The significance of peroxisomes in methanol metabolism in methylotrophic yeast

Klei, Ida J. van der; Yurimoto, Hiroya; Sakai, Yasuyoshi; Veenhuis, Marten

doi:10.1016/j.bbamcr.2006.07.016

Cited by 173 publications

(116 citation statements)

References 66 publications

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“…Adaptation of glucose-grown P. pastoris cells to methanol medium leads to a great increase in the number and size of peroxisomes (van der Klei et al, 2006). In this study, we observed a morphological change in the vacuole during the methanol adaptation period.…”

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confidence: 52%

Atg8 regulates vacuolar membrane dynamics in a lipidation-independent manner in Pichia pastoris

Tamura¹,

Oku²,

Sakai³

2010

Development

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ResultsDeletion of ATG8 results in abnormal vacuolar shape P. pastoris can use methanol as the sole carbon and energy source. Adaptation of glucose-grown P. pastoris cells to methanol medium leads to a great increase in the number and size of peroxisomes (van der Klei et al., 2006). In this study, we observed a morphological change in the vacuole during the methanol adaptation period. A wild-type strain shifted to methanol medium for 2 hours contained a single spherical vacuole per cell, compared with 2-4 clustered vacuoles per cell when growing on glucose medium (Fig. 1A).To examine the morphological change after methanol adaptation of P. pastoris in greater detail, we performed a morphometric analysis during the transition process by counting the cells exhibiting a single spherical vacuole over time (Fig. 1B). FM4-64-labeled P. pastoris cells under methanol adaptation were sampled, and fluorescence images were immediately taken. It was found that the number of cells containing a single round vacuole increased immediately following the shift to methanol medium, and the SummaryAtg8 is a ubiquitin-like protein that is required, along with its lipidation system, for autophagy in all eukaryotic cells. The lipidated form of Atg8 is anchored on the autophagosomal membrane during autophagy. Here, we demonstrate a previously unknown role for Atg8 in vacuolar membrane dynamics. In the methylotrophic yeast Pichia pastoris, vacuoles were found to fuse to become a single spherical vacuole during adaptation from glucose-to methanol-containing medium. Atg8 is responsible for the vacuolar fusion in P. pastoris during this adaptation to methanol. Although vacuole fusion required processing of Atg8 at the C-terminus, it did not require lipidation of Atg8 for autophagy. This is the first report of the function of any Atg8 protein family member in a process other than autophagy that is independent of lipidation.

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confidence: 52%

Atg8 regulates vacuolar membrane dynamics in a lipidation-independent manner in Pichia pastoris

Tamura¹,

Oku²,

Sakai³

2010

Development

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“…In mammals, peroxisomes are responsible for key enzymatic steps in the synthesis of plasmalogens -ether-linked phospholipids that are abundant in brain and nervous tissue (Brites et al, 2004). Peroxisomes of fungi often contain environmentally inducible enzymes, for example, those involved in metabolism of methanol (van der Klei et al, 2006) or biosynthesis of penicillin (van den . The Woronin body of filamentous fungi which functions to seal septal pores is also a highly specialized peroxisome (Jedd and Chua, 2000).…”

Section: Introductionmentioning

confidence: 99%

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

Lanyon‐Hogg

Warriner

Baker

2010

Biology of the Cell

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Peroxisomes are a family of organelles which have many unusual features. They can arise de novo from the endoplasmic reticulum by a still poorly characterized process, yet possess a unique machinery for the import of their matrix proteins. As peroxisomes lack DNA, their function, which is highly variable and dependent on developmental and/or environmental conditions, is determined by the post-translational import of specific metabolic enzymes in folded or oligomeric states. The two classes of matrix targeting signals for peroxisomal proteins [PTS1 (peroxisomal targeting signal 1) and PTS2] are recognized by cytosolic receptors [PEX5 (peroxin 5) and PEX7 respectively] which escort their cargo proteins to, or possibly across, the peroxisome membrane. Although the membrane translocation mechanism remains unclear, it appears to be driven by thermodynamically favourable binding interactions. Recycling of the receptors from the peroxisome membrane requires ATP hydrolysis for two linked processes: ubiquitination of PEX5 (and the PEX7 co-receptors in yeast) and the function of two peroxisome-associated AAA (ATPase associated with various cellular activities) ATPases, which play a role in recycling or turnover of the ubiquitinated receptors. This review summarizes and integrates recent findings on peroxisome matrix protein import from yeast, plant and mammalian model systems, and discusses some of the gaps in our understanding of this remarkable protein transport system.

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“…In the former, HCHO is fixed to xylulose 5-phosphate by dihydroxyacetone synthase within peroxisomes (33). Otherwise, HCHO nonenzymically reacts with GSH to form S-hydroxymethylglutathione, and subsequently, HCHO is oxidized to CO 2 via the dissimilation pathway (44,51). S-Hydroxymethylglutathione formed in peroxisomes may be exported to the cytosol (14), where it acts as a substrate for GSH-dependent HCHO dehydrogenase.…”

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Yap1-Regulated Glutathione Redox System Curtails Accumulation of Formaldehyde and Reactive Oxygen Species in Methanol Metabolism of Pichia pastoris

et al. 2009

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The glutathione redox system, including the glutathione biosynthesis and glutathione regeneration reaction, has been found to play a critical role in the yeast Pichia pastoris during growth on methanol, and this regulation was at least partly executed by the transcription factor PpYap1. During adaptation to methanol medium, PpYap1 transiently localized to the nucleus and activated the expression of the glutathione redox system and upregulated glutathione reductase 1 (Glr1). Glr1 activates the regeneration of the reduced form of glutathione (GSH). Depletion of Glr1 caused a severe growth defect on methanol and hypersensitivity to formaldehyde (HCHO), which could be complemented by addition of GSH to the medium. Disruption of the genes for the HCHO-oxidizing enzymes PpFld1 and PpFgh1 caused a comparable phenotype, but disruption of the downstream gene PpFDH1 did not, demonstrating the importance of maintaining intracellular GSH levels. Absence of the peroxisomal glutathione peroxidase Pmp20 also triggered nuclear localization of PpYap1, and although cells were not sensitive to HCHO, growth on methanol was again severely impaired due to oxidative stress. Thus, the PpYap1-regulated glutathione redox system has two important roles, i.e., HCHO metabolism and detoxification of reactive oxygen species.

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The significance of peroxisomes in methanol metabolism in methylotrophic yeast

Cited by 173 publications

References 66 publications

Atg8 regulates vacuolar membrane dynamics in a lipidation-independent manner in Pichia pastoris

Atg8 regulates vacuolar membrane dynamics in a lipidation-independent manner in Pichia pastoris

Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes

Yap1-Regulated Glutathione Redox System Curtails Accumulation of Formaldehyde and Reactive Oxygen Species in Methanol Metabolism of Pichia pastoris

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