[The role of ATPase subunits from E. coli in hydrogen-potassium exchange].
A hypothesis was developed that in membranes of glycolysing bacteria functioned supercomplexes (F1 X F0-TrkA) and (F0-TrkA) which operated as H+-K+-pump exchanging 2H+ for one K+ and as H+-K+-antiport respectively. The mutants with defects in alpha, beta and gamma subunits of ATPase F1 manifested the alteration only in the work of (F1 X F0-TrkA). Defect in epsilon subunit of F1 broke the regulation of pump operation on the part of a cell turgor. In mutants with defects in F0 the changes in both supercomplexes were observed. The only mutation in unc- cluster producing the complete blocking of both systems operation was related to a defect in h3-subunit of F0 which was the dicyclohexylcarbodiimide-sensitive and apparently "gate" component of F0.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D006859:Hydrogen / Q000378:metabolism*; D007474:Ion Exchange; D007527:Isoenzymes / Q000378:metabolism*; D009154:Mutation; D011188:Potassium / Q000378:metabolism*
D007527:Isoenzymes; D006859:Hydrogen; D000251:Adenosine Triphosphatases; D011188:Potassium
Rol' otdel'nykh sub''edinits ATFazy E. coli v vodorodno-kalievom obmene.