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  1. Article: Bacterial cell membranes and their role in daptomycin resistance: A review.

    Nguyen, April H / Hood, Kara S / Mileykovskaya, Eugenia / Miller, William R / Tran, Truc T

    Frontiers in molecular biosciences

    2022  Volume 9, Page(s) 1035574

    Abstract: Lipids play a major role in bacterial cells. Foremost, lipids are the primary constituents of the cell membrane bilayer, providing structure and separating the cell from the surrounding environment. This makes the lipid bilayer a prime target for ... ...

    Abstract Lipids play a major role in bacterial cells. Foremost, lipids are the primary constituents of the cell membrane bilayer, providing structure and separating the cell from the surrounding environment. This makes the lipid bilayer a prime target for antimicrobial peptides and membrane-acting antibiotics such as daptomycin. In response, bacteria have evolved mechanisms by which the membrane can be adapted to resist attack by these antimicrobial compounds. In this review, we focus on the membrane phospholipid changes associated with daptomycin resistance in enterococci,
    Language English
    Publishing date 2022-11-14
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2022.1035574
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  2. Article ; Online: Bacterial cell membranes and their role in daptomycin resistance

    April H. Nguyen / Kara S. Hood / Eugenia Mileykovskaya / William R. Miller / Truc T. Tran

    Frontiers in Molecular Biosciences, Vol

    A review

    2022  Volume 9

    Abstract: Lipids play a major role in bacterial cells. Foremost, lipids are the primary constituents of the cell membrane bilayer, providing structure and separating the cell from the surrounding environment. This makes the lipid bilayer a prime target for ... ...

    Abstract Lipids play a major role in bacterial cells. Foremost, lipids are the primary constituents of the cell membrane bilayer, providing structure and separating the cell from the surrounding environment. This makes the lipid bilayer a prime target for antimicrobial peptides and membrane-acting antibiotics such as daptomycin. In response, bacteria have evolved mechanisms by which the membrane can be adapted to resist attack by these antimicrobial compounds. In this review, we focus on the membrane phospholipid changes associated with daptomycin resistance in enterococci, Staphylococcus aureus, and the Viridans group streptococci.
    Keywords daptomycin ; resistance ; phospholipids ; enterococci ; Staphylococcus aureus ; streptococci ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-11-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex.

    Hryc, Corey F / Mallampalli, Venkata K P S / Bovshik, Evgeniy I / Azinas, Stavros / Fan, Guizhen / Serysheva, Irina I / Sparagna, Genevieve C / Baker, Matthew L / Mileykovskaya, Eugenia / Dowhan, William

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 2783

    Abstract: Cardiolipin is a hallmark phospholipid of mitochondrial membranes. Despite established significance of cardiolipin in supporting respiratory supercomplex organization, a mechanistic understanding of this lipid-protein interaction is still lacking. To ... ...

    Abstract Cardiolipin is a hallmark phospholipid of mitochondrial membranes. Despite established significance of cardiolipin in supporting respiratory supercomplex organization, a mechanistic understanding of this lipid-protein interaction is still lacking. To address the essential role of cardiolipin in supercomplex organization, we report cryo-EM structures of a wild type supercomplex (IV
    MeSH term(s) Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Cardiolipins/metabolism ; Phosphatidylglycerols/metabolism ; Phospholipids/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Cardiolipins ; Phosphatidylglycerols ; Phospholipids ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2023-05-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-38441-5
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  4. Article: Molecular Basis of Cell Membrane Adaptation in Daptomycin-Resistant

    Nguyen, April H / Tran, Truc T / Panesso, Diana / Hood, Kara / Polamraju, Vinathi / Zhang, Rutan / Khan, Ayesha / Miller, William R / Mileykovskaya, Eugenia / Shamoo, Yousif / Xu, Libin / Vitrac, Heidi / Arias, Cesar A

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Daptomycin is a last-resort lipopeptide antibiotic that disrupts cell membrane (CM) and peptidoglycan homeostasis. Enterococcus faecalis has developed a sophisticated mechanism to avoid daptomycin killing by re-distributing CM anionic phospholipids away ... ...

    Abstract Daptomycin is a last-resort lipopeptide antibiotic that disrupts cell membrane (CM) and peptidoglycan homeostasis. Enterococcus faecalis has developed a sophisticated mechanism to avoid daptomycin killing by re-distributing CM anionic phospholipids away from the septum. The CM changes are orchestrated by a three-component regulatory system, designated LiaFSR, with a possible contribution of cardiolipin synthase (Cls). However, the mechanism by which LiaFSR controls the CM response and the role of Cls are unknown. Here, we show that cardiolipin synthase activity is essential for anionic phospholipid redistribution and daptomycin resistance since deletion of the two genes (
    Language English
    Publishing date 2023-08-02
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.08.02.551704
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  5. Article: Subcellular localization of Escherichia coli osmosensory transporter ProP: focus on cardiolipin membrane domains.

    Mileykovskaya, Eugenia

    Molecular microbiology

    2007  Volume 64, Issue 6, Page(s) 1419–1422

    Abstract: The role for specific lipids in the spatial distribution of the membrane proteins and formation of the lipid-protein membrane domains is an emerging theme in the studies of the supramolecular organization of the bacterial cell. A combination of the lipid ...

    Abstract The role for specific lipids in the spatial distribution of the membrane proteins and formation of the lipid-protein membrane domains is an emerging theme in the studies of the supramolecular organization of the bacterial cell. A combination of the lipid and protein visualization techniques with manipulation of the cell lipid composition provides a useful tool for these studies. This MicroCommentary reviews the first experimental example demonstrating an involvement of the phospholipid cardiolipin in recruitment of a membrane protein (specifically H(+)-osmoprotectant symporter ProP) to the Escherichia coli cell poles. The properties of cardiolipin domains employed in creating a specific environment for structural organization and function of membrane protein complexes are also discussed.
    MeSH term(s) Cardiolipins/metabolism ; Cell Membrane/metabolism ; Cell Polarity ; Escherichia coli/metabolism ; Escherichia coli/ultrastructure ; Escherichia coli Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Microscopy, Fluorescence ; Symporters/metabolism
    Chemical Substances Cardiolipins ; Escherichia coli Proteins ; ProP protein, E coli ; Symporters
    Language English
    Publishing date 2007-06
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/j.1365-2958.2007.05766.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2502: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: Cardiolipin-dependent formation of mitochondrial respiratory supercomplexes.

    Mileykovskaya, Eugenia / Dowhan, William

    Chemistry and physics of lipids

    2013  Volume 179, Page(s) 42–48

    Abstract: The organization of individual respiratory Complexes I, III, and IV (mammalian cells) or III and IV (yeast) of the mitochondria into higher order supercomplexes (SCs) is generally accepted. However, the factors that regulate SC formation and the ... ...

    Abstract The organization of individual respiratory Complexes I, III, and IV (mammalian cells) or III and IV (yeast) of the mitochondria into higher order supercomplexes (SCs) is generally accepted. However, the factors that regulate SC formation and the functional significance of SCs are not well understood. The mitochondrial signature phospholipid cardiolipin (CL) plays a central role in formation and stability of respiratory SCs from yeast to man. Studies in yeast mutants in which the CL level can be regulated displayed a direct correlation between CL levels and SC formation. Disease states in which CL levels are reduced also show defects in SC formation. Three-dimensional density maps of yeast and bovine SCs by electron cryo-microscopy show gaps between the transmembrane-localized interfaces of individual complexes consistent with the large excess of CL in SCs over that integrated into the structure of individual respiratory complexes. Finally, the yeast SC composed of Complex III and two Complexes IV was reconstituted in liposomes from purified individual complexes containing integrated CLs. Reconstitution was wholly dependent on inclusion of additional CL in the liposomes. Therefore, non-integral CL molecules play an important role in SC formation and may be involved in regulation of SC stability under metabolic conditions where CL levels fluctuate.
    MeSH term(s) Animals ; Cardiolipins/biosynthesis ; Cardiolipins/chemistry ; Cardiolipins/metabolism ; Computer Simulation ; Electron Transport Chain Complex Proteins/chemistry ; Electron Transport Chain Complex Proteins/metabolism ; Humans ; Mitochondria/metabolism
    Chemical Substances Cardiolipins ; Electron Transport Chain Complex Proteins
    Language English
    Publishing date 2013-11-09
    Publishing country Ireland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 213869-4
    ISSN 1873-2941 ; 0009-3084
    ISSN (online) 1873-2941
    ISSN 0009-3084
    DOI 10.1016/j.chemphyslip.2013.10.012
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 804: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article: Cardiolipin-dependent formation of mitochondrial respiratory supercomplexes

    Mileykovskaya, Eugenia / William Dowhan

    Chemistry and physics of lipids. 2014 Apr., v. 179

    2014  

    Abstract: The organization of individual respiratory Complexes I, III, and IV (mammalian cells) or III and IV (yeast) of the mitochondria into higher order supercomplexes (SCs) is generally accepted. However, the factors that regulate SC formation and the ... ...

    Abstract The organization of individual respiratory Complexes I, III, and IV (mammalian cells) or III and IV (yeast) of the mitochondria into higher order supercomplexes (SCs) is generally accepted. However, the factors that regulate SC formation and the functional significance of SCs are not well understood. The mitochondrial signature phospholipid cardiolipin (CL) plays a central role in formation and stability of respiratory SCs from yeast to man. Studies in yeast mutants in which the CL level can be regulated displayed a direct correlation between CL levels and SC formation. Disease states in which CL levels are reduced also show defects in SC formation. Three-dimensional density maps of yeast and bovine SCs by electron cryo-microscopy show gaps between the transmembrane-localized interfaces of individual complexes consistent with the large excess of CL in SCs over that integrated into the structure of individual respiratory complexes. Finally, the yeast SC composed of Complex III and two Complexes IV was reconstituted in liposomes from purified individual complexes containing integrated CLs. Reconstitution was wholly dependent on inclusion of additional CL in the liposomes. Therefore, non-integral CL molecules play an important role in SC formation and may be involved in regulation of SC stability under metabolic conditions where CL levels fluctuate.
    Keywords cattle ; cryo-electron microscopy ; mitochondria ; mutants ; phospholipids ; yeasts
    Language English
    Dates of publication 2014-04
    Size p. 42-48.
    Publishing place Elsevier Ireland Ltd
    Document type Article
    ZDB-ID 213869-4
    ISSN 1873-2941 ; 0009-3084
    ISSN (online) 1873-2941
    ISSN 0009-3084
    DOI 10.1016/j.chemphyslip.2013.10.012
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 804: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  8. Article ; Online: Cardiolipin Synthesis in Skeletal Muscle Is Rhythmic and Modifiable by Age and Diet.

    Nohara, Kazunari / Kim, Eunju / Wirianto, Marvin / Mileykovskaya, Eugenia / Dowhan, William / Chen, Zheng / Yoo, Seung-Hee

    Oxidative medicine and cellular longevity

    2020  Volume 2020, Page(s) 5304768

    Abstract: Circadian clocks regulate metabolic processes in a tissue-specific manner, which deteriorates during aging. Skeletal muscle is the largest metabolic organ in our body, and our previous studies highlight a key role of circadian regulation of skeletal ... ...

    Abstract Circadian clocks regulate metabolic processes in a tissue-specific manner, which deteriorates during aging. Skeletal muscle is the largest metabolic organ in our body, and our previous studies highlight a key role of circadian regulation of skeletal muscle mitochondria in healthy aging. However, a possible circadian regulation of cardiolipin (CL), the signature lipid class in the mitochondrial inner membrane, remains largely unclear. Here, we show that CL levels oscillate during the diurnal cycle in C2C12 myotubes. Disruption of the
    MeSH term(s) Aging/metabolism ; Animals ; Cardiolipins/biosynthesis ; Cardiolipins/genetics ; Cell Line ; Circadian Clocks/drug effects ; Circadian Clocks/genetics ; Circadian Rhythm/drug effects ; Circadian Rhythm/genetics ; Diet ; Flavones/pharmacology ; Gene Expression Regulation/drug effects ; Male ; Mice, Inbred C57BL ; Muscle Fibers, Skeletal/drug effects ; Muscle Fibers, Skeletal/metabolism ; Muscle, Skeletal/metabolism ; Nuclear Receptor Subfamily 1, Group F, Member 1/metabolism
    Chemical Substances Cardiolipins ; Flavones ; Nuclear Receptor Subfamily 1, Group F, Member 1 ; nobiletin (D65ILJ7WLY)
    Language English
    Publishing date 2020-06-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2455981-7
    ISSN 1942-0994 ; 1942-0994
    ISSN (online) 1942-0994
    ISSN 1942-0994
    DOI 10.1155/2020/5304768
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Subcellular localization of Escherichia coli osmosensory transporter ProP: focus on cardiolipin membrane domains

    Mileykovskaya, Eugenia

    Molecular microbiology. 2007 June, v. 64, no. 6

    2007  

    Abstract: The role for specific lipids in the spatial distribution of the membrane proteins and formation of the lipid-protein membrane domains is an emerging theme in the studies of the supramolecular organization of the bacterial cell. A combination of the lipid ...

    Abstract The role for specific lipids in the spatial distribution of the membrane proteins and formation of the lipid-protein membrane domains is an emerging theme in the studies of the supramolecular organization of the bacterial cell. A combination of the lipid and protein visualization techniques with manipulation of the cell lipid composition provides a useful tool for these studies. This MicroCommentary reviews the first experimental example demonstrating an involvement of the phospholipid cardiolipin in recruitment of a membrane protein (specifically H⁺-osmoprotectant symporter ProP) to the Escherichia coli cell poles. The properties of cardiolipin domains employed in creating a specific environment for structural organization and function of membrane protein complexes are also discussed.
    Language English
    Dates of publication 2007-06
    Size p. 1419-1422.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/j.1365-2958.2007.05766.x
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2005/703: Show issues

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  10. Article: The membrane: transertion as an organizing principle in membrane heterogeneity.

    Matsumoto, Kouji / Hara, Hiroshi / Fishov, Itzhak / Mileykovskaya, Eugenia / Norris, Vic

    Frontiers in microbiology

    2015  Volume 6, Page(s) 572

    Abstract: The bacterial membrane exhibits a significantly heterogeneous distribution of lipids and proteins. This heterogeneity results mainly from lipid-lipid, protein-protein, and lipid-protein associations which are orchestrated by the coupled transcription, ... ...

    Abstract The bacterial membrane exhibits a significantly heterogeneous distribution of lipids and proteins. This heterogeneity results mainly from lipid-lipid, protein-protein, and lipid-protein associations which are orchestrated by the coupled transcription, translation and insertion of nascent proteins into and through membrane (transertion). Transertion is central not only to the individual assembly and disassembly of large physically linked groups of macromolecules (alias hyperstructures) but also to the interactions between these hyperstructures. We review here these interactions in the context of the processes in Bacillus subtilis and Escherichia coli of nutrient sensing, membrane synthesis, cytoskeletal dynamics, DNA replication, chromosome segregation, and cell division.
    Language English
    Publishing date 2015-06-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2015.00572
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