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  1. Article ; Online: Membrane translocation of folded proteins.

    Pei, Dehua / Dalbey, Ross E

    The Journal of biological chemistry

    2022  Volume 298, Issue 7, Page(s) 102107

    Abstract: ... in eukaryotes, and the cytosolic entry of proteins (e.g., bacterial toxins) and viruses into eukaryotes. We also ...

    Abstract An ever-increasing number of proteins have been shown to translocate across various membranes of bacterial as well as eukaryotic cells in their folded states as a part of physiological and/or pathophysiological processes. Herein, we provide an overview of the systems/processes that are established or likely to involve the membrane translocation of folded proteins, such as protein export by the twin-arginine translocation system in bacteria and chloroplasts, unconventional protein secretion and protein import into the peroxisome in eukaryotes, and the cytosolic entry of proteins (e.g., bacterial toxins) and viruses into eukaryotes. We also discuss the various mechanistic models that have previously been proposed for the membrane translocation of folded proteins including pore/channel formation, local membrane disruption, membrane thinning, and transport by membrane vesicles. Finally, we introduce a newly discovered vesicular transport mechanism, vesicle budding and collapse, and present evidence that vesicle budding and collapse may represent a unifying mechanism that drives some (and potentially all) of folded protein translocation processes.
    MeSH term(s) Bacteria/metabolism ; Bacterial Proteins/metabolism ; Eukaryota/metabolism ; Membrane Transport Proteins/metabolism ; Peroxisomes/metabolism ; Protein Folding ; Protein Sorting Signals ; Protein Transport ; Twin-Arginine-Translocation System/metabolism
    Chemical Substances Bacterial Proteins ; Membrane Transport Proteins ; Protein Sorting Signals ; Twin-Arginine-Translocation System
    Language English
    Publishing date 2022-06-04
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2022.102107
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Book: Protein targeting, transport & translocation

    Dalbey, Ross E.

    2002  

    Author's details ed. by Ross E. Dalbey
    Keywords Proteintransport ; Membrantransport ; Zielerkennung ; Proteine
    Subject Zielerfassung ; Eiweiss ; Protein ; Proteine ; Proteintranslokation ; Biomembran
    Language English
    Size XIV, 424 S. : Ill.
    Publisher Academic Press
    Publishing place Amsterdam u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT013326564
    ISBN 0-12-200731-X ; 978-0-12-200731-6
    Database Catalogue ZB MED Medicine, Health

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    2002 A 2015 order for loan Magazin

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  3. Article: Bacterial Signal Peptides- Navigating the Journey of Proteins.

    Kaushik, Sharbani / He, Haoze / Dalbey, Ross E

    Frontiers in physiology

    2022  Volume 13, Page(s) 933153

    Abstract: In 1971, Blobel proposed the first statement of the Signal Hypothesis which suggested that proteins have amino-terminal sequences that dictate their export and localization in the cell. A cytosolic binding factor was predicted, and later the protein ... ...

    Abstract In 1971, Blobel proposed the first statement of the Signal Hypothesis which suggested that proteins have amino-terminal sequences that dictate their export and localization in the cell. A cytosolic binding factor was predicted, and later the protein conducting channel was discovered that was proposed in 1975 to align with the large ribosomal tunnel. The 1975 Signal Hypothesis also predicted that proteins targeted to different intracellular membranes would possess distinct signals and integral membrane proteins contained uncleaved signal sequences which initiate translocation of the polypeptide chain. This review summarizes the central role that the signal peptides play as address codes for proteins, their decisive role as targeting factors for delivery to the membrane and their function to activate the translocation machinery for export and membrane protein insertion. After shedding light on the navigation of proteins, the importance of removal of signal peptide and their degradation are addressed. Furthermore, the emerging work on signal peptidases as novel targets for antibiotic development is described.
    Language English
    Publishing date 2022-07-26
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2564217-0
    ISSN 1664-042X
    ISSN 1664-042X
    DOI 10.3389/fphys.2022.933153
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  4. Article ; Online: YidC as a potential antibiotic target.

    Dalbey, Ross E / Kaushik, Sharbani / Kuhn, Andreas

    Biochimica et biophysica acta. Molecular cell research

    2022  Volume 1870, Issue 2, Page(s) 119403

    Abstract: The membrane insertase YidC, is an essential bacterial component and functions in the folding and insertion of many membrane proteins during their biogenesis. It is a multispanning protein in the inner (cytoplasmic) membrane of Escherichia coli that ... ...

    Abstract The membrane insertase YidC, is an essential bacterial component and functions in the folding and insertion of many membrane proteins during their biogenesis. It is a multispanning protein in the inner (cytoplasmic) membrane of Escherichia coli that binds its substrates in the "greasy slide" through hydrophobic interaction. The hydrophilic part of the substrate transiently localizes in the groove of YidC before it is translocated into the periplasm. The groove, which is flanked by the greasy slide, is within the center of the membrane, and provides a promising target for inhibitors that would block the insertase function of YidC. In addition, since the greasy slide is available for the binding of various substrates, it could also provide a binding site for inhibitory molecules. In this review we discuss in detail the structure and the mechanism of how YidC interacts not only with its substrates, but also with its partner proteins, the SecYEG translocase and the SRP signal recognition particle. Insight into the substrate binding to the YidC catalytic groove is presented. We wind up the review with the idea that the hydrophilic groove would be a potential site for drug binding and the feasibility of YidC-targeted drug development.
    MeSH term(s) Membrane Transport Proteins/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Membrane Proteins/metabolism ; Cell Membrane/metabolism
    Chemical Substances Membrane Transport Proteins ; Escherichia coli Proteins ; Membrane Proteins ; YIDC protein, E coli
    Language English
    Publishing date 2022-11-23
    Publishing country Netherlands
    Document type Review ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2022.119403
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  5. Article ; Online: The Conserved Role of YidC in Membrane Protein Biogenesis.

    Shanmugam, Sri Karthika / Dalbey, Ross E

    Microbiology spectrum

    2019  Volume 7, Issue 1

    Abstract: YidC insertase plays a pivotal role in the membrane integration, folding, and assembly of a number of proteins, including energy-transducing respiratory complexes, both autonomously and in concert with the SecYEG channel in bacteria. The YidC family of ... ...

    Abstract YidC insertase plays a pivotal role in the membrane integration, folding, and assembly of a number of proteins, including energy-transducing respiratory complexes, both autonomously and in concert with the SecYEG channel in bacteria. The YidC family of proteins is widely conserved in all domains of life, with new members recently identified in the eukaryotic endoplasmic reticulum membrane. Bacterial and organellar members share the conserved 5-transmembrane core, which forms a unique hydrophilic cavity in the inner leaflet of the bilayer accessible from the cytoplasm and the lipid phase. In this chapter, we discuss the YidC family of proteins, focusing on its mechanism of substrate insertion independently and in association with the Sec translocon.
    MeSH term(s) Bacillus subtilis/metabolism ; Biological Transport/physiology ; Cell Membrane/metabolism ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers/metabolism ; Membrane Transport Proteins/metabolism ; SEC Translocation Channels/physiology
    Chemical Substances Escherichia coli Proteins ; Lipid Bilayers ; Membrane Transport Proteins ; SEC Translocation Channels ; YIDC protein, E coli
    Language English
    Publishing date 2019-02-11
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 2165-0497
    ISSN (online) 2165-0497
    DOI 10.1128/microbiolspec.PSIB-0014-2018
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  6. Book: Protein export and membrane biogenesis

    Dalbey, Ross E.

    (Advances in cell and molecular biology of membranes ; 4)

    1995  

    Author's details ed.: Ross E. Dalbey
    Series title Advances in cell and molecular biology of membranes ; 4
    Advances in cell and molecular biology of membranes and organelles
    Collection Advances in cell and molecular biology of membranes and organelles
    Keywords Cell Membrane / physiology ; Bacterial Proteins / physiology ; Bacterial Proteins / metabolism ; Biological Transport / physiology ; Proteine ; Translokation ; Biomembran ; Entwicklung ; Biogenese
    Subject Entstehung ; Biologische Membran ; Einheitsmembran ; Zelle ; Zellmembran ; Chromosomentranslokation ; Chromosomale Translokation ; Eiweiss ; Protein ; Ursprung ; Entwicklungsstadium
    Language English
    Size XIV, 276 S. : Ill., graph. Darst.
    Publisher JAI Press
    Publishing place Greenwich, Conn. u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT006806067
    ISBN 1-55938-924-9 ; 978-1-55938-924-2
    Database Catalogue ZB MED Medicine, Health

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    Se 1360 -4- verfügbar in Königswinter Königswinter

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  7. Article: Oxa1 Superfamily: New Members Found in the ER.

    Chen, Yuanyuan / Dalbey, Ross E

    Trends in biochemical sciences

    2018  Volume 43, Issue 3, Page(s) 151–153

    Abstract: Oxa1/Alb3/YidC family members promote the insertion of proteins into the mitochondrial inner membrane, the chloroplast thylakoid membrane, and the bacterial plasma membrane. Remarkably, two recent studies identify new Oxa1 homologs that reside in the ... ...

    Abstract Oxa1/Alb3/YidC family members promote the insertion of proteins into the mitochondrial inner membrane, the chloroplast thylakoid membrane, and the bacterial plasma membrane. Remarkably, two recent studies identify new Oxa1 homologs that reside in the endoplasmic reticulum (ER) and function in ER membrane protein biogenesis.
    MeSH term(s) Electron Transport Complex IV ; Endoplasmic Reticulum ; Escherichia coli Proteins ; Membrane Transport Proteins ; Mitochondrial Membranes ; Mitochondrial Proteins ; Nuclear Proteins
    Chemical Substances Escherichia coli Proteins ; Membrane Transport Proteins ; Mitochondrial Proteins ; Nuclear Proteins ; Electron Transport Complex IV (EC 1.9.3.1)
    Language English
    Publishing date 2018-01-12
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Comment
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2017.12.005
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  8. Article ; Online: Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases.

    Xie, Kun / Dalbey, Ross E

    Nature reviews. Microbiology

    2017  Volume 16, Issue 2, Page(s) 120

    Abstract: This corrects the article DOI: 10.1038/nrmicro3595. ...

    Abstract This corrects the article DOI: 10.1038/nrmicro3595.
    Language English
    Publishing date 2017-12-11
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2139054-X
    ISSN 1740-1534 ; 1740-1526
    ISSN (online) 1740-1534
    ISSN 1740-1526
    DOI 10.1038/nrmicro.2017.160
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  9. Article ; Online: The Principles of Protein Targeting and Transport Across Cell Membranes.

    Chen, Yuanyuan / Shanmugam, Sri Karthika / Dalbey, Ross E

    The protein journal

    2019  Volume 38, Issue 3, Page(s) 236–248

    Abstract: The past several decades have witnessed tremendous growth in the protein targeting, transport and translocation field. Major advances were made during this time period. Now the molecular details of the targeting factors, receptors and the membrane ... ...

    Abstract The past several decades have witnessed tremendous growth in the protein targeting, transport and translocation field. Major advances were made during this time period. Now the molecular details of the targeting factors, receptors and the membrane channels that were envisioned in Blobel's Signal Hypothesis in the 1970s have been revealed by powerful structural methods. It is evident that there is a myriad of cytosolic and membrane associated systems that accurately sort and target newly synthesized proteins to their correct membrane translocases for membrane insertion or protein translocation. Here we will describe the common principles for protein transport in prokaryotes and eukaryotes.
    MeSH term(s) Escherichia coli/metabolism ; Molecular Chaperones/chemistry ; Molecular Chaperones/physiology ; Protein Sorting Signals ; Protein Translocation Systems/chemistry ; Protein Translocation Systems/physiology ; Protein Transport ; Proteins/metabolism ; SEC Translocation Channels/chemistry ; Yeasts/metabolism
    Chemical Substances Molecular Chaperones ; Protein Sorting Signals ; Protein Translocation Systems ; Proteins ; SEC Translocation Channels
    Language English
    Publishing date 2019-06-11
    Publishing country Netherlands
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2143071-8
    ISSN 1875-8355 ; 1572-3887
    ISSN (online) 1875-8355
    ISSN 1572-3887
    DOI 10.1007/s10930-019-09847-2
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  10. Article ; Online: Tracking the Stepwise Movement of a Membrane-inserting Protein In Vivo.

    He, Haoze / Kuhn, Andreas / Dalbey, Ross E

    Journal of molecular biology

    2019  Volume 432, Issue 2, Page(s) 484–496

    Abstract: ... We show that Pf3 is inserted as a helical hairpin, i.e., the prospective transmembrane segment moves along ...

    Abstract Proper membrane insertion is crucial for the structure and function of membrane proteins in all cells. The YidC insertase plays an essential role in this process, but the molecular mechanism of YidC-mediated insertion remains unknown. Here we track the stepwise movement of Pf3 coat through YidC by obtaining a series of translational arrested intermediates, and investigate them by thiol cross-linking. We show that Pf3 is inserted as a helical hairpin, i.e., the prospective transmembrane segment moves along the YidC greasy slide comprised of TM3 and TM5, whereas the N-terminal tail transiently folds back into the hydrophilic groove of YidC located in the inner leaflet of the membrane until it is translocated to the periplasm in a subsequent step involving the electrochemical membrane potential. In addition to providing virtual insights about how YidC inserts single-spanning membrane proteins, our study also demonstrates a valuable in vivo tracking method that can be applied to study more complicated substrates or other translocases.
    MeSH term(s) Cell Membrane/genetics ; Cell Membrane/ultrastructure ; Escherichia coli/genetics ; Escherichia coli/ultrastructure ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/ultrastructure ; Hydrophobic and Hydrophilic Interactions ; Membrane Proteins/genetics ; Membrane Proteins/ultrastructure ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/ultrastructure ; Mutation/genetics ; Periplasm/genetics ; Protein Biosynthesis ; Protein Transport/genetics ; Substrate Specificity
    Chemical Substances Escherichia coli Proteins ; Membrane Proteins ; Membrane Transport Proteins ; YIDC protein, E coli
    Language English
    Publishing date 2019-10-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2019.10.010
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