ◽  
pp. 145-150 ◽  
Author(s):  
Yvetta Gbelsk� ◽  
Katar�na Horv�thov� ◽  
Quirina J. M. van der Aart ◽  
B. J. M. Zonneveld ◽  
H. Y. Steensma ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Molecular Analysis ◽  
Kluyveromyces Lactis

scholarly journals Mutations in MGI genes convert Kluyveromyces lactis into a petite-positive yeast.

Genetics ◽  
1993 ◽  
Vol 133 (3) ◽  
pp. 517-525 ◽  
Author(s):  
X J Chen ◽  
G D Clark-Walker
Keyword(s):  
Cytochrome C ◽  
Mitochondrial Genome ◽  
Ethidium Bromide ◽  
High Frequency ◽  
Kluyveromyces Lactis ◽  
Genome Integrity ◽  
Gene Products ◽  
Targeted Disruption ◽  
Nuclear Mutation ◽  
Petite Negative Yeast

Abstract Following targeted disruption of the unique CYC1 gene, the petite-negative yeast, Kluyveromyces lactis, was found to grow fermentatively in the absence of cytochrome c-mediated respiration. This observation encouraged us to seek mitochondrial mutants by treatment of K. lactis with ethidium bromide at the highest concentration permitting survival. By this technique, we isolated four mtDNA mutants, three lacking mtDNA and one with a deleted mitochondrial genome. In the three isolates lacking mtDNA, a nuclear mutation is present that permits petite formation. The three mutations occur at two different loci, designated MGI1 and MGI2 (for Mitochondrial Genome Integrity). The mgi mutations convert K. lactis into a petite-positive yeast. Like bakers' yeast, the mgi mutants spontaneously produce petites with deletions in mtDNA and lose this genome at high frequency on treatment with ethidium bromide. We suggest that the MGI gene products are required for maintaining the integrity of the mitochondrial genome and that, petite-positive yeasts may be naturally altered in one or other of these genes.

Nucleic Acid Molecules Prepared by Monolayer Techniques

1972 ◽  
Vol 30 ◽  
pp. 178-179
Author(s):  
Dimitrij Lang
Keyword(s):  
Electron Microscopy ◽  
Standard Deviation ◽  
Nucleic Acid ◽  
Cytochrome C ◽  
Nucleic Acids ◽  
Contour Length ◽  
Sample Standard Deviation ◽  
Molecular Weights ◽  
Length Measurements ◽  
Protein Monolayer

The success of the protein monolayer technique for electron microscopy of individual DNA molecules is based on the prevention of aggregation and orientation of the molecules during drying on specimen grids. DNA adsorbs first to a surface-denatured, insoluble cytochrome c monolayer which is then transferred to grids, without major distortion, by touching. Fig. 1 shows three basic procedures which, modified or not, permit the study of various important properties of nucleic acids, either in concert with other methods or exclusively:1) Molecular weights relative to DNA standards as well as number distributions of molecular weights can be obtained from contour length measurements with a sample standard deviation between 1 and 4%.

Activation of cytochrome c to a peroxidase compound I-type intermediate by H2O2: relevance to redox signalling in apoptosis

2004 ◽  
Vol 71 ◽  
pp. 97-106 ◽  
Author(s):  
Mark Burkitt ◽  
Clare Jones ◽  
Andrew Lawrence ◽  
Peter Wardman
Keyword(s):  
Cytochrome C ◽  
Hydroxyl Radical ◽  
Redox Regulation ◽  
Chemotherapeutic Agents ◽  
Tyrosyl Radical ◽  
Compound I ◽  
Definitive Evidence ◽  
Enhanced Production ◽  
Physico Chemical

The release of cytochrome c from mitochondria during apoptosis results in the enhanced production of superoxide radicals, which are converted to H2O2 by Mn-superoxide dismutase. We have been concerned with the role of cytochrome c/H2O2 in the induction of oxidative stress during apoptosis. Our initial studies showed that cytochrome c is a potent catalyst of 2′,7′-dichlorofluorescin oxidation, thereby explaining the increased rate of production of the fluorophore 2′,7′-dichlorofluorescein in apoptotic cells. Although it has been speculated that the oxidizing species may be a ferryl-haem intermediate, no definitive evidence for the formation of such a species has been reported. Alternatively, it is possible that the hydroxyl radical may be generated, as seen in the reaction of certain iron chelates with H2O2. By examining the effects of radical scavengers on 2′,7′-dichlorofluorescin oxidation by cytochrome c/H2O2, together with complementary EPR studies, we have demonstrated that the hydroxyl radical is not generated. Our findings point, instead, to the formation of a peroxidase compound I species, with one oxidizing equivalent present as an oxo-ferryl haem intermediate and the other as the tyrosyl radical identified by Barr and colleagues [Barr, Gunther, Deterding, Tomer and Mason (1996) J. Biol. Chem. 271, 15498-15503]. Studies with spin traps indicated that the oxo-ferryl haem is the active oxidant. These findings provide a physico-chemical basis for the redox changes that occur during apoptosis. Excessive changes (possibly catalysed by cytochrome c) may have implications for the redox regulation of cell death, including the sensitivity of tumour cells to chemotherapeutic agents.

Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c

2001 ◽  
Vol 268 (6) ◽  
pp. 1620-1630
Author(s):  
Yibing Wu ◽  
Yunhua Wang ◽  
Chengmin Qian ◽  
Jun Lu ◽  
Ercheng Li ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Solution Structure ◽  
Cytochrome B5
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