PortalPublikationenBiogenesis of MalF and the MalFGK(2) maltose transport compl...

Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC

Standard

Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC. / Wagner, Samuel; Pop, Ovidiu Ioan; Pop, Ovidio; Haan, Gert-Jan; Baars, Louise; Koningstein, Gregory; Klepsch, Mirjam M; Genevaux, Pierre; Luirink, Joen; de Gier, Jan-Willem.

in: J BIOL CHEM, Jahrgang 283, Nr. 26, 27.06.2008, S. 17881-90.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Wagner, S, Pop, OI, Pop, O, Haan, G-J, Baars, L, Koningstein, G, Klepsch, MM, Genevaux, P, Luirink, J & de Gier, J-W 2008, 'Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC', J BIOL CHEM, Jg. 283, Nr. 26, S. 17881-90. https://doi.org/10.1074/jbc.M801481200

APA

Wagner, S., Pop, O. I., Pop, O., Haan, G-J., Baars, L., Koningstein, G., Klepsch, M. M., Genevaux, P., Luirink, J., & de Gier, J-W. (2008). Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC. J BIOL CHEM, 283(26), 17881-90. https://doi.org/10.1074/jbc.M801481200

Vancouver

Wagner S, Pop OI, Pop O, Haan G-J, Baars L, Koningstein G et al. Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC. J BIOL CHEM. 2008 Jun 27;283(26):17881-90. https://doi.org/10.1074/jbc.M801481200

Bibtex

@article{de1ddcbcc9b44e5baa573668673b7ffe,
title = "Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC",
abstract = "The polytopic inner membrane protein MalF is a constituent of the MalFGK(2) maltose transport complex in Escherichia coli. We have studied the biogenesis of MalF using a combination of in vivo and in vitro approaches. MalF is targeted via the SRP pathway to the Sec/YidC insertion site. Despite close proximity of nascent MalF to YidC during insertion, YidC is not required for the insertion of MalF into the membrane. However, YidC is required for the stability of MalF and the formation of the MalFGK(2) maltose transport complex. Our data indicate that YidC supports the folding of MalF into a stable conformation before it is incorporated into the maltose transport complex.",
keywords = "ATP-Binding Cassette Transporters, Biological Transport, Cell Membrane, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Maltose, Membrane Transport Proteins, Models, Biological, Monosaccharide Transport Proteins, Plasmids, Protein Binding, Protein Conformation, Protein Folding, Journal Article, Research Support, Non-U.S. Gov't",
author = "Samuel Wagner and Pop, {Ovidiu Ioan} and Ovidio Pop and Gert-Jan Haan and Louise Baars and Gregory Koningstein and Klepsch, {Mirjam M} and Pierre Genevaux and Joen Luirink and {de Gier}, Jan-Willem",
year = "2008",
month = jun,
day = "27",
doi = "10.1074/jbc.M801481200",
language = "English",
volume = "283",
pages = "17881--90",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "26",

}

RIS

TY - JOUR

T1 - Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC

AU - Wagner, Samuel

AU - Pop, Ovidiu Ioan

AU - Pop, Ovidio

AU - Haan, Gert-Jan

AU - Baars, Louise

AU - Koningstein, Gregory

AU - Klepsch, Mirjam M

AU - Genevaux, Pierre

AU - Luirink, Joen

AU - de Gier, Jan-Willem

PY - 2008/6/27

Y1 - 2008/6/27

N2 - The polytopic inner membrane protein MalF is a constituent of the MalFGK(2) maltose transport complex in Escherichia coli. We have studied the biogenesis of MalF using a combination of in vivo and in vitro approaches. MalF is targeted via the SRP pathway to the Sec/YidC insertion site. Despite close proximity of nascent MalF to YidC during insertion, YidC is not required for the insertion of MalF into the membrane. However, YidC is required for the stability of MalF and the formation of the MalFGK(2) maltose transport complex. Our data indicate that YidC supports the folding of MalF into a stable conformation before it is incorporated into the maltose transport complex.

AB - The polytopic inner membrane protein MalF is a constituent of the MalFGK(2) maltose transport complex in Escherichia coli. We have studied the biogenesis of MalF using a combination of in vivo and in vitro approaches. MalF is targeted via the SRP pathway to the Sec/YidC insertion site. Despite close proximity of nascent MalF to YidC during insertion, YidC is not required for the insertion of MalF into the membrane. However, YidC is required for the stability of MalF and the formation of the MalFGK(2) maltose transport complex. Our data indicate that YidC supports the folding of MalF into a stable conformation before it is incorporated into the maltose transport complex.

KW - ATP-Binding Cassette Transporters

KW - Biological Transport

KW - Cell Membrane

KW - Escherichia coli

KW - Escherichia coli Proteins

KW - Gene Expression Regulation, Bacterial

KW - Maltose

KW - Membrane Transport Proteins

KW - Models, Biological

KW - Monosaccharide Transport Proteins

KW - Plasmids

KW - Protein Binding

KW - Protein Conformation

KW - Protein Folding

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1074/jbc.M801481200

DO - 10.1074/jbc.M801481200

M3 - SCORING: Journal article

C2 - 18456666

VL - 283

SP - 17881

EP - 17890

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 26

ER -