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  1. Article: Autophagy in organelle homeostasis: peroxisome turnover.

    Monastyrska, Iryna / Klionsky, Daniel J

    Molecular aspects of medicine

    2006  Volume 27, Issue 5-6, Page(s) 483–494

    Abstract: When cells are confronted with an insufficient supply of nutrients in their extracellular fluid, they may begin to cannibalize some of their internal proteins as well as whole organelles for reuse in the synthesis of new components. This process is ... ...

    Abstract When cells are confronted with an insufficient supply of nutrients in their extracellular fluid, they may begin to cannibalize some of their internal proteins as well as whole organelles for reuse in the synthesis of new components. This process is termed autophagy and it involves the formation of a double-membrane structure within the cell, which encloses the material to be degraded into a vesicle called an autophagosome. The autophagosome subsequently fuses with a lysosome/vacuole whose hydrolytic enzymes degrade the sequestered organelle. Degradation of peroxisomes is a specific type of autophagy, which occurs in a selective manner and has been mostly studied in yeast. Recently, it was reported that a similar selective process of autophagy occurs in mammalian cells with proliferated peroxisomes. Here we discuss characteristics of the autophagy of peroxisomes in mammalian cells and present a comprehensive model of their likely mechanism of degradation on the basis of known and common elements from other systems.
    MeSH term(s) Animals ; Autophagy ; Cytoskeleton/metabolism ; Homeostasis ; Organelles/metabolism ; Oxidation-Reduction ; Peroxisomes/metabolism
    Language English
    Publishing date 2006-09-14
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 197640-0
    ISSN 1872-9452 ; 0098-2997
    ISSN (online) 1872-9452
    ISSN 0098-2997
    DOI 10.1016/j.mam.2006.08.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1189: Show issues Location:
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  2. Article ; Online: Harpooning the Cvt complex to the phagophore assembly site.

    Monastyrska, Iryna / Reggiori, Fulvio / Klionsky, Daniel J

    Autophagy

    2008  Volume 4, Issue 7, Page(s) 914–916

    Abstract: Autophagy is a catabolic process employed by eukaryotes to degrade and recycle intracellular components. When this pathway is induced by starvation conditions, part of the cytoplasm and organelles are sequestered into double-membrane vesicles called ... ...

    Abstract Autophagy is a catabolic process employed by eukaryotes to degrade and recycle intracellular components. When this pathway is induced by starvation conditions, part of the cytoplasm and organelles are sequestered into double-membrane vesicles called autophagosomes, and delivered into the lysosome/vacuole for degradation. In addition to the random bulk elimination of cytoplasmic contents, the selective removal of specific cargo molecules has also been described. These selective types of autophagy are characterized by the recruitment of the cargo destined for degradation in close proximity to the forming double-membrane vesicle that results in an exclusive incorporation (that is, without bulk cytoplasm). A number of factors required for selective types of autophagy have been identified. In particular, we have recently shown that actin and the actin-binding Arp2/3 protein complex are involved in the cytoplasm to vacuole targeting (Cvt) pathway, a yeast selective type of autophagy. The contribution at a molecular level of these factors, however, remains unknown. In this addendum, we present mechanistic models that take into account possible roles of actin and the Arp2/3 complex in the Cvt pathway.
    MeSH term(s) Actin-Related Protein 2-3 Complex/metabolism ; Autophagy ; Cytoplasm/metabolism ; Membrane Fusion ; Membrane Proteins/metabolism ; Models, Biological ; Phagosomes/metabolism ; Protein Transport ; Vacuoles/metabolism
    Chemical Substances Actin-Related Protein 2-3 Complex ; Membrane Proteins
    Language English
    Publishing date 2008-10-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.4161/auto.6657
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  3. Article ; Online: Visualizing coronavirus RNA synthesis in time by using click chemistry.

    Hagemeijer, Marne C / Vonk, Annelotte M / Monastyrska, Iryna / Rottier, Peter J M / de Haan, Cornelis A M

    Journal of virology

    2012  Volume 86, Issue 10, Page(s) 5808–5816

    Abstract: Coronaviruses induce in infected cells the formation of replicative structures, consisting of double-membrane vesicles (DMVs) and convoluted membranes, where viral RNA synthesis supposedly takes place and to which the nonstructural proteins (nsp's) ... ...

    Abstract Coronaviruses induce in infected cells the formation of replicative structures, consisting of double-membrane vesicles (DMVs) and convoluted membranes, where viral RNA synthesis supposedly takes place and to which the nonstructural proteins (nsp's) localize. Double-stranded RNA (dsRNA), the presumed intermediate in RNA synthesis, is localized to the DMV interior. However, as pores connecting the DMV interior with the cytoplasm have not been detected, it is unclear whether RNA synthesis occurs at these same sites. Here, we studied coronavirus RNA synthesis by feeding cells with a uridine analogue, after which nascent RNAs were detected using click chemistry. Early in infection, nascent viral RNA and nsp's colocalized with or occurred adjacent to dsRNA foci. Late in infection, the correlation between dsRNA dots, then found dispersed throughout the cytoplasm, and nsp's and nascent RNAs was less obvious. However, foci of nascent RNAs were always found to colocalize with the nsp12-encoded RNA-dependent RNA polymerase. These results demonstrate the feasibility of detecting viral RNA synthesis by using click chemistry and indicate that dsRNA dots do not necessarily correspond with sites of active viral RNA synthesis. Rather, late in infection many DMVs may harbor dsRNA molecules that are no longer functioning as intermediates in RNA synthesis.
    MeSH term(s) Animals ; Cell Line ; Click Chemistry/methods ; Coronavirus/chemistry ; Coronavirus/genetics ; Coronavirus/metabolism ; Coronavirus Infections/virology ; Humans ; Mice ; Microscopy, Confocal/methods ; RNA, Viral/chemistry ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Uridine/analogs & derivatives ; Uridine/metabolism
    Chemical Substances RNA, Viral ; Uridine (WHI7HQ7H85)
    Keywords covid19
    Language English
    Publishing date 2012-03-21
    Publishing country United States
    Document type Evaluation Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.07207-11
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 609: Show issues Location:
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  4. Article ; Online: Multiple roles of the cytoskeleton in autophagy.

    Monastyrska, Iryna / Rieter, Ester / Klionsky, Daniel J / Reggiori, Fulvio

    Biological reviews of the Cambridge Philosophical Society

    2009  Volume 84, Issue 3, Page(s) 431–448

    Abstract: Autophagy is involved in a wide range of physiological processes including cellular remodeling during development, immuno-protection against heterologous invaders and elimination of aberrant or obsolete cellular structures. This conserved degradation ... ...

    Abstract Autophagy is involved in a wide range of physiological processes including cellular remodeling during development, immuno-protection against heterologous invaders and elimination of aberrant or obsolete cellular structures. This conserved degradation pathway also plays a key role in maintaining intracellular nutritional homeostasis and during starvation, for example, it is involved in the recycling of unnecessary cellular components to compensate for the limitation of nutrients. Autophagy is characterized by specific membrane rearrangements that culminate with the formation of large cytosolic double-membrane vesicles called autophagosomes. Autophagosomes sequester cytoplasmic material that is destined for degradation. Once completed, these vesicles dock and fuse with endosomes and/or lysosomes to deliver their contents into the hydrolytically active lumen of the latter organelle where, together with their cargoes, they are broken down into their basic components. Specific structures destined for degradation via autophagy are in many cases selectively targeted and sequestered into autophagosomes. A number of factors required for autophagy have been identified, but numerous questions about the molecular mechanism of this pathway remain unanswered. For instance, it is unclear how membranes are recruited and assembled into autophagosomes. In addition, once completed, these vesicles are transported to cellular locations where endosomes and lysosomes are concentrated. The mechanism employed for this directed movement is not well understood. The cellular cytoskeleton is a large, highly dynamic cellular scaffold that has a crucial role in multiple processes, several of which involve membrane rearrangements and vesicle-mediated events. Relatively little is known about the roles of the cytoskeleton network in autophagy. Nevertheless, some recent studies have revealed the importance of cytoskeletal elements such as actin microfilaments and microtubules in specific aspects of autophagy. In this review, we will highlight the results of this work and discuss their implications, providing possible working models. In particular, we will first describe the findings obtained with the yeast Saccharomyces cerevisiae, for long the leading organism for the study of autophagy, and, successively, those attained in mammalian cells, to emphasize possible differences between eukaryotic organisms.
    MeSH term(s) Autophagy/physiology ; Cytoskeleton/physiology ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Gene Expression Regulation, Fungal/physiology ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism
    Chemical Substances Fungal Proteins
    Language English
    Publishing date 2009-02-18
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1423558-4
    ISSN 1469-185X ; 0006-3231 ; 1464-7931
    ISSN (online) 1469-185X
    ISSN 0006-3231 ; 1464-7931
    DOI 10.1111/j.1469-185X.2009.00082.x
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    Z 71/734: Show issues

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  5. Article: Atg11 directs autophagosome cargoes to the PAS along actin cables.

    Monastyrska, Iryna / Shintani, Takahiro / Klionsky, Daniel J / Reggiori, Fulvio

    Autophagy

    2006  Volume 2, Issue 2, Page(s) 119–121

    Abstract: For more than 40 years, autophagy has been almost exclusively studied as a cellular response that allows adaptation to starvation situations. In nutrient-deprived conditions, cytoplasmic components and organelles are randomly sequestered into double- ... ...

    Abstract For more than 40 years, autophagy has been almost exclusively studied as a cellular response that allows adaptation to starvation situations. In nutrient-deprived conditions, cytoplasmic components and organelles are randomly sequestered into double-membrane vesicles called autophagosomes, creating the notion that this pathway is a nonselective process (reviewed in Refs 1, 2). Recent results, however, have demonstrated that under certain circumstances, cargoes such as protein complexes, organelles and bacteria can be selectively and exclusively incorporated into double-membrane vesicles.(1) We have recently shown that actin plays an essential role in two selective types of autophagy in the yeast Saccharomyces cerevisiae, the cytoplasm to vacuole targeting (Cvt) pathway and pexophagy, raising the possibility that the structures formed by polymers of this protein helps autophagosomes in recognizing the cargoes that must be delivered to the vacuole.(3) In this addendum, we discuss the possible central role of Atg11 as a molecule connecting cargoes, actin and pre-utophagosomal structure (PAS) elements.
    MeSH term(s) Actins/physiology ; Autophagy/physiology ; Autophagy-Related Proteins ; Biological Transport, Active ; Cytoskeleton/physiology ; Myosin Heavy Chains/physiology ; Myosin Type V/physiology ; Phagosomes/physiology ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/physiology ; Vacuoles/physiology ; Vesicular Transport Proteins/physiology
    Chemical Substances Actins ; Atg11 protein, S cerevisiae ; Autophagy-Related Proteins ; MYO2 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Vesicular Transport Proteins ; Myosin Type V (EC 3.6.1.-) ; Myosin Heavy Chains (EC 3.6.4.1)
    Language English
    Publishing date 2006-04-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.4161/auto.2.2.2298
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  6. Article ; Online: An autophagy-independent role for LC3 in equine arteritis virus replication.

    Monastyrska, Iryna / Ulasli, Mustafa / Rottier, Peter J M / Guan, Jun-Lin / Reggiori, Fulvio / de Haan, Cornelis A M

    Autophagy

    2012  Volume 9, Issue 2, Page(s) 164–174

    Abstract: Equine arteritis virus (EAV) is an enveloped, positive-strand RNA virus. Genome replication of EAV has been associated with modified intracellular membranes that are shaped into double-membrane vesicles (DMVs). We showed by immuno-electron microscopy ... ...

    Abstract Equine arteritis virus (EAV) is an enveloped, positive-strand RNA virus. Genome replication of EAV has been associated with modified intracellular membranes that are shaped into double-membrane vesicles (DMVs). We showed by immuno-electron microscopy that the DMVs induced in EAV-infected cells contain double-strand (ds)RNA molecules, presumed RNA replication intermediates, and are decorated with the autophagy marker protein microtubule-associated protein 1 light chain 3 (LC3). Replication of EAV, however, was not affected in autophagy-deficient cells lacking autophagy-related protein 7 (ATG7). Nevertheless, colocalization of DMVs and LC3 was still observed in these knockout cells, which only contain the nonlipidated form of LC3. Although autophagy is not required, depletion of LC3 markedly reduced the replication of EAV. EAV replication could be fully restored in these cells by expression of a nonlipidated form of LC3. These findings demonstrate an autophagy-independent role for LC3 in EAV replication. Together with the observation that EAV-induced DMVs are also positive for ER degradation-enhancing α-mannosidase-like 1 (EDEM1), our data suggested that this virus, similarly to the distantly-related mouse hepatitis coronavirus, hijacks the ER-derived membranes of EDEMosomes to ensure its efficient replication.
    MeSH term(s) Animals ; Arterivirus Infections/metabolism ; Arterivirus Infections/pathology ; Arterivirus Infections/virology ; Autophagy ; Cell Line ; Cell Membrane/metabolism ; Cell Membrane/ultrastructure ; Equartevirus/physiology ; Equartevirus/ultrastructure ; Green Fluorescent Proteins/metabolism ; Membrane Proteins/metabolism ; Mice ; Microtubule-Associated Proteins/metabolism ; RNA Transport ; RNA, Double-Stranded/metabolism ; Transport Vesicles/metabolism ; Transport Vesicles/ultrastructure ; Viral Proteins/metabolism ; Virus Replication/physiology
    Chemical Substances Membrane Proteins ; Microtubule-Associated Proteins ; RNA, Double-Stranded ; Viral Proteins ; Green Fluorescent Proteins (147336-22-9)
    Keywords covid19
    Language English
    Publishing date 2012-11-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.4161/auto.22743
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  7. Article: The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae.

    Reggiori, Fulvio / Monastyrska, Iryna / Shintani, Takahiro / Klionsky, Daniel J

    Molecular biology of the cell

    2005  Volume 16, Issue 12, Page(s) 5843–5856

    Abstract: Autophagy is a catabolic multitask transport route that takes place in all eukaryotic cells. During starvation, cytoplasmic components are randomly sequestered into huge double-membrane vesicles called autophagosomes and delivered into the lysosome/ ... ...

    Abstract Autophagy is a catabolic multitask transport route that takes place in all eukaryotic cells. During starvation, cytoplasmic components are randomly sequestered into huge double-membrane vesicles called autophagosomes and delivered into the lysosome/vacuole where they are destroyed. Cells are able to modulate autophagy in response to their needs, and under certain circumstances, cargoes such as aberrant protein aggregates, organelles and bacteria can be selectively and exclusively incorporated into autophagosomes. In the yeast Saccharomyces cerevisiae, for example, double-membrane vesicles are used to transport the Ape1 protease into the vacuole, or for the elimination of superfluous peroxisomes. In the present study we reveal that in this organism, actin plays a role in these two types of selective autophagy but not in the nonselective, bulk process. In particular, we show that precursor Ape1 is not correctly recruited to the PAS, the putative site of double-membrane vesicle biogenesis, and superfluous peroxisomes are not degraded in a conditional actin mutant. These phenomena correlate with a defect in Atg9 trafficking from the mitochondria to the PAS.
    MeSH term(s) Actins/physiology ; Autophagy ; Cell Division ; Cytoskeleton/physiology ; Cytoskeleton/ultrastructure ; Genotype ; Microscopy, Fluorescence ; Mitochondria/ultrastructure ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae/ultrastructure
    Chemical Substances Actins
    Language English
    Publishing date 2005-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E05-07-0629
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2853: Show issues Location:
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    Zs.MO 410: Show issues

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  8. Article ; Online: Arp2 links autophagic machinery with the actin cytoskeleton.

    Monastyrska, Iryna / He, Congcong / Geng, Jiefei / Hoppe, Adam D / Li, Zhijian / Klionsky, Daniel J

    Molecular biology of the cell

    2008  Volume 19, Issue 5, Page(s) 1962–1975

    Abstract: Macroautophagy involves lysosomal/vacuolar elimination of long-lived proteins and entire organelles from the cytosol. The process begins with formation of a double-membrane vesicle that sequesters bulk cytoplasm, or a specific cargo destined for ... ...

    Abstract Macroautophagy involves lysosomal/vacuolar elimination of long-lived proteins and entire organelles from the cytosol. The process begins with formation of a double-membrane vesicle that sequesters bulk cytoplasm, or a specific cargo destined for lysosomal/vacuolar delivery. The completed vesicle fuses with the lysosome/vacuole limiting membrane, releasing its content into the organelle lumen for subsequent degradation and recycling of the resulting macromolecules. A majority of the autophagy-related (Atg) proteins are required at the step of vesicle formation. The integral membrane protein Atg9 cycles between certain intracellular compartments and the vesicle nucleation site, presumably to supply membranes necessary for macroautophagic vesicle formation. In this study we have tracked the movement of Atg9 over time in living cells by using real-time fluorescence microscopy. Our results reveal that an actin-related protein, Arp2, briefly colocalizes with Atg9 and directly regulates the dynamics of Atg9 movement. We propose that proteins of the Arp2/3 complex regulate Atg9 transport for specific types of autophagy.
    MeSH term(s) Actin-Related Protein 2/metabolism ; Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Autophagy ; Autophagy-Related Proteins ; Cytoskeleton/metabolism ; Membrane Proteins/metabolism ; Mutation/genetics ; Protein Binding ; Protein Transport ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Vesicular Transport Proteins/metabolism
    Chemical Substances ARP2 protein, S cerevisiae ; ATG9 protein, S cerevisiae ; Actin-Related Protein 2 ; Actin-Related Protein 2-3 Complex ; Actins ; Atg11 protein, S cerevisiae ; Autophagy-Related Proteins ; Membrane Proteins ; Saccharomyces cerevisiae Proteins ; Vesicular Transport Proteins
    Language English
    Publishing date 2008-02-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E07-09-0892
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 410: Show issues

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  9. Article ; Online: Membrane rearrangements mediated by coronavirus nonstructural proteins 3 and 4.

    Hagemeijer, Marne C / Monastyrska, Iryna / Griffith, Janice / van der Sluijs, Peter / Voortman, Jarno / van Bergen en Henegouwen, Paul M / Vonk, Annelotte M / Rottier, Peter J M / Reggiori, Fulvio / de Haan, Cornelis A M

    Virology

    2014  Volume 458-459, Page(s) 125–135

    Abstract: Coronaviruses replicate their genomes in association with rearranged cellular membranes. The coronavirus nonstructural integral membrane proteins (nsps) 3, 4 and 6, are key players in the formation of the rearranged membranes. Previously, we demonstrated ...

    Abstract Coronaviruses replicate their genomes in association with rearranged cellular membranes. The coronavirus nonstructural integral membrane proteins (nsps) 3, 4 and 6, are key players in the formation of the rearranged membranes. Previously, we demonstrated that nsp3 and nsp4 interact and that their co-expression results in the relocalization of these proteins from the endoplasmic reticulum (ER) into discrete perinuclear foci. We now show that these foci correspond to areas of rearranged ER-derived membranes, which display increased membrane curvature. These structures, which were able to recruit other nsps, were only detected when nsp3 and nsp4 were derived from the same coronavirus species. We propose, based on the analysis of a large number of nsp3 and nsp4 mutants, that interaction between the large luminal loops of these proteins drives the formation of membrane rearrangements, onto which the coronavirus replication-transcription complexes assemble in infected cells.
    MeSH term(s) Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane ; Conserved Sequence ; Coronavirus/genetics ; Coronavirus/metabolism ; Endoplasmic Reticulum/physiology ; Endoplasmic Reticulum/virology ; Gene Expression Regulation, Viral/physiology ; Mice ; Mutation ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Virus Replication
    Chemical Substances Viral Nonstructural Proteins
    Keywords covid19
    Language English
    Publishing date 2014-05-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 200425-2
    ISSN 1096-0341 ; 0042-6822
    ISSN (online) 1096-0341
    ISSN 0042-6822
    DOI 10.1016/j.virol.2014.04.027
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Ud II Zs.172: Show issues Location:
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  10. Article: Old yellow enzyme confers resistance of Hansenula polymorpha towards allyl alcohol.

    Komduur, Janet A / Leão, Adriana N / Monastyrska, Iryna / Veenhuis, Marten / Kiel, Jan A K W

    Current genetics

    2002  Volume 41, Issue 6, Page(s) 401–406

    Abstract: In the methylotrophic yeast, Hansenula polymorpha, peroxisomes are formed during growth on methanol as sole carbon and energy source and contain the key enzymes for its metabolism, one of the major enzymes being alcohol oxidase (AO). Upon a shift of ... ...

    Abstract In the methylotrophic yeast, Hansenula polymorpha, peroxisomes are formed during growth on methanol as sole carbon and energy source and contain the key enzymes for its metabolism, one of the major enzymes being alcohol oxidase (AO). Upon a shift of these cells to glucose-containing medium, peroxisomes become redundant for growth and are rapidly degraded via a highly selective process designated macropexophagy. H. polymorpha pdd mutants are disturbed in macropexophagy and hence retain high levels of peroxisomal AO activity upon induction of this process. To enable efficient isolation of PDD genes via functional complementation, we make use of the fact that AO can convert allyl alcohol into the highly toxic compound acrolein. When allyl alcohol is added to cells under conditions that induce macropexophagy, pdd mutants die, whereas complemented pdd mutants and wild-type cells survive. Besides isolating bona fide PDD genes, we occasionally obtained pdd transformants that retained high levels of AO activity although their allyl alcohol sensitive phenotype was suppressed. These invariably contained extra copies of a gene cluster encoding homologues of Saccharomyces carlsbergensis old yellow enzyme. Our data suggest that the proteins encoded by these genes detoxify acrolein by converting it into less harmful components.
    MeSH term(s) Alcohol Oxidoreductases/genetics ; Alcohol Oxidoreductases/metabolism ; Amino Acid Sequence ; Drug Resistance, Microbial ; Methanol/metabolism ; Molecular Sequence Data ; Peroxisomes/metabolism ; Pichia/drug effects ; Pichia/enzymology ; Propanols/metabolism ; Propanols/pharmacology ; Selection, Genetic ; Sequence Homology, Amino Acid
    Chemical Substances Propanols ; allyl alcohol (3W678R12M0) ; Alcohol Oxidoreductases (EC 1.1.-) ; alcohol oxidase (EC 1.1.3.13) ; Methanol (Y4S76JWI15)
    Language English
    Publishing date 2002-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 282876-5
    ISSN 1432-0983 ; 0172-8083
    ISSN (online) 1432-0983
    ISSN 0172-8083
    DOI 10.1007/s00294-002-0321-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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