ATP Synthases With Novel Rotor Subunits: New Insights into Structure,Function and Evolution of ATPases |
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Authors: | Email author" target="_blank">Volker?MüllerEmail author Astrid?Lingl Kim?Lewalter Michael?Fritz |
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Institution: | (1) Molecular Microbiology & Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University, Frankfurt, Germany |
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Abstract: | ATPases with unusual membrane-embedded rotor subunits were found in both F1F0 and A1A0 ATP synthases. The rotor subunit c of A1A0 ATPases is, in most cases, similar to subunit c from F0. Surprisingly, multiplied c subunits with four, six, or even 26 transmembrane spans have been found in some archaea and these multiplication events were
sometimes accompanied by loss of the ion-translocating group. Nevertheless, these enzymes are still active as ATP synthases.
A duplicated c subunit with only one ion-translocating group was found along with “normal” F0 c subunits in the Na+ F1F0 ATP synthase of the bacterium Acetobacterium woodii. These extraordinary features and exceptional structural and functional variability in the rotor of ATP synthases may have
arisen as an adaptation to different cellular needs and the extreme physicochemical conditions in the early history of life. |
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Keywords: | Archaea A1A0 ATPase Acetobacterium Na+ F1F0 ATPase rotor diversity ion specificity |
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