Transport of nutrients by a thermophilic bacterium--reconstruction of vesicles from crystalline ATPase or solubilized alanine carrier.
A strain of aerobic thermophilic bacteria was selected in order to purify highly stable membrane proteins and no reconstitute proteoliposomes capable of transporting nutrients from them. These proteins responsible for the transport could be divided into (1) proteins which supply energy to the transporting system, and (2) specific nutrient carriers driven by the energy. The former included a stable ATPase (TF1) and a lipoprotein TF0) which rendered TF1 sensitive to energy transfer inhibitors. The complex of TF0 anlysis of ATP. And one of the latter reported in this paper was alanine carrier protein which was driven by proton movement. TF1 was the first crystallized ATPase in biomembranes, and was reconstituted from its five different polypeptides, two of which were necessary for ATPase activity and four of which, for proton translocation. Purification of alanine carrier and reconstitution of proteoliposomes capable of alanine accumulation were also demonstrated.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000409:Alanine / Q000378:metabolism*; D001693:Biological Transport, Active; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D006088:Gram-Negative Aerobic Bacteria / Q000378:metabolism* / Q000648:ultrastructure; D006358:Hot Temperature; D006868:Hydrolysis; D008081:Liposomes / Q000378:metabolism; D014871:Water Microbiology
D008081:Liposomes; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; D004024:Dicyclohexylcarbodiimide; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D000409:Alanine