LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 38

Search options

  1. Article: Impact of Hydrogen Peroxide on Protein Synthesis in Yeast.

    Picazo, Cecilia / Molin, Mikael

    Antioxidants (Basel, Switzerland)

    2021  Volume 10, Issue 6

    Abstract: Cells must be able to respond and adapt to different stress conditions to maintain normal function. A common response to stress is the global inhibition of protein synthesis. Protein synthesis is an expensive process consuming much of the cell's energy. ... ...

    Abstract Cells must be able to respond and adapt to different stress conditions to maintain normal function. A common response to stress is the global inhibition of protein synthesis. Protein synthesis is an expensive process consuming much of the cell's energy. Consequently, it must be tightly regulated to conserve resources. One of these stress conditions is oxidative stress, resulting from the accumulation of reactive oxygen species (ROS) mainly produced by the mitochondria but also by other intracellular sources. Cells utilize a variety of antioxidant systems to protect against ROS, directing signaling and adaptation responses at lower levels and/or detoxification as levels increase to preclude the accumulation of damage. In this review, we focus on the role of hydrogen peroxide, H
    Language English
    Publishing date 2021-06-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2704216-9
    ISSN 2076-3921
    ISSN 2076-3921
    DOI 10.3390/antiox10060952
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article: Impact of Hydrogen Peroxide on Protein Synthesis in Yeast

    Picazo, Cecilia / Molin, Mikael

    Antioxidants. 2021 June 12, v. 10, no. 6

    2021  

    Abstract: Cells must be able to respond and adapt to different stress conditions to maintain normal function. A common response to stress is the global inhibition of protein synthesis. Protein synthesis is an expensive process consuming much of the cell’s energy. ... ...

    Abstract Cells must be able to respond and adapt to different stress conditions to maintain normal function. A common response to stress is the global inhibition of protein synthesis. Protein synthesis is an expensive process consuming much of the cell’s energy. Consequently, it must be tightly regulated to conserve resources. One of these stress conditions is oxidative stress, resulting from the accumulation of reactive oxygen species (ROS) mainly produced by the mitochondria but also by other intracellular sources. Cells utilize a variety of antioxidant systems to protect against ROS, directing signaling and adaptation responses at lower levels and/or detoxification as levels increase to preclude the accumulation of damage. In this review, we focus on the role of hydrogen peroxide, H₂O₂, as a signaling molecule regulating protein synthesis at different levels, including transcription and various parts of the translation process, e.g., initiation, elongation, termination and ribosome recycling.
    Keywords energy ; hydrogen peroxide ; mitochondria ; oxidative stress ; protein synthesis ; ribosomes ; stress response ; yeasts
    Language English
    Dates of publication 2021-0612
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2704216-9
    ISSN 2076-3921
    ISSN 2076-3921
    DOI 10.3390/antiox10060952
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

  3. Article ; Online: High-throughput Growth Measurements of Yeast Exposed to Visible Light.

    Logg, Katarina / Andersson, Mikael / Blomberg, Anders / Molin, Mikael

    Bio-protocol

    2022  Volume 12, Issue 2, Page(s) e4292

    Abstract: Light is a double-edged sword: it is essential for life on the planet but also causes cellular damage and death. Consequently, organisms have evolved systems not only for harvesting and converting light energy into chemical energy but also for countering ...

    Abstract Light is a double-edged sword: it is essential for life on the planet but also causes cellular damage and death. Consequently, organisms have evolved systems not only for harvesting and converting light energy into chemical energy but also for countering its toxic effects. Despite the omnipresence and importance of such light-dependent effects, there are very few unbiased genetic screens, if any, investigating the mechanistic consequences that visible light has on cells. Baker's yeast,
    Language English
    Publishing date 2022-01-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2833269-6
    ISSN 2331-8325 ; 2331-8325
    ISSN (online) 2331-8325
    ISSN 2331-8325
    DOI 10.21769/BioProtoc.4292
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  4. Article ; Online: A Hypersensitive Genetically Encoded Fluorescent Indicator (roGFP2-Prx1) Enables Continuous Measurement of Intracellular H

    Gast, Veronica / Siewers, Verena / Molin, Mikael

    Bio-protocol

    2022  Volume 12, Issue 3, Page(s) e4317

    Abstract: Hydrogen peroxide ( ... ...

    Abstract Hydrogen peroxide (H
    Language English
    Publishing date 2022-02-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2833269-6
    ISSN 2331-8325 ; 2331-8325
    ISSN (online) 2331-8325
    ISSN 2331-8325
    DOI 10.21769/BioProtoc.4317
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  5. Article ; Online: Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function.

    Troussicot, Laura / Burmann, Björn M / Molin, Mikael

    Structure (London, England : 1993)

    2021  Volume 29, Issue 7, Page(s) 640–654

    Abstract: Peroxiredoxins (PRDXs) are abundant peroxidases present in all kingdoms of life. Recently, they have been shown to also carry out additional roles as molecular chaperones. To address this emerging supplementary function, this review focuses on structural ...

    Abstract Peroxiredoxins (PRDXs) are abundant peroxidases present in all kingdoms of life. Recently, they have been shown to also carry out additional roles as molecular chaperones. To address this emerging supplementary function, this review focuses on structural studies of 2-Cys PRDX systems exhibiting chaperone activity. We provide a detailed understanding of the current knowledge of structural determinants underlying the chaperone function of PRDXs. Specifically, we describe the mechanisms which may modulate their quaternary structure to facilitate interactions with client proteins and how they are coordinated with the functions of other molecular chaperones. Following an overview of PRDX molecular architecture, we outline structural details of the presently best-characterized peroxiredoxins exhibiting chaperone function and highlight common denominators. Finally, we discuss the remarkable structural similarities between 2-Cys PRDXs, small HSPs, and J-domain-independent Hsp40 holdases in terms of their functions and dynamic equilibria between low- and high-molecular-weight oligomers.
    MeSH term(s) Humans ; Models, Molecular ; Peroxiredoxins/chemistry ; Peroxiredoxins/metabolism ; Protein Conformation ; Protein Multimerization ; Structure-Activity Relationship
    Chemical Substances Peroxiredoxins (EC 1.11.1.15)
    Language English
    Publishing date 2021-05-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2021.04.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  6. Article ; Online: Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.

    Troussicot, Laura / Vallet, Alicia / Molin, Mikael / Burmann, Björn M / Schanda, Paul

    Journal of the American Chemical Society

    2023  Volume 145, Issue 19, Page(s) 10700–10711

    Abstract: Disulfide bond formation is fundamentally important for protein structure and constitutes a key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen peroxide ... ...

    Abstract Disulfide bond formation is fundamentally important for protein structure and constitutes a key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen peroxide through a catalytic cycle of Cys oxidation and reduction. Additionally, upon Cys oxidation PRDXs undergo extensive conformational rearrangements that may underlie their presently structurally poorly defined functions as molecular chaperones. Rearrangements include high molecular-weight oligomerization, the dynamics of which are, however, poorly understood, as is the impact of disulfide bond formation on these properties. Here we show that formation of disulfide bonds along the catalytic cycle induces extensive μs time scale dynamics, as monitored by magic-angle spinning NMR of the 216 kDa-large Tsa1 decameric assembly and solution-NMR of a designed dimeric mutant. We ascribe the conformational dynamics to structural frustration, resulting from conflicts between the disulfide-constrained reduction of mobility and the desire to fulfill other favorable contacts.
    MeSH term(s) Peroxiredoxins/chemistry ; Peroxiredoxins/metabolism ; Oxidation-Reduction ; Hydrogen Peroxide/metabolism ; Molecular Conformation ; Disulfides/chemistry
    Chemical Substances Peroxiredoxins (EC 1.11.1.15) ; Hydrogen Peroxide (BBX060AN9V) ; Disulfides
    Language English
    Publishing date 2023-05-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.3c01200
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  7. Article ; Online: Calcineurin stimulation by Cnb1p overproduction mitigates protein aggregation and α-synuclein toxicity in a yeast model of synucleinopathy.

    Chawla, Srishti / Ahmadpour, Doryaneh / Schneider, Kara L / Kumar, Navinder / Fischbach, Arthur / Molin, Mikael / Nystrom, Thomas

    Cell communication and signaling : CCS

    2023  Volume 21, Issue 1, Page(s) 220

    Abstract: The calcium-responsive phosphatase, calcineurin, senses changes in ... ...

    Abstract The calcium-responsive phosphatase, calcineurin, senses changes in Ca
    MeSH term(s) Humans ; Synucleinopathies ; alpha-Synuclein ; Protein Aggregates ; Calcineurin ; Saccharomyces cerevisiae ; Parkinson Disease ; DNA-Binding Proteins ; Transcription Factors ; Saccharomyces cerevisiae Proteins
    Chemical Substances alpha-Synuclein ; Protein Aggregates ; Calcineurin (EC 3.1.3.16) ; CRZ1 protein, S cerevisiae ; DNA-Binding Proteins ; Transcription Factors ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2023-08-24
    Publishing country England
    Document type Video-Audio Media ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126315-2
    ISSN 1478-811X ; 1478-811X
    ISSN (online) 1478-811X
    ISSN 1478-811X
    DOI 10.1186/s12964-023-01242-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  8. Article ; Online: The Yeast eIF2 Kinase Gcn2 Facilitates H

    Gast, Veronica / Campbell, Kate / Picazo, Cecilia / Engqvist, Martin / Siewers, Verena / Molin, Mikael

    Applied and environmental microbiology

    2021  Volume 87, Issue 15, Page(s) e0030121

    Abstract: Recombinant protein production is a known source of oxidative stress. However, knowledge of which reactive oxygen species are involved or the specific growth phase in which stress occurs remains lacking. Using modern, hypersensitive genetic ... ...

    Abstract Recombinant protein production is a known source of oxidative stress. However, knowledge of which reactive oxygen species are involved or the specific growth phase in which stress occurs remains lacking. Using modern, hypersensitive genetic H
    MeSH term(s) Endoplasmic Reticulum/metabolism ; Feedback, Physiological ; Hydrogen Peroxide/metabolism ; Protein Biosynthesis ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Recombinant Proteins/biosynthesis ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; alpha-Amylases/biosynthesis
    Chemical Substances Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Hydrogen Peroxide (BBX060AN9V) ; GCN2 protein, S cerevisiae (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; alpha-Amylases (EC 3.2.1.1)
    Language English
    Publishing date 2021-07-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/AEM.00301-21
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  9. Article: Linking Peroxiredoxin and Vacuolar-ATPase Functions in Calorie Restriction-Mediated Life Span Extension.

    Molin, Mikael / Demir, Ayse Banu

    International journal of cell biology

    2014  Volume 2014, Page(s) 913071

    Abstract: Calorie restriction (CR) is an intervention extending the life spans of many organisms. The mechanisms underlying CR-dependent retardation of aging are still poorly understood. Despite mechanisms involving conserved nutrient signaling pathways proposed, ... ...

    Abstract Calorie restriction (CR) is an intervention extending the life spans of many organisms. The mechanisms underlying CR-dependent retardation of aging are still poorly understood. Despite mechanisms involving conserved nutrient signaling pathways proposed, few target processes that can account for CR-mediated longevity have so far been identified. Recently, both peroxiredoxins and vacuolar-ATPases were reported to control CR-mediated retardation of aging downstream of conserved nutrient signaling pathways. In this review, we focus on peroxiredoxin-mediated stress-defence and vacuolar-ATPase regulated acidification and pinpoint common denominators between the two mechanisms proposed for how CR extends life span. Both the activities of peroxiredoxins and vacuolar-ATPases are stimulated upon CR through reduced activities in conserved nutrient signaling pathways and both seem to stimulate cellular resistance to peroxide-stress. However, whereas vacuolar-ATPases have recently been suggested to control both Ras-cAMP-PKA- and TORC1-mediated nutrient signaling, neither the physiological benefits of a proposed role for peroxiredoxins in H2O2-signaling nor downstream targets regulated are known. Both peroxiredoxins and vacuolar-ATPases do, however, impinge on mitochondrial iron-metabolism and further characterization of their impact on iron homeostasis and peroxide-resistance might therefore increase our understanding of the beneficial effects of CR on aging and age-related diseases.
    Language English
    Publishing date 2014-02-03
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2536742-0
    ISSN 1687-8884 ; 1687-8876
    ISSN (online) 1687-8884
    ISSN 1687-8876
    DOI 10.1155/2014/913071
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  10. Article ; Online: Engineering Saccharomyces cerevisiae for the production and secretion of Affibody molecules.

    Gast, Veronica / Sandegren, Anna / Dunås, Finn / Ekblad, Siri / Güler, Rezan / Thorén, Staffan / Tous Mohedano, Marta / Molin, Mikael / Engqvist, Martin K M / Siewers, Verena

    Microbial cell factories

    2022  Volume 21, Issue 1, Page(s) 36

    Abstract: Background: Affibody molecules are synthetic peptides with a variety of therapeutic and diagnostic applications. To date, Affibody molecules have mainly been produced by the bacterial production host Escherichia coli. There is an interest in exploring ... ...

    Abstract Background: Affibody molecules are synthetic peptides with a variety of therapeutic and diagnostic applications. To date, Affibody molecules have mainly been produced by the bacterial production host Escherichia coli. There is an interest in exploring alternative production hosts to identify potential improvements in terms of yield, ease of production and purification advantages. In this study, we evaluated the feasibility of Saccharomyces cerevisiae as a production chassis for this group of proteins.
    Results: We examined the production of three different Affibody molecules in S. cerevisiae and found that these Affibody molecules were partially degraded. An albumin-binding domain, which may be attached to the Affibody molecules to increase their half-life, was identified to be a substrate for several S. cerevisiae proteases. We tested the removal of three vacuolar proteases, proteinase A, proteinase B and carboxypeptidase Y. Removal of one of these, proteinase A, resulted in intact secretion of one of the targeted Affibody molecules. Removal of either or both of the two additional proteases, carboxypeptidase Y and proteinase B, resulted in intact secretion of the two remaining Affibody molecules. The produced Affibody molecules were verified to bind their target, human HER3, as potently as the corresponding molecules produced in E. coli in an in vitro surface-plasmon resonance binding assay. Finally, we performed a fed-batch fermentation with one of the engineered protease-deficient S. cerevisiae strains and achieved a protein titer of 530 mg Affibody molecule/L.
    Conclusion: This study shows that engineered S. cerevisiae has a great potential as a production host for recombinant Affibody molecules, reaching a high titer, and for proteins where endotoxin removal could be challenging, the use of S. cerevisiae obviates the need for endotoxin removal from protein produced in E. coli.
    MeSH term(s) Escherichia coli/metabolism ; Fermentation ; Humans ; Metabolic Engineering ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Vacuoles
    Chemical Substances Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2022-03-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 2091377-1
    ISSN 1475-2859 ; 1475-2859
    ISSN (online) 1475-2859
    ISSN 1475-2859
    DOI 10.1186/s12934-022-01761-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top