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Interactions between subunits a and b in the rotary ATP synthase as determined by cross‐linking
Author(s) -
DeLeon-Rangel Jessica,
Ishmukhametov Robert R.,
Jiang Warren,
Fillingame Robert H.,
Vik Steven B.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.02.012
Subject(s) - periplasmic space , protein subunit , atp synthase gamma subunit , atp synthase , specificity factor , chemistry , biochemistry , biophysics , stereochemistry , biology , atp hydrolysis , enzyme , atpase , escherichia coli , rna dependent rna polymerase , polymerase , gene
The interaction of the membrane traversing stator subunits a and b of the rotary ATP synthase was probed by substitution of a single Cys into each subunit with subsequent Cu 2+ catalyzed cross‐linking. Extensive interaction between the transmembrane (TM) region of one b subunit and TM2 of subunit a was indicated by cross‐linking with 6 Cys pairs introduced into these regions. Additional disulfide cross‐linking was observed between the N‐terminus of subunit b and the periplasmic loop connecting TM4 and TM5 of subunit a . Finally, benzophenone‐4‐maleimide derivatized Cys in the 2–3 periplasmic loop of subunit a were shown to cross‐link with the periplasmic N‐terminal region of subunit b . These experiments help to define the juxtaposition of subunits b and a in the ATP synthase.
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