Evidence for solvent-induced conformational changes of the soluble Dunaliella chloroplast coupling factor 1 (CF1).
The ATPase activity of the chloroplast coupling factor 1 (CF1) isolated from the green alga Dunaliella is completely latent. A brief heat treatment irreversibly induces a Ca2+-dependent activity. The Ca2+-dependent ATPase activity can be reversibly inhibited by ethanol, which changes the divalent cation dependency from Ca2+ to Mg2+. Both the Ca2+-dependent and Mg2+-dependent ATPase activities of heat-treated Dunaliella CF1 are inhibited by monospecific antisera directed against Chlamydomonas reinhardi CF1. However, when assayed under identical conditions, the Ca2+-dependent ATPase activity is significantly more sensitive to inhibition by the antisera than is the Mg2+-dependent activity. These data are interpreted as indicating that soluble Dunaliella CF1 can exist in a variety of conformations, at least one of which catalyzes a Ca2+-dependent ATPase and two or more of which catalyze an Mg2+-dependent ATPase.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002696:Chlamydomonas / Q000201:enzymology; D000460:Chlorophyta / Q000201:enzymology*; D000431:Ethanol / Q000494:pharmacology; D006358:Hot Temperature; D007106:Immune Sera; D011487:Protein Conformation / Q000187:drug effects; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D007106:Immune Sera; D000431:Ethanol; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D006180:Proton-Translocating ATPases; D000252:Calcium-Transporting ATPases