scholarly journals Cytochrome b diversity of Hungarian Botrytis cinerea strains

2010 ◽  
pp. 18-21
Author(s):  
Mojtaba Asadollahi ◽  
Éva Fekete ◽  
Erzsébet Fekete ◽  
Levente Karaffa ◽  
László Irinyi ◽  
...  
Keyword(s):  
Cytochrome B ◽  
Rational Design ◽  
Chain Complex ◽  
Grey Mould ◽  
Complex Iii ◽  
Control Programs ◽  
Plant Disease Control ◽  
Large Intron ◽  
Essential Components ◽  
Qoi Resistance

In the mitochondrion of eukaryotes, cytochrome b is a component of respiratory chain complex III. Cytochrome b is encoded by thecytochrome b (CYTB) gene located in the mitochondrial genome. The fungicidal activity of QoIs relies on their ability to inhibit mitochondrial respiration by binding at the so-called Qo site (the outer quinol-oxidation site) of the complex III. Since their introduction, QoIs (like azoxystrobin) have become essential components of plant disease control programs because of their wide-ranging efficacy against many agriculturally important fungal diseases like grey mould on various crops. QoI resistance primarily arises from a target-site-based mechanism involving mutations in the mitochondrial CYTB. As the management of grey mould is often dependent on chemicals, the rational design of control programs requires the information about the diversity of genes connected with resistance in field populations of the pathogen.Monospore B. cinerea field isolates has been collected during 2008-2009 from different hosts in Hungary. PCR fragment length analysisindicated the high frequency presence of type large intron in the isolates while in a few strains G143A substitution could also be detected.These results indicated the heterogeneity of CYTB in the Hungarian B. cinerea populations, which possibly involve the heteroplasmy of thismitochondrial gene, moreover indicates the existence op azoxystrobin resistant populations in Hungary.This work was supported by NKFP-A2-2006/0017 grant. Erzsébet Fekete is a grantee of the János Bolyai Scholarship (BO/00519/09/8).

The yeast CBP1 gene produces two differentially regulated transcripts by alternative 3'-end formation

1989 ◽  
Vol 9 (10) ◽  
pp. 4161-4169
Author(s):  
S A Mayer ◽  
C L Dieckmann
Keyword(s):  
Carbon Source ◽  
Cytochrome B ◽  
Mitochondrial Protein ◽  
Nuclear Gene ◽  
Chain Complex ◽  
Complex Iii ◽  
Yeast Cells ◽  
Transcriptional Level ◽  
Amino Acid Residues ◽  
Gene Encoding

CBP1 is a yeast nuclear gene encoding a mitochondrial protein that stabilizes the 5' end of cytochrome b (cob) pre-mRNA. Cytochrome b is the only mitochondrially synthesized component of the respiratory chain complex III. Since the nuclearly encoded subunits of this complex are regulated at the transcriptional level by catabolite repression, we hypothesized that CBP1 might be similarly regulated. To test the idea that transcriptional regulation of CBP1 could coordinate an increase in cytochrome b mRNA stability with an increase in nuclearly encoded complex III subunit production, we characterized the change in abundance of CBP1 mRNA during derepression on a nonfermentable carbon source. Poly(A)+ RNA from derepressed yeast cells was examined by Northern (RNA) analyses with cRNA probes from CBP1. Both 2.2- and 1.3-kilobase (kb) transcripts were detected. The 1.3-kb mRNA lacked approximately 900 nucleotides of the 3' end of the 2.2-kb mRNA, which encodes the carboxyl-terminal 250 amino acid residues of the CBP1 coding sequence. Northern analyses of RNA isolated from deletion-insertion mutants of CBP1 and from strains that overexpress CBP1 mRNA demonstrated that both mRNAs were transcribed from the CBP1 gene. Furthermore, we demonstrated that the levels of the two CBP1 mRNAs were reciprocally regulated by the carbon source in the growth medium. This is the first description of a yeast gene from which two transcripts that can encode proteins with distinctly different coding properties are generated by alternative 3'-end formation.

scholarly journals The yeast CBP1 gene produces two differentially regulated transcripts by alternative 3'-end formation.

1989 ◽  
Vol 9 (10) ◽  
pp. 4161-4169 ◽  
Author(s):  
S A Mayer ◽  
C L Dieckmann
Keyword(s):  
Carbon Source ◽  
Cytochrome B ◽  
Mitochondrial Protein ◽  
Nuclear Gene ◽  
Chain Complex ◽  
Complex Iii ◽  
Yeast Cells ◽  
Transcriptional Level ◽  
Amino Acid Residues ◽  
Gene Encoding

CBP1 is a yeast nuclear gene encoding a mitochondrial protein that stabilizes the 5' end of cytochrome b (cob) pre-mRNA. Cytochrome b is the only mitochondrially synthesized component of the respiratory chain complex III. Since the nuclearly encoded subunits of this complex are regulated at the transcriptional level by catabolite repression, we hypothesized that CBP1 might be similarly regulated. To test the idea that transcriptional regulation of CBP1 could coordinate an increase in cytochrome b mRNA stability with an increase in nuclearly encoded complex III subunit production, we characterized the change in abundance of CBP1 mRNA during derepression on a nonfermentable carbon source. Poly(A)+ RNA from derepressed yeast cells was examined by Northern (RNA) analyses with cRNA probes from CBP1. Both 2.2- and 1.3-kilobase (kb) transcripts were detected. The 1.3-kb mRNA lacked approximately 900 nucleotides of the 3' end of the 2.2-kb mRNA, which encodes the carboxyl-terminal 250 amino acid residues of the CBP1 coding sequence. Northern analyses of RNA isolated from deletion-insertion mutants of CBP1 and from strains that overexpress CBP1 mRNA demonstrated that both mRNAs were transcribed from the CBP1 gene. Furthermore, we demonstrated that the levels of the two CBP1 mRNAs were reciprocally regulated by the carbon source in the growth medium. This is the first description of a yeast gene from which two transcripts that can encode proteins with distinctly different coding properties are generated by alternative 3'-end formation.

scholarly journals Molecular Modeling and Docking Analysis Of Callosobruchus maculates Cytochrome B Proteins with Bio Active Compound Phytolfrom Glinus lotoides and Synthetic Pesticide Pirimiphos-Methyl

2017 ◽  
Vol 9 (6) ◽  
Author(s):  
Adline Jennefa Daniel ◽  
Gunasekaran C.
Keyword(s):  
Electron Transport ◽  
Cytochrome B ◽  
Chain Complex ◽  
Vital Role ◽  
Complex Iii ◽  
Docking Analysis ◽  
Transport Chain ◽  
Pirimiphos Methyl ◽  
Synthetic Pesticide ◽  
Molecular Modeling And Docking

Cytochrome b is a component of respiratory chain complex III, also known as bc1 complex or ubiquinol-cytochrome c reductase. These complexes are involved in electron transport and generation of ATP and thus play a vital role in electron transport chain. Phytol is a phytochemical derived from ethyl acetate extract of Glinus lotoides. Cytochrome b modeled and the structure was used for In-silico binding efficiency and comparative analysis of cytochrome b with Phytol and synthetic pesticide were showed good docking score and binding affinity when compared to control. This study will be used in broad screening of the protein in the respiratory process and can be further implemented in designing pest control.

scholarly journals AB0031 T HELPER 17 CELLS WERE SIGNIFICANTLY DECREASED BY MITOCHONDRIAL ELECTRON TRANSPORT CHAIN COMPLEX INHIBITOR IN PATIENTS WITH RHEUMATOID ARTHRITIS

2020 ◽  
Vol 79 (Suppl 1) ◽  
pp. 1318.2-1318
Author(s):  
H. R. Lee ◽  
S. J. Yoo ◽  
J. Kim ◽  
I. S. Yoo ◽  
C. K. Park ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Electron Transport ◽  
Disease Activity ◽  
Th17 Cells ◽  
Electron Transport Chain ◽  
Chain Complex ◽  
Complex Iii ◽  
Mitochondrial Electron Transport Chain ◽  
Transport Chain ◽  
Healthy Control

Background:Reactive oxygen species (ROS) and T helper 17 (TH17) cells have been known to play an important role in the pathogenesis of rheumatoid arthritis (RA). However, the interrelationship between ROS and TH17 remains unclear in RAObjectives:To explore whether ROS affect TH17 cells in peripheral blood mononuclear cells (PBMC) of RA patients, we analyzed ROS expressions among T cell subsets following treatment with mitochondrial electron transport chain complex inhibitors.Methods:Blood samples were collected from 40 RA patients and 10 healthy adult volunteers. RA activity was divided according to clinical parameter DAS28. PBMC cells were obtained from the whole blood using lymphocyte separation medium density gradient centrifugation. Following PBMC was stained with Live/Dead stain dye, cells were incubated with antibodies for CD3, CD4, CD8, and CD25. After fixation and permeabilization, samples were stained with antibodies for FoxP3 and IL-17A. MitoSox were used for mitochondrial specific staining.Results:The frequency of TH17 cells was increased by 4.83 folds in moderate disease activity group (5.1>DAS28≥3.2) of RA patients compared to healthy control. Moderate RA activity patients also showed higher ratio of TH17/Treg than healthy control (3.57 folds). All RA patients had elevated expression of mitochondrial specific ROS than healthy control. When PBMC cells were treated with 2.5uM of antimycin A (mitochondrial electron transport chain complex III inhibitor) for 16 h, the frequency of TH17 cells was significantly decreased.Conclusion:The mitochondrial electron transport chain complex III inhibitor markedly downregulated the frequency of TH17 cells in moderate disease activity patients with RA. These findings provide a novel approach to regulate TH17 function in RA through mitochondrial metabolism related ROS production.References:[1]Szekanecz, Z., et al., New insights in synovial angiogenesis. Joint Bone Spine, 2010. 77(1): p. 13-9.[2]Prevoo, M.L., et al., Modified disease activity scores that include twenty-eight-joint counts. Development and validation in a prospective longitudinal study of patients with rheumatoid arthritis. Arthritis Rheum, 1995. 38(1): p. 44-8.Disclosure of Interests:None declared

scholarly journals NAD + repletion produces no therapeutic effect in mice with respiratory chain complex III deficiency and chronic energy deprivation

2018 ◽  
Vol 32 (11) ◽  
pp. 5913-5926 ◽  
Author(s):  
Janne Purhonen ◽  
Jayasimman Rajendran ◽  
Saara Tegelberg ◽  
Olli-Pekka Smolander ◽  
Eija Pirinen ◽  
...  
Keyword(s):  
Therapeutic Effect ◽  
Respiratory Chain ◽  
Chain Complex ◽  
Complex Iii ◽  
Respiratory Chain Complex ◽  
Energy Deprivation

scholarly journals Assembly factors monitor sequential hemylation of cytochrome b to regulate mitochondrial translation

2014 ◽  
Vol 205 (4) ◽  
pp. 511-524 ◽  
Author(s):  
Markus Hildenbeutel ◽  
Eric L. Hegg ◽  
Katharina Stephan ◽  
Steffi Gruschke ◽  
Brigitte Meunier ◽  
...  
Keyword(s):  
Electron Transport ◽  
Cytochrome B ◽  
Mitochondrial Respiratory Chain ◽  
Complex Iii ◽  
Mitochondrial Translation ◽  
Respiratory Chain Complexes ◽  
Mitochondrial Inner Membrane ◽  
Sequence Of Events ◽  
Chain Complexes ◽  
Assembly Factors

Mitochondrial respiratory chain complexes convert chemical energy into a membrane potential by connecting electron transport with charge separation. Electron transport relies on redox cofactors that occupy strategic positions in the complexes. How these redox cofactors are assembled into the complexes is not known. Cytochrome b, a central catalytic subunit of complex III, contains two heme bs. Here, we unravel the sequence of events in the mitochondrial inner membrane by which cytochrome b is hemylated. Heme incorporation occurs in a strict sequential process that involves interactions of the newly synthesized cytochrome b with assembly factors and structural complex III subunits. These interactions are functionally connected to cofactor acquisition that triggers the progression of cytochrome b through successive assembly intermediates. Failure to hemylate cytochrome b sequesters the Cbp3–Cbp6 complex in early assembly intermediates, thereby causing a reduction in cytochrome b synthesis via a feedback loop that senses hemylation of cytochrome b.

scholarly journals Mutations in CYC1, Encoding Cytochrome c1 Subunit of Respiratory Chain Complex III, Cause Insulin-Responsive Hyperglycemia

2013 ◽  
Vol 93 (2) ◽  
pp. 384-389 ◽  
Author(s):  
Pauline Gaignard ◽  
Minal Menezes ◽  
Manuel Schiff ◽  
Aurélien Bayot ◽  
Malgorzata Rak ◽  
...  
Keyword(s):  
Respiratory Chain ◽  
Chain Complex ◽  
Complex Iii ◽  
Respiratory Chain Complex ◽  
Cytochrome C1

scholarly journals Potential of Mitochondria-Targeted Antioxidants to Prevent Oxidative Stress in Pancreatic β-cells

2019 ◽  
Vol 2019 ◽  
pp. 1-16 ◽  
Author(s):  
Lydie Plecitá-Hlavatá ◽  
Hana Engstová ◽  
Jan Ježek ◽  
Blanka Holendová ◽  
Jan Tauber ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Pancreatic Islets ◽  
Targeted Delivery ◽  
Complex I ◽  
Chain Complex ◽  
Redox Signaling ◽  
Complex Iii ◽  
Mitochondrial Matrix ◽  
Isolated Pancreatic Islets ◽  
Superoxide Formation

Pancreatic β-cells are vulnerable to oxidative stress due to their low content of redox buffers, such as glutathione, but possess a rich content of thioredoxin, peroxiredoxin, and other proteins capable of redox relay, transferring redox signaling. Consequently, it may be predicted that cytosolic antioxidants could interfere with the cytosolic redox signaling and should not be recommended for any potential therapy. In contrast, mitochondrial matrix-targeted antioxidants could prevent the primary oxidative stress arising from the primary superoxide sources within the mitochondrial matrix, such as at the flavin (IF) and ubiquinone (IQ) sites of superoxide formation within respiratory chain complex I and the outer ubiquinone site (IIIQ) of complex III. Therefore, using time-resolved confocal fluorescence monitoring with MitoSOX Red, we investigated various effects of mitochondria-targeted antioxidants in model pancreatic β-cells (insulinoma INS-1E cells) and pancreatic islets. Both SkQ1 (a mitochondria-targeted plastoquinone) and a suppressor of complex III site Q electron leak (S3QEL) prevented superoxide production released to the mitochondrial matrix in INS-1E cells with stimulatory glucose, where SkQ1 also exhibited an antioxidant role for UCP2-silenced cells. SkQ1 acted similarly at nonstimulatory glucose but not in UCP2-silenced cells. Thus, UCP2 can facilitate the antioxidant mechanism based on SkQ1+ fatty acid anion- pairing. The elevated superoxide formation induced by antimycin A was largely prevented by S3QEL, and that induced by rotenone was decreased by SkQ1 and S3QEL and slightly by S1QEL, acting at complex I site Q. Similar results were obtained with the MitoB probe, for the LC-MS-based assessment of the 4 hr accumulation of reactive oxygen species within the mitochondrial matrix but for isolated pancreatic islets. For 2 hr INS-1E incubations, some samples were influenced by the cell death during the experiment. Due to the frequent dependency of antioxidant effects on metabolic modes, we suggest a potential use of mitochondria-targeted antioxidants for the treatment of prediabetic states after cautious nutrition-controlled tests. Their targeted delivery might eventually attenuate the vicious spiral leading to type 2 diabetes.

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