TY - JOUR
T1 - Catalytic activity of MsbA reconstituted in nanodisc particles is modulated by remote interactions with the bilayer
AU - Kawai, Takeaki
AU - Caaveiro, Jose M.M.
AU - Abe, Ryota
AU - Katagiri, Toyomasa
AU - Tsumoto, Kouhei
N1 - Funding Information:
We thank Dr. Mitani for assistance with SPR measurements, and Dr. Tadakuma for valuable suggestions. This work was supported in part by a Grant-in-Aid for General Researches (to K.T.) from the Japan Society for the Promotion of Science.
PY - 2011/11/16
Y1 - 2011/11/16
N2 - ATP-binding cassette (ABC) transporters couple hydrolysis of ATP with vectorial transport across the cell membrane. We have reconstituted ABC transporter MsbA in nanodiscs of various sizes and lipid compositions to test whether ATPase activity is modulated by the properties of the bilayer. ATP hydrolysis rates, Michaelis-Menten parameters, and dissociation constants of substrate analog ATP-γ-S demonstrated that physicochemical properties of the bilayer modulated binding and ATPase activity. This is remarkable when considering that the catalytic unit is located ∼50 from the transmembrane region. Our results validated the use of nanodiscs as an effective tool to reconstitute MsbA in an active catalytic state, and highlighted the close relationship between otherwise distant transmembrane and ATPase modules.
AB - ATP-binding cassette (ABC) transporters couple hydrolysis of ATP with vectorial transport across the cell membrane. We have reconstituted ABC transporter MsbA in nanodiscs of various sizes and lipid compositions to test whether ATPase activity is modulated by the properties of the bilayer. ATP hydrolysis rates, Michaelis-Menten parameters, and dissociation constants of substrate analog ATP-γ-S demonstrated that physicochemical properties of the bilayer modulated binding and ATPase activity. This is remarkable when considering that the catalytic unit is located ∼50 from the transmembrane region. Our results validated the use of nanodiscs as an effective tool to reconstitute MsbA in an active catalytic state, and highlighted the close relationship between otherwise distant transmembrane and ATPase modules.
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U2 - 10.1016/j.febslet.2011.10.015
DO - 10.1016/j.febslet.2011.10.015
M3 - Article
C2 - 22020218
AN - SCOPUS:80855144109
SN - 0014-5793
VL - 585
SP - 3533
EP - 3537
JO - FEBS Letters
JF - FEBS Letters
IS - 22
ER -