The 110kDa glutathione transferase of Yarrowia lipolytica is encoded by a homologue of the TEF3 gene from Saccharomyces cerevisiae: Cloning, expression, and homology modeling of the recombinant protein

McGoldrick, Shane; McCarthy, Tommie V.; Sheehan, David

doi:10.1016/j.bbrc.2005.09.162

Cited by 3 publications

(1 citation statement)

References 44 publications

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“…The N-terminal domain of eEF1Bg has sequence motifs characteristic of the Theta class of glutathione transferases (GSTs) (48), enzymes that catalyse conjugation of electrophillic compounds to glutathione (GSH) (91). However, the GST domain of eEF1Bg purified from diverse plant and microbial species does not show any GST activity with the model substrate 1-chloro-2,4-dintrobenzene (63). A link with oxidative stress has been demonstrated since yeast mutants lacking either of two nonidentical eEF1Bg subunits (Tef3, Tef4) are resistant to oxidative stress conditions, including exposure to H 2 O 2 (75).…”

Section: Grantmentioning

confidence: 98%

Regulation of Translation by Hydrogen Peroxide

Grant

2011

Antioxidants & Redox Signaling

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Cells must be able to maintain their intracellular homeostasis in the face of changing conditions. Typically, they respond by invoking complex regulatory mechanisms, including a global inhibition of translation. This reduction in protein synthesis may prevent continued gene expression during potentially error-prone conditions as well as allow for the turnover of existing mRNAs and proteins, whilst gene expression is directed toward the production of new molecules required to protect against or detoxify the stress. However, it is becoming increasingly recognized that not all translation is inhibited and translational control of specific mRNAs is required for survival under stress conditions. Control of protein levels via translational regulation offers a significant advantage to the cell due to the immediacy of the regulatory effect. This review describes how protein synthesis is regulated in response to oxidative stress conditions induced by exposure to hydrogen peroxide. Translational control can be mediated via direct oxidative regulation of translation factors as well via mRNA-specific regulatory mechanisms. Additionally, increasing evidence suggests that oxidative damage to the translational apparatus can itself alter the proteomic output. The resulting translational reprogramming is fundamental for adaptation to the oxidative stress.

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Section: Grantmentioning

confidence: 98%

Regulation of Translation by Hydrogen Peroxide

Grant

2011

Antioxidants & Redox Signaling

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Current awareness on yeast

2006

Yeast

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In order to keep subscribers up‐to‐date with the latest developments in their field, this current awareness service is provided by John Wiley & Sons and contains newly‐published material on yeasts. Each bibliography is divided into 10 sections. 1 Books, Reviews & Symposia; 2 General; 3 Biochemistry; 4 Biotechnology; 5 Cell Biology; 6 Gene Expression; 7 Genetics; 8 Physiology; 9 Medical Mycology; 10 Recombinant DNA Technology. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted. (4 weeks journals ‐ search completed 10th. Mar. 2006)

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Identification of an elongation factor 1Bγ protein with glutathione transferase activity in both yeast and mycelial morphologies from human pathogenic Blastoschizomyces capitatus

et al. 2013

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Blastoschizomyces capitatus is an uncommon, opportunistic pathogenic fungus, which causes invasive and disseminated infections. This microorganism is normally present in both environmental and normal human flora. Within a host, B. capitatus is able to grow in both unicellular yeast and multicellular filamentous growth forms. In this study, we obtained in vitro morphological conversion of B. capitatus from yeast-to-mycelial phase to investigate the presence and expression of glutathione transferase (GST) enzymes in both cell forms. A protein with GST activity using the model substrate 1-chloro-2,4-dinitrobenzene was detected in both morphologies and identified by tandem mass spectrometry as a eukaryotic elongation factor 1Bγ (eEF1Bγ) protein, a member of the GST superfamily. No significant difference in GST-specific activity and kinetic constants were observed between mycelial and yeast forms, indicating that eEF1Bγ protein did not show differential expression between the two phases.

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The 110kDa glutathione transferase of Yarrowia lipolytica is encoded by a homologue of the TEF3 gene from Saccharomyces cerevisiae: Cloning, expression, and homology modeling of the recombinant protein

Cited by 3 publications

References 44 publications

Regulation of Translation by Hydrogen Peroxide

Regulation of Translation by Hydrogen Peroxide

Current awareness on yeast

Identification of an elongation factor 1Bγ protein with glutathione transferase activity in both yeast and mycelial morphologies from human pathogenic Blastoschizomyces capitatus

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