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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 …