Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC
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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, Vol. 283, No. 26, 27.06.2008, p. 17881-90.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -