Haplogroup relationships between domestic and wild sheep resolved using a mitogenome panel

Meadows, Jennifer R. S.; Hiendleder, Stefan; Kijas, James W.

doi:10.1038/hdy.2010.122

Cited by 99 publications

(131 citation statements)

References 27 publications

(51 reference statements)

Supporting

Mentioning

120

Contrasting

Unclassified

Order By: Relevance

“…1C and Table 2). Multiple sequences of the ovine mitochondrion-encoded sequences can be found in on-line databases (31)(32)(33)(34)(35)(36), and in most cases, our MS data confirmed the particular sequence present in our samples (Table 2). In the case of subunit ND4L, no peptides corresponding to available ovine sequences were detected; however, when searched against a database of all mammalian sequences, a match was found for a peptide corresponding to a Connochaetes taurinus (blue wildebeest) sequence of ND4L (Fig.…”

Section: Sequence Comparisons For Mitochondrial Complex I Fromsupporting

confidence: 73%

“…There exists a stark difference in the relative conservation of the mitochondrionand nucleus-encoded core subunits (on average across species, ϳ70% versus ϳ96% identical relative to human, respectively), which likely results from the reduced conservation of hydrophobic residues exposed to the membrane and the higher mutation rate of the mitochondrial genome (Table 1) (29,30). Because of this increased mutation rate, many isoforms of the O. aries mitochondrion-encoded subunits (usually differing by a single amino acid change) have been reported (31)(32)(33)(34)(35)(36). Therefore, where possible, we used protein-identification mass spectrometry experiments (described below) to specifically identify the subunit isoforms present in our sample (see Table 2 for database accession codes for the O. aries sequences used in our analyses).…”

Section: Sequence Comparisons For Mitochondrial Complex I Frommentioning

confidence: 99%

“…2). Given the variability seen in the ovine mitochondrial sequences (31)(32)(33)(34)(35)(36), it is likely that this peptide corresponds to the ND4L protein present in our ovine sample that contains a Lys at position 80.…”

Section: Sequence Comparisons For Mitochondrial Complex I Frommentioning

confidence: 99%

See 2 more Smart Citations

Purification of Ovine Respiratory Complex I Results in a Highly Active and Stable Preparation

Letts¹,

Degliesposti²,

Fiedorczuk³

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

Edited by Linda SpremulliNADH-ubiquinone oxidoreductase (complex I) is the largest (ϳ1 MDa) and the least characterized complex of the mitochondrial electron transport chain. Because of the ease of sample availability, previous work has focused almost exclusively on bovine complex I. However, only medium resolution structural analyses of this complex have been reported. Working with other mammalian complex I homologues is a potential approach for overcoming these limitations. Due to the inherent difficulty of expressing large membrane protein complexes, screening of complex I homologues is limited to large mammals reared for human consumption. The high sequence identity among these available sources may preclude the benefits of screening. Here, we report the characterization of complex I purified from Ovis aries (ovine) heart mitochondria. All 44 unique subunits of the intact complex were identified by mass spectrometry. We identified differences in the subunit composition of subcomplexes of ovine complex I as compared with bovine, suggesting differential stability of inter-subunit interactions within the complex. Furthermore, the 42-kDa subunit, which is easily lost from the bovine enzyme, remains tightly bound to ovine complex I. Additionally, we developed a novel purification protocol for highly active and stable mitochondrial complex I using the branched-chain detergent lauryl maltose neopentyl glycol. Our data demonstrate that, although closely related, significant differences exist between the biochemical properties of complex I prepared from ovine and bovine mitochondria and that ovine complex I represents a suitable alternative target for further structural studies.Many products from the catabolic processing of monosaccharides, fatty acids, nucleotides, and amino acids are transported into the mitochondria, where their redox energy is harvested to synthesize ATP. The main process by which ATP is produced involves the five large membrane protein complexes of the oxidative phosphorylation electron transport chain (OXPHOS-ETC) 4 in the inner mitochondrial membrane (IMM) (1). NADH-ubiquinone oxidoreductase (complex I) is the first and largest of the OXPHOS-ETC complexes and couples the reduction of ubiquinone by NADH to the pumping of 4 H ϩ across the IMM (2-5). Together with the other protonpumping OXPHOS-ETC complexes, ubiquinol-cytochrome c oxidoreductase (complex III or the bc 1 complex) and cytochrome c oxidase (complex IV), complex I is responsible for building up a large proton electrochemical gradient that is then harvested by ATP synthase (complex V) for ATP production (1). Succinate-coenzyme Q reductase (complex II) is also a transmembrane protein complex and forms an integral part of the tricarboxylic acid cycle, but it only contributes to the membrane potential indirectly through reduction of the Q-pool (1).Although progress has been made in our understanding of the mechanism of the OXPHOS-ETC complexes, including high resolution structures of mammalian mitochondrial complexes II, III, and IV (6 ...

show abstract

Section: Sequence Comparisons For Mitochondrial Complex I Fromsupporting

confidence: 73%

Section: Sequence Comparisons For Mitochondrial Complex I Frommentioning

confidence: 99%

See 1 more Smart Citation

Purification of Ovine Respiratory Complex I Results in a Highly Active and Stable Preparation

Letts¹,

Degliesposti²,

Fiedorczuk³

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Cleaned sequences were aligned using the Cluster W algorithm included in program MEGA version 4.0 (Tamura et al, 2007) to identify different haplotypes. Ten sheep mtDNA control region reference sequences belonging to the five known haplogroups (Meadows et al, 2011) were also included in the analysis, to facilitate the recognition of haplogroup status of each individual (Table 2). A neighbour-joining (NJ) tree was constructed for identified haplotypes together with all reference sequences based on the Kimura 2-parameter model implemented in the program MEGA 4.0.…”

Section: Analysis Of Sequence Datamentioning

confidence: 99%

Mitochondrial DNA variation in indigenous sheep (Ovis aries) breeds of Nepal

Gorkhali

Han²,

2015

Trop. Agric. Res.

View full text Add to dashboard Cite

“…In a recent study Meadows et al (2011) analyzed complete mtDNA sequences from each haplogroup previously identified in domestic sheep, and from a sample of their wild relatives. Bayesian, maximum likelihood revealed that among various mtDNA components the control region is the more suitable to detect the true relationship between sheep.…”

Section: Box 7 High-throughput Snp Genotyping In Livestockmentioning

confidence: 99%