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Full-Text Articles in Biochemistry
The Proton-Translocating A Subunit Of F0f1-Atp Synthase Is Allocated Asymmetrically To The Peripheral Stalk., Monika G Düser, Yumin Bi, Nawid Zarrabi, Stanley D Dunn, Michael Börsch
The Proton-Translocating A Subunit Of F0f1-Atp Synthase Is Allocated Asymmetrically To The Peripheral Stalk., Monika G Düser, Yumin Bi, Nawid Zarrabi, Stanley D Dunn, Michael Börsch
Biochemistry Publications
The position of the a subunit of the membrane-integral F0 sector of Escherichia coli ATP synthase was investigated by single molecule fluorescence resonance energy transfer studies utilizing a fusion of enhanced green fluorescent protein to the C terminus of the a subunit and fluorescent labels attached to specific positions of the epsilon or gamma subunits. Three fluorescence resonance energy transfer levels were observed during rotation driven by ATP hydrolysis corresponding to the three resting positions of the rotor subunits, gamma or epsilon, relative to the a subunit of the stator. Comparison of these positions of the rotor sites with those …
Probing The Functional Tolerance Of The B Subunit Of Escherichia Coli Atp Synthase For Sequence Manipulation Through A Chimera Approach., Yumin Bi, Joel C Watts, Pamela Krauss Bamford, Lee-Ann K Briere, Stanley D Dunn
Probing The Functional Tolerance Of The B Subunit Of Escherichia Coli Atp Synthase For Sequence Manipulation Through A Chimera Approach., Yumin Bi, Joel C Watts, Pamela Krauss Bamford, Lee-Ann K Briere, Stanley D Dunn
Biochemistry Publications
A dimer of 156-residue b subunits forms the peripheral stator stalk of eubacterial ATP synthase. Dimerization is mediated by a sequence with an unusual 11-residue (hendecad) repeat pattern, implying a right-handed coiled coil structure. We investigated the potential for producing functional chimeras in the b subunit of Escherichia coli ATP synthase by replacing parts of its sequence with corresponding regions of the b subunits from other eubacteria, sequences from other polypeptides having similar hendecad patterns, and sequences forming left-handed coiled coils. Replacement of positions 55-110 with corresponding sequences from Bacillus subtilis and Thermotoga maritima b subunits resulted in fully functional …