Nuclear functions required for cytochrome c oxidase biogenesis in Saccharomyces cerevisiae: multiple trans-acting nuclear genes exert specific effects on expression of each of the cytochrome c oxidase subunits encoded on mitochondrial DNA

1987 ◽  
Vol 12 (5) ◽  
pp. 311-322 ◽  
Author(s):  
Barbara Kloeckener-Gruissem ◽  
Joan E. McEwen ◽  
Robert O. Poyton
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mitochondrial Dna ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Nuclear Genes ◽  
Specific Effects

Four new species of the primitively segmented spider genus Songthela (Mesothelae, Liphistiidae) from Chongqing Municipality, China

Zootaxa ◽  
2022 ◽  
Vol 5091 (4) ◽  
pp. 546-558
Author(s):  
ZHAOYANG CHEN ◽  
FENGXIANG LIU ◽  
DAIQIN LI ◽  
XIN XU
Keyword(s):  
Mitochondrial Dna ◽  
New Species ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Dna Barcode ◽  
Morphological Characters ◽  
Oxidase Subunit ◽  
Chongqing Municipality ◽  
Males And Females

This paper reports four new species of the primitively segmented spider genus Songthela from Chongqing Municipality, China, based on morphological characters of both males and females: S. jinyun sp. nov., S. longbao sp. nov., S. serriformis sp. nov. and S. wangerbao sp. nov. We also provide the GenBank accession codes of mitochondrial DNA barcode gene, cytochrome c oxidase subunit I (COI), for the holotype of four new species for future identification.  

scholarly journals Molecular analysis of populations of the invasive species Rhynchophorus ferrugineus Olivier, 1790 (Coleoptera: Curculionidae) in the Region of Murcia (Spain)

2017 ◽  
pp. 155-176
Author(s):  
Miguel Lozano-Terol ◽  
María Juliana Rodríguez-García ◽  
José Galián
Keyword(s):  
Invasive Species ◽  
Phylogenetic Analysis ◽  
Mitochondrial Dna ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Molecular Analysis ◽  
Cox1 Gene ◽  
Rhynchophorus Ferrugineus ◽  
Phylogeographic Analysis ◽  
Oxidase Subunit

En este estudio se analizan dos fragmentos del gen de la citocromo c oxidasa subunidad I (COX1) del ADN mitocondrial de 61 individuos del género Rhynchophorus colectados en la Región de Murcia a fin de determinar su procedencia. El análisis filogenético del fragmento 1 de las muestras de la Región de Murcia conjuntamente con las secuencias disponibles en GenBank indica que los individuos corresponden a la especie Rhynchophorus ferrugineus.Las secuencias de Murcia se colapsan en un único haplotipo (H8 mediterráneo) que aparece dentro del clado de R. ferrugineus. De los análisis filogeográficos se infiere que el origen de los individuos de Murcia es Egipto. Adicionalmente, se examinó una región contigua del COX1 (fragmento 2) en la que las secuencias se colapsaron en dos haplotipos. In this research two fragments of the cytochrome c oxidase subunit I (COX1) gene of the mitochondrial DNA were analyzed in 61 individuals of the genus Rhynchophorus collected in the Region of Murcia with the aim of determining their origin. Phylogenetic analysis of fragment 1 of the samples collected in the Region of Murcia together with the available sequences in GenBank, indicated that these individuals correspond to the species R. ferrugineus. Sequences from Murcia collapsed into the H8 Mediterranean haplotype, which cluster into the R. ferrugineus clade. Phylogeographic analysis shows that the origin of the individuals collected in the Region of Murcia is Egypt. Additionally, a contiguous fragment of COX1 (fragment 2) was analyzed and the sequences collapsed into two haplotypes.

scholarly journals Heteroplasmic Point Mutations of Mitochondrial DNA Affecting Subunit I of Cytochrome c Oxidase in Two Patients With Acquired Idiopathic Sideroblastic Anemia

Blood ◽  
1997 ◽  
Vol 90 (12) ◽  
pp. 4961-4972 ◽  
Author(s):  
Norbert Gattermann ◽  
Stefan Retzlaff ◽  
Yan-Ling Wang ◽  
Götz Hofhaus ◽  
Jürgen Heinisch ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Mitochondrial Dna ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Ferric Iron ◽  
Point Mutations ◽  
Polymorphism Analysis ◽  
Sideroblastic Anemia ◽  
Wide Range

Mitochondrial iron overload in acquired idiopathic sideroblastic anemia (AISA) may be attributable to mutations of mitochondrial DNA (mtDNA), because these can cause respiratory chain dysfunction, thereby impairing reduction of ferric iron (Fe3+) to ferrous iron (Fe2+). The reduced form of iron is essential to the last step of mitochondrial heme biosynthesis. It is not yet understood to which part of the respiratory chain the reduction of ferric iron is linked. In two patients with AISA we identified point mutations of mtDNA affecting the same transmembrane helix within subunit I of cytochrome c oxidase (COX I; ie, complex IV of the respiratory chain). The mutations were detected by restriction fragment length polymorphism analysis and temperature gradient gel electrophoresis. One of the mutations involves a T → C transition in nucleotide position 6742, causing an amino acid change from methionine to threonine. The other mutation is a T → C transition at nt 6721, changing isoleucine to threonine. Both amino acids are highly conserved in a wide range of species. Both mutations are heteroplasmic, ie, they establish a mixture of normal and mutated mitochondrial genomes, which is typical of disorders of mtDNA. The mutations were present in bone marrow and whole blood samples, in isolated platelets, and in granulocytes, but appeared to be absent from T and B lymphocytes purified by immunomagnetic bead separation. They were not detected in buccal mucosa cells obtained by mouthwashes and in cultured skin fibroblasts examined in one of the patients. In both patients, this pattern of involvement suggests that the mtDNA mutation occurred in a self-renewing bone marrow stem cell with myeloid determination. Identification of two point mutations with very similar location suggests that cytochrome c oxidase plays an important role in the pathogenesis of AISA. COX may be the physiologic site of iron reduction and transport through the inner mitochondrial membrane.

[8] Cytochrome-c oxidase from Saccharomyces cerevisiae

1995 ◽  
pp. 97-116 ◽  
Author(s):  
Robert O. Poyton ◽  
Bradley Goehring ◽  
Martin Droste ◽  
Kevin A. Sevarino ◽  
Larry A. Allen ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase

Rpm2, the Protein Subunit of Mitochondrial RNase P in Saccharomyces cerevisiae, Also Has a Role in the Translation of Mitochondrially Encoded Subunits of Cytochrome c Oxidase

Genetics ◽  
2001 ◽  
Vol 158 (2) ◽  
pp. 573-585
Author(s):  
Vilius Stribinskis ◽  
Guo-Jian Gao ◽  
Steven R Ellis ◽  
Nancy C Martin
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Biogenesis ◽  
Mitochondrial Protein ◽  
Nuclear Gene ◽  
Rnase P ◽  
Wild Type ◽  
Protein Subunit ◽  
Mitochondrial Translation

Abstract RPM2 is a Saccharomyces cerevisiae nuclear gene that encodes the protein subunit of mitochondrial RNase P and has an unknown function essential for fermentative growth. Cells lacking mitochondrial RNase P cannot respire and accumulate lesions in their mitochondrial DNA. The effects of a new RPM2 allele, rpm2-100, reveal a novel function of RPM2 in mitochondrial biogenesis. Cells with rpm2-100 as their only source of Rpm2p have correctly processed mitochondrial tRNAs but are still respiratory deficient. Mitochondrial mRNA and rRNA levels are reduced in rpm2-100 cells compared to wild type. The general reduction in mRNA is not reflected in a similar reduction in mitochondrial protein synthesis. Incorporation of labeled precursors into mitochondrially encoded Atp6, Atp8, Atp9, and Cytb protein was enhanced in the mutant relative to wild type, while incorporation into Cox1p, Cox2p, Cox3p, and Var1p was reduced. Pulse-chase analysis of mitochondrial translation revealed decreased rates of translation of COX1, COX2, and COX3 mRNAs. This decrease leads to low steady-state levels of Cox1p, Cox2p, and Cox3p, loss of visible spectra of aa3 cytochromes, and low cytochrome c oxidase activity in mutant mitochondria. Thus, RPM2 has a previously unrecognized role in mitochondrial biogenesis, in addition to its role as a subunit of mitochondrial RNase P. Moreover, there is a synthetic lethal interaction between the disruption of this novel respiratory function and the loss of wild-type mtDNA. This synthetic interaction explains why a complete deletion of RPM2 is lethal.

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