The 18-kD Protein That Binds to the Chloroplast DNA Replicative Origin Is an Iron-Sulfur Protein Related to a Subunit of NADH Dehydrogenase

1989 ◽  
Vol 1 (5) ◽  
pp. 551 ◽  
Author(s):  
Madeline Wu ◽  
Z. Q. Nie ◽  
Junming Yang
Keyword(s):  
Chloroplast Dna ◽  
Nadh Dehydrogenase ◽  
Iron Sulfur ◽  
A Subunit ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

scholarly journals Higher NDUFS8 Serum Levels Correlate with Better Insulin Sensitivity in Type 1 Diabetes

2021 ◽  
Author(s):  
Justyna Flotyńska ◽  
Daria Klause ◽  
Michał Kulecki ◽  
Aleksandra Cieluch ◽  
Martyna Pakuła ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Insulin Sensitivity ◽  
Serum Concentration ◽  
Mitochondrial Function ◽  
Nadh Dehydrogenase ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Protein Serum

Abstract Aim: The aim of the study was to evaluate the function of Complex I by measuring NADH dehydrogenase [ubiquinone] iron-sulfur protein 8 serum level and the relationship with insulin resistance in type 1 diabetes. T1DM causes adverse changes in the mitochondria, which can influence the development of chronic complications. The NADH dehydrogenase [ubiquinone] iron-sulfur protein 8 (NDUFS8 protein) is a subunit of NADH dehydrogenase and plays an important role in the mitochondrial function. NDUFS8 serum concentration probably reflects the function of mitochondria. Methods: All of 36 people suffer from T1DM. All participants were treated with functional intensive insulin therapy. NDUFS8 protein serum concentration was measured using the ELISA test. Insulin resistance was evaluated with indirect marker estimated glucose disposal rate (eGDR). The group was divided on the base of median value of eGDR (higher eGDR – less IR). Results: The study group consisted of 12 women and 24 men, aged 39.5 (28.0-46.5) years with the duration of the disease 22 (15-26) years. Medians of eGDR and NDUFS8 protein concentration were 7.6 (5.58-8.99) mg/kg/min and 2.25 (0.72-3.81) ng/ml, respectively. The group with higher insulin sensitivity had higher NDUFS8 protein serum concentration, lower WHR, BMI and they were younger. A negative correlation was observed between NDUFS8 protein serum concentration and WHR (rs=-0.35,p=0.03), whereas a positive correlation was observed between NDUFS8 protein serum concentration and eGDR (rs=0.43,p=0.008). Multivariate linear regression confirmed a significant association between insulin sensitivity and better mitochondrial function (beta=0.54,p=0.003), independent of age, duration of diabetes and smoking. Conclusions: Higher NDUFS8 protein serum concentration is associated with higher insulin sensitivity among people with T1DM and might reflects better mitochondrial function.

Maxicircle CR1 transcripts of Trypanosoma brucei are edited and developmentally regulated and encode a putative iron-sulfur protein homologous to an NADH dehydrogenase subunit

1992 ◽  
Vol 12 (5) ◽  
pp. 2100-2107
Author(s):  
A E Souza ◽  
P J Myler ◽  
K Stuart
Keyword(s):  
Trypanosoma Brucei ◽  
Nadh Dehydrogenase ◽  
Developmental Regulation ◽  
Developmentally Regulated ◽  
Reading Frame ◽  
Guide Rnas ◽  
Iron Sulfur ◽  
Mitochondrial Dnas ◽  
A Subunit ◽  
Sulfur Protein

The maxicircle of Trypanosoma brucei encodes components of the mitochondrial oxidative phosphorylation system, as do other mitochondrial DNAs, but maxicircle gene identification is complicated by extensive editing of some transcripts. We found that transcripts from the CR1 region were extensively edited, as are other transcripts from maxicircle regions which exhibit strong G versus C strand bias. Editing added 259 uridines and removed 46 uridines to produce an approximately 574-nucleotide mature mRNA. Partially edited cDNAs and potential guide RNAs were also characterized. Initiation and termination codons were created, and they defined an open reading frame encoding a predicted protein of 145 amino acids. This protein contains two iron-sulfur cysteine motifs and is homologous to a subunit of NADH dehydrogenase and to other electron-carrier proteins. Higher levels of both edited and unedited CR1 transcripts accumulated in bloodstream forms of the parasite than in procyclic forms, suggesting developmental regulation of CR1 gene expression.

Cloning and sequencing of a cDNA encoding the precursor to the 24 kDa iron-sulfur protein of human mitochondrial NADH dehydrogenase

1989 ◽  
Vol 21 (10) ◽  
pp. 1161-1168 ◽  
Author(s):  
Toda Haruo ◽  
Hosokawa Yoshitaka ◽  
Nishikimi Morimitsu ◽  
Suzuki Hiroshi ◽  
Kato Katsumi ◽  
...  
Keyword(s):  
Nadh Dehydrogenase ◽  
Cloning And Sequencing ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

scholarly journals Proteomic Analysis of Peroxynitrite-Induced Protein Nitration in Isolated Beef Heart Mitochondria

2018 ◽  
pp. 239-250 ◽  
Author(s):  
M. KOHUTIAR ◽  
A. ECKHARDT ◽  
I. MIKŠÍK ◽  
P. ŠANTOROVÁ ◽  
J. WILHELM
Keyword(s):  
Atp Synthase ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
2D Electrophoresis ◽  
Beef Heart ◽  
Protein Nitration ◽  
Iron Sulfur ◽  
Beef Heart Mitochondria ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

Mitochondria are exposed to reactive nitrogen species under physiological conditions and even more under several pathologic states. In order to reveal the mechanism of these processes we studied the effects of peroxynitrite on isolated beef heart mitochondria in vitro. Peroxynitrite has the potential to nitrate protein tyrosine moieties, break the peptide bond, and eventually release the membrane proteins into the solution. All these effects were found in our experiments. Mitochondrial proteins were resolved by 2D electrophoresis and the protein nitration was detected by immunochemical methods and by nano LC-MS/MS. Mass spectrometry confirmed nitration of ATP synthase subunit beta, pyruvate dehydrogenase E1 component subunit beta, citrate synthase and acetyl-CoA acetyltransferase. Immunoblot detection using chemiluminiscence showed possible nitration of other proteins such as cytochrome b-c1 complex subunit 1, NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, elongation factor Tu, NADH dehydrogenase [ubiquinone] flavoprotein 2, heat shock protein beta-1 and NADH dehydrogenase [ubiquinone] iron-sulfur protein 8. ATP synthase beta subunit was nitrated both in membrane and in fraction prepared by osmotic lysis. The high sensitivity of proteins to nitration by peroxynitrite is of potential biological importance, as these enzymes are involved in various pathways associated with energy production in the heart.

scholarly journals Maxicircle CR1 transcripts of Trypanosoma brucei are edited and developmentally regulated and encode a putative iron-sulfur protein homologous to an NADH dehydrogenase subunit.

1992 ◽  
Vol 12 (5) ◽  
pp. 2100-2107 ◽  
Author(s):  
A E Souza ◽  
P J Myler ◽  
K Stuart
Keyword(s):  
Trypanosoma Brucei ◽  
Nadh Dehydrogenase ◽  
Developmental Regulation ◽  
Developmentally Regulated ◽  
Reading Frame ◽  
Guide Rnas ◽  
Iron Sulfur ◽  
Mitochondrial Dnas ◽  
A Subunit ◽  
Sulfur Protein

The maxicircle of Trypanosoma brucei encodes components of the mitochondrial oxidative phosphorylation system, as do other mitochondrial DNAs, but maxicircle gene identification is complicated by extensive editing of some transcripts. We found that transcripts from the CR1 region were extensively edited, as are other transcripts from maxicircle regions which exhibit strong G versus C strand bias. Editing added 259 uridines and removed 46 uridines to produce an approximately 574-nucleotide mature mRNA. Partially edited cDNAs and potential guide RNAs were also characterized. Initiation and termination codons were created, and they defined an open reading frame encoding a predicted protein of 145 amino acids. This protein contains two iron-sulfur cysteine motifs and is homologous to a subunit of NADH dehydrogenase and to other electron-carrier proteins. Higher levels of both edited and unedited CR1 transcripts accumulated in bloodstream forms of the parasite than in procyclic forms, suggesting developmental regulation of CR1 gene expression.

scholarly journals Proteomic Analysis of Peroxynitrite-Induced Protein Nitration in Isolated Beef Heart Mitochondria

2018 ◽  
pp. 239-250 ◽  
Author(s):  
M. KOHUTIAR ◽  
A. ECKHARDT ◽  
I. MIKŠÍK ◽  
P. ŠANTOROVÁ ◽  
J. WILHELM
Keyword(s):  
Atp Synthase ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
2D Electrophoresis ◽  
Beef Heart ◽  
Protein Nitration ◽  
Iron Sulfur ◽  
Beef Heart Mitochondria ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

Mitochondria are exposed to reactive nitrogen species under physiological conditions and even more under several pathologic states. In order to reveal the mechanism of these processes we studied the effects of peroxynitrite on isolated beef heart mitochondria in vitro. Peroxynitrite has the potential to nitrate protein tyrosine moieties, break the peptide bond, and eventually release the membrane proteins into the solution. All these effects were found in our experiments. Mitochondrial proteins were resolved by 2D electrophoresis and the protein nitration was detected by immunochemical methods and by nano LC-MS/MS. Mass spectrometry confirmed nitration of ATP synthase subunit beta, pyruvate dehydrogenase E1 component subunit beta, citrate synthase and acetyl-CoA acetyltransferase. Immunoblot detection using chemiluminiscence showed possible nitration of other proteins such as cytochrome b-c1 complex subunit 1, NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, elongation factor Tu, NADH dehydrogenase [ubiquinone] flavoprotein 2, heat shock protein beta-1 and NADH dehydrogenase [ubiquinone] iron-sulfur protein 8. ATP synthase beta subunit was nitrated both in membrane and in fraction prepared by osmotic lysis. The high sensitivity of proteins to nitration by peroxynitrite is of potential biological importance, as these enzymes are involved in various pathways associated with energy production in the heart.

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