Peroxisomal Localization of MN Sod Enzyme in<i>Saccharomyces Cerevisiae</i>Yeasts:<i>In Silico</i>Analysis

Petrova, Ventsislava Yankova; Uzunov, Zlatyo; Kujumdzieva, Anna

doi:10.2478/v10133-009-0023-5

Cited by 6 publications

(1 citation statement)

References 35 publications

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“…Certain data about migration of SOD enzymes trough different compartments in methilotrophic yeast have been already reported by other authors Nedeva et al (23), after electrophoretical visualization of SOD patterns, provided evidence for possible migration of cytosolic Cu/Zn SOD to mitochondria in several fermentative and respiratory yeast species. As regards the Mn SOD enzyme, besides its typical subcellular localization -mitochondrial matrix, recently it was shown that it could be also successively targeted to yeast peroxisomes (27). In S. cerevisiae amino acid sequence of Mn SOD enzyme (Sod2p) was analyzed and two possible subcellular localizations were identified -mitochondrial and peroxisomal.…”

Section: Visualization Of Sods In Cell Free Extract Of H Polymorpha mentioning

confidence: 99%

Superoxide Dismutase Enzymes in Oxidative Type YeastH. Polymorpha

Koleva

Docheva

Petrova

et al. 2010

Biotechnology & Biotechnological Equipment

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Hansenula polymorpha CBS 4732, cultivated on media containing glucose, glycerol or methanol as carbon source has been investigated for specific activity of Superoxide dismutase (SOD) enzymes during batch -wise cultivation. Furthermore cell free extract from the analyzed strain cultivated on different carbon sources were subjected to 8% native PAGE. One band corresponding to sensitive of KCN Cu/Zn SOD with Rm 0.29 is inhibiting in all samples. After inhibition of cyanide sensitive Cu/Zn SOD, three bands specifically stained for SOD activity, corresponding to Mn SOD are observed in samples obtained by H. polymorpha cultivated on medium containing methanol. Two bans are retaining in glucose and glycerol grown cells. This data suggest that probably in H. polymorpha yeasts appears multiple enzyme forms of Mn SOD enzyme. Multiple enzyme forms become more stable and do not disappear after 1 min at 75°C. One band with Rm 0.34 in all yeast samples cultivated on methanol, glucose and glycerol, remains till heating at 75°C for 10 minutes.

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Section: Visualization Of Sods In Cell Free Extract Of H Polymorpha mentioning

confidence: 99%

Superoxide Dismutase Enzymes in Oxidative Type YeastH. Polymorpha

Koleva

Docheva

Petrova

et al. 2010

Biotechnology & Biotechnological Equipment

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Plant Peroxisomes and Their Metabolism of ROS, RNS, and RSS

Rı́o

2020

Progress in Botany

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Role of Peroxisomes as a Source of Reactive Oxygen Species (ROS) Signaling Molecules

Sandalio

Rodríguez‐Serrano

Romero‐Puertas

et al. 2013

Subcellular Biochemistry

142

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Peroxisomes are very dynamic and metabolically active organelles and are a very important source of reactive oxygen species (ROS), H2O2, O2 (.-) and · OH, which are mainly produced in different metabolic pathways, including fatty acid β-oxidation, photorespiration, nucleic acid and polyamine catabolism, ureide metabolism, etc. ROS were originally associated to oxygen toxicity; however, these reactive species also play a central role in the signaling network regulating essential processes in the cell. Peroxisomes have the capacity to rapidly produce and scavenge H2O2 and O2 (.-) which allows to regulate dynamic changes in ROS levels. This fact and the plasticity of these organelles, which allows adjusting their metabolism depending on different developmental and environmental cues, makes these organelles play a central role in cellular signal transduction. The use of catalase and glycolate oxidase loss-of-function mutants has allowed to study the consequences of changes in the levels of endogenous H2O2 in peroxisomes and has improved our knowledge of the transcriptomic profile of genes regulated by peroxisomal ROS. It is now known that peroxisomal ROS participate in more complex signaling networks involving calcium, hormones, and redox homeostasis which finally determine the response of plants to their environment.

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Peroxisomal Localization of MN Sod Enzyme inSaccharomyces CerevisiaeYeasts:In SilicoAnalysis

Cited by 6 publications

References 35 publications

Superoxide Dismutase Enzymes in Oxidative Type YeastH. Polymorpha

Superoxide Dismutase Enzymes in Oxidative Type YeastH. Polymorpha

Plant Peroxisomes and Their Metabolism of ROS, RNS, and RSS

Role of Peroxisomes as a Source of Reactive Oxygen Species (ROS) Signaling Molecules

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