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Cytb1-1-Ascorbate metabolism in plants: physiological function and biochemical properties of cytochrome b561

ABSTRACT: What is the physiological function of cytochrome b561 in Arabidopsis thaliana - We want to check which possible changes occur in gene expression by knocking out the AtCytb1 gene. au08-01_cytb561 - cytb1-1 Keywords: gene knock out

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE19739 | GEO | 2010/04/01

SECONDARY ACCESSION(S): PRJNA122203

REPOSITORIES: GEO

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Cytb1-1-Ascorbate metabolism in plants: physiological function and biochemical properties of cytochrome b561

Project description:What is the physiological function of cytochrome b561 in Arabidopsis thaliana - We want to check which possible changes occur in gene expression by knocking out the AtCytb1 gene. au08-01_cytb561 - cytb1-1 Keywords: gene knock out 4 dye-swap - CATMA arrays

2010-03-31 | E-GEOD-19739 | biostudies-arrayexpress

ccme-The cytochrome pathway and cytochrome C biogenesis

Project description:rs04-01_cytc - ccme - Is there a retrograde regulation of mitochondrial cytochrome pathway ? - The homozygote arabidopsis line 9S9 overproducing AtCCME-HIS (At3g1790), a mitochondrial heme chaperon involved in c-type cytochrome maturation will be compared with the corresponding wild type (Wassilievskjia). Keywords: gene knock in (transgenic)

2007-06-20 | GSE7995 | GEO

antimycine a-The cytochrome pathway and cytochrome C biogenesis

Project description:rs04-01_cytc - antimycine a - Is there a retrograde regulation of mitochondrial cytochrome pathway ? - Presence of an inhibitor of the cytochrome pathway (antimycine A). This treatment induces the expression of a gene coding for an alternative oxydase (AOX1a) and one of the two genes coding for apocytochrome c (CYTc-a). Keywords: treated vs untreated comparison

2007-06-20 | GSE7994 | GEO

Transcriptional response of Mycobacterium tuberculosis to inhibition of Cytochrome bd oxidase and Cytochrome bcc:aa3 oxidase

Project description:Comparative analysis of the transcriptional response, as quantified by RNA-Seq, of Mycobacterium tuberculosis (Mtb) during inhibition of the terminal cytochrome oxidases, Cytochrome bd oxidase and Cytochrome bcc:aa3. This study was designed to evaluate the efficacy if a novel small molecule inhibitor of the Cytochrome bd oxidase. Specifically, we compared the transcriptional response of Mtb during inhibition by Q203 with a Cytochrome bd deletion mutant to the transcriptional response of Mtb treated with a combination of Q203 and the purported Cytorchomre bd small molecule inhibitor (ND-011992).

2020-10-07 | GSE159080 | GEO

The unusual properties of the photosynthetic cytochrome c550 from the red algal lineage evidence additional biological roles

Project description:Cytochrome c550 is an extrinsic component in the luminal side of photosystem II in cyanobacteria, as well as in eukaryotic algae from the red photosynthetic lineage including, among others, diatoms. By using strong and specific protease inhibitors we have confirmed that cytochrome c550 from the diatom Phaeodactylum tricornutum is expressed as a truncated form lacking the last hydrophobic residues at the C-terminal.. Phaeodactylum tricornutum cytochrome c550 seems to be modified at a post-translational level as the gene is appropriately transcribed. In addition, co-immunoprecipitation and mass spectrometry experiments have allowed the identification of novel interactions of Phaeodactylum tricornutum cytochrome c550 with proteins related to the CO2 concentrating mechanism and assimilation located in the chloroplast pyrenoid. Furthermore, immunoelectron microscopy analysis indicates that although cytochrome c550 is mainly located in the thylakoid domain of the chloroplast, it can also be found in the pyrenoid. The results are interpreted in terms of a specific protein modification associated to a higher PSII turnover or to new alternative functions of the heme protein, maybe related to carbon fixation.

2022-03-03 | PXD008763 | Pride

Transcriptional response of Mycobacterium tuberculosis to inhibition of Cytochrome bd oxidase and Cytochrome bcc:aa3 oxidase

Project description:Transcriptional response of Mycobacterium tuberculosis to inhibition of Cytochrome bd oxidase and Cytochrome bcc:aa3 oxidase

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Biochemical and physiological properties of K+ channel-associated AKR6A (Kvβ) proteins.

Project description:Voltage-gated potassium (Kv) channels play an essential role in the regulation of membrane excitability and thereby control physiological processes such as cardiac excitability, neural communication, muscle contraction, and hormone secretion. Members of the Kv1 and Kv4 families are known to associate with auxiliary intracellular Kvβ subunits, which belong to the aldo-keto reductase superfamily. Electrophysiological studies have shown that these proteins regulate the gating properties of Kv channels. Although the three gene products encoding Kvβ proteins are functional enzymes in that they catalyze the nicotinamide adenine dinucleotide phosphate (NAD[P]H)-dependent reduction of a wide range of aldehyde and ketone substrates, the physiological role for these proteins and how each subtype may perform unique roles in coupling membrane excitability with cellular metabolic processes remains unclear. Here, we discuss current knowledge of the enzymatic properties of Kvβ proteins from biochemical studies with their described and purported physiological and pathophysiological influences.

| S-EPMC6584034 | biostudies-literature

Biochemical Properties and Physiological Functions of pLG72: Twenty Years of Investigations.

Project description:In 2002, the novel human gene G72 was associated with schizophrenia susceptibility. This gene encodes a small protein of 153 amino acids, named pLG72, which represents a rare case of primate-specific protein. In particular, the rs2391191 single nucleotide polymorphism (resulting in in the R30K substitution) was robustly associated to schizophrenia and bipolar disorder. In this review, we aim to summarize the results of 20 years of biochemical investigations on pLG72. The main known role of pLG72 is related to its ability to bind and inactivate the flavoenzyme d-amino acid oxidase, i.e., the enzyme that controls the catabolism of d-serine, the main NMDA receptor coagonist in the brain. pLG72 was proposed to target the cytosolic form of d-amino acid oxidase for degradation, preserving d-serine and protecting the cell from oxidative stress generated by hydrogen peroxide produced by the flavoenzyme reaction. Anyway, pLG72 seems to play additional roles, such as affecting mitochondrial functions. The level of pLG72 in the human body is still a controversial issue because of its low expression and challenging detection. Anyway, the intriguing hypothesis that pLG72 level in blood could represent a suitable marker of Alzheimer's disease progression (a suggestion not sufficiently established yet) merits further investigations.

| S-EPMC9220908 | biostudies-literature

Engineering ascorbate peroxidase activity into cytochrome c peroxidase.

Project description:Cytochrome c peroxidase (CCP) and ascorbate peroxidase (APX) have very similar structures, and yet neither CCP nor APX exhibits each other's activities with respect to reducing substrates. APX has a unique substrate binding site near the heme propionates where ascorbate H-bonds with a surface Arg and one heme propionate (Sharp et al. (2003) Nat. Struct. Biol. 10, 303-307). The corresponding region in CCP has a much longer surface loop, and the critical Arg residue that is required for ascorbate binding in APX is Asn in CCP. In order to convert CCP into an APX, the ascorbate-binding loop and critical arginine were engineered into CCP to give the CCP2APX mutant. The mutant crystal structure shows that the engineered site is nearly identical to that found in APX. While wild-type CCP shows no APX activity, CCP2APX catalyzes the peroxidation of ascorbate at a rate of approximately 12 min (-1), indicating that the engineered ascorbate-binding loop can bind ascorbate.

| S-EPMC2770236 | biostudies-literature

Evidence for a key role of cytochrome bo3 oxidase in respiratory energy metabolism of Gluconobacter oxydans

Project description:The obligatory aerobic acetic acid bacterium Gluconobacter oxydans oxidizes a variety of substrates in the periplasm by membrane-bound dehydrogenases, which transfer the reducing equivalents to ubiquinone. Two quinol oxidases, cytochrome bo3 and cytochrome bd, then catalyze transfer of the electrons from ubiquinol to molecular oxygen. In this study, mutants lacking either of these terminal oxidases were characterized. Deletion of the cydAB genes for cytochrome bd had no obvious influence on growth, whereas the lack of the cyoBACD genes for cytochrome bo3 severely reduced the growth rate and the cell yield. Using a respiration activity monitoring system and adjusting different levels of oxygen availability, hints for a low oxygen affinity of cytochrome bd oxidase were obtained, which were supported by measurements of oxygen consumption in a respirometer. The H+/O ratio of the ΔcyoBACD mutant with mannitol as substrate was 0.56 ± 0.11 and more than 50% lower than that of the reference strain (1.26 ± 0.06) and the delta-cydAB mutant (1.31 ± 0.16), indicating that cytochrome bo3 oxidase is the main component for proton extrusion via the respiratory chain. Plasmid-based overexpression of cyoBACD led to increased growth rates and growth yields, both in the wild type and the delta-cyoBACD mutant, suggesting that cytochrome bo3 might be the rate-limiting factor of the respiratory chain.

2013-07-26 | GSE47782 | GEO

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